pathophysiology scripta

8/13/2019 pathophysiology scripta

http://slidepdf.com/reader/full/pathophysiology-scripta 1/233

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to environment with feelings, referred to as “psychosocial adaptation” which can lead to

neurotic and psychosomatic disorders when not present.

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1. Oxidation of bases and generation of DNA strand interruptions from reactive oxygen

species,

2. Alkylation of bases (usually methylation), such as formation of 7-methylguanine.

3. Hydrolysis of bases, such as deamination (hydrolysis reaction of cytosine into uracil,

releasing ammonia (an amine) in the process), H@NKLDGCBD>G of DNA (results in the

loss of a purine from the DNA backbone and occurs at a lower rate compared to

depurination with only 500 cytosine and thymine bases lost per cell per day in atypical), and depyrimidination.

4. %D?@LDACBD>Gd cross-linking between adjacent cytosine and thymine bases, creating

pyrimidine dimers

5. Mismatch of bases, due to errors in DNA replication, in which the wrong DNA base is

stitched into place in a newly forming DNA strand, or a DNA base is skipped over or

mistakenly inserted.

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Human genetic disorders can be broadly classified into three categories

Disorders related to mutations in single genes with large effects. These mutations cause the disease or

predispose to the disease and are typically not present in normal population. Such mutations and their associated

disorders are highly penetrant, meaning that the presence of the mutation is associated with the disease in a

large proportion of individuals. Because these diseases are caused by single gene mutations, they usually follow

the classic Mendelian pattern of inheritance and are also referred to as Mendelian disorders. A few important

exceptions to this rule are noted later.

Study of single genes and mutations with large effects has been extremely informative in medicine since a greatdeal of what we know about several physiologic pathways (such as cholesterol transport, chloride secretion) has

been learned from analysis of single gene disorders. Although informative, these disorders are generally rare

unless they are maintained in a population by strong selective forces (e.g., sickle cell anemia in areas where

malaria is endemic,

Chromosomal disorders. These arise from structural or numerical alteration in the autosomes and sex

chromosomes. Like monogenic disease they are uncommon but associated with high penetrance

Complex multigenic disorders. These are far more common than the previous two categories. They are

caused by interactions between multiple variant forms of genes and environmental factors. Such variations in

genes are common within the population and are also called polymorphisms. Each such variant gene confers a

small increase in disease risk, and no single susceptibility gene is necessary or sufficient to produce the disease.

It is only when several such polymorphisms are present in an individual that disease occurs, hence the term



multigenic or polygenic . Thus, unlike mutant genes with large effects that are highly penetrant and give rise to

Mendelian disorders, each polymorphism has a small effect and is of low penetrance. Since environmental

interactions are important in the pathogenesis of these diseases, they are also called multifactorial disorders. In

this category are some of the most common diseases that afflict humans, including atherosclerosis, diabetes

mellitus, hypertension, and autoimmune diseases. Even normal traits such as height and weight are governed bypolymorphisms in several genes.

Mendelian Disorders

It is estimated that every individual is a carrier of five to eight deleterious genes. Most of these are recessive and

therefore do not have serious phenotypic effects. About 80% to 85% of these mutations are familial. The

remainder represent new mutations acquired de novo by an affected individual.

Some autosomal mutations produce partial expression in the heterozygote and full expression in the

homozygote. Sickle cell anemia is caused by substitution of normal hemoglobin (HbA) by hemoglobin S (HbS).

When an individual is homozygous for the mutant gene, all the hemoglobin is of the abnormal, HbS, type, and

even with normal saturation of oxygen the disorder is fully expressed (i.e., sickling deformity of all red cells and

hemolytic anemia). In the heterozygote, only a proportion of the hemoglobin is HbS (the remainder being HbA),

and therefore red cell sickling occurs only when there is exposure to lowered oxygen tension. This is referred to

as the sickle cell trait to differentiate it from full-blown sickle cell anemia.

Although gene expression and mendelian traits are usually described as dominant or recessive, in some cases

both of the alleles of a gene pair contribute to the phenotype—a condition called codominance. Histocompatibility

and blood group antigens are good examples of codominant inheritance.

A single mutant gene may lead to many end effects, termed pleiotropism; conversely, mutations at several

genetic loci may produce the same trait (genetic heterogeneity). Sickle cell anemia is an example of pleiotropism.

In this hereditary disorder not only does the point mutation in the gene give rise to HbS, which predisposes thered cells to hemolysis, but also the abnormal red cells tend to cause a logjam in small vessels, inducing, for

example, splenic fibrosis, organ infarcts, and bone changes. The numerous differing end-organ derangements

are all related to the primary defect in hemoglobin synthesis. On the other hand, profound childhood deafness, an

apparently homogeneous clinical entity, results from many different types of autosomal recessive mutations.

TRANSMISSION PATTERNS OF SINGLE-GENE DISORDERS

Mutations involving single genes typically follow one of three patterns of inheritance: autosomal dominant,

autosomal recessive, and X-linked.

Autosomal Dominant Disorders

Autosomal dominant disorders are manifested in the heterozygous state, so at least one parent of an index case

is usually affected; both males and females are affected, and both can transmit the condition. When an affected

person marries an unaffected one, every child has one chance in two of having the disease. In addition to these

basic rules, autosomal dominant conditions are characterized by the following:

• With every autosomal dominant disorder, some proportion of patients do not have affected parents. Such patients

owe their disorder to new mutations involving either the egg or the sperm from which they were derived. Their

siblings are neither affected nor at increased risk for developing the disease. The proportion of patients who develop

the disease as a result of a new mutation is related to the effect of the disease on reproductive capability. If a disease

markedly reduces reproductive fitness, most cases would be expected to result from new mutations. Many new

mutations seem to occur in germ cells of relatively older fathers.

•

Clinical features can be modified by variations in penetrance and expressivity. Some individuals inheritthe mutant gene but are phenotypically normal. This is referred to as incomplete penetrance.



Penetrance is expressed in mathematical terms. Thus, 50% penetrance indicates that 50% of those who

carry the gene express the trait. In contrast to penetrance, if a trait is seen in all individuals carrying the

mutant gene but is expressed differently among individuals, the phenomenon is called variable

expressivity . For example, manifestations of neurofibromatosis type 1 range from brownish spots on the

skin to multiple skin tumors and skeletal deformities. The mechanisms underlying incompletepenetrance and variable expressivity are not fully understood, but they most likely result from effects of

other genes or environmental factors that modify the phenotypic expression of the mutant allele. For

example, the phenotype of a patient with sickle cell anemia (resulting from mutation at the !-globin

locus) is influenced by the genotype at the "-globin locus, because the latter influences the total amount

of hemoglobin made

• In many conditions the age at onset is delayed: symptoms and signs may not appear until adulthood (as

in Huntington disease).

The biochemical mechanisms of autosomal dominant disorders are best considered in the context of the

nature of the mutation and the type of protein affected. Most mutations lead to the reduced production of a

gene product or give rise to an inactive protein. The effect of such loss-of-function mutations depends on

the nature of the protein affected. If the mutation affects an enzyme protein the heterozygotes are usually

normal. Because up to 50% loss of enzyme activity can be compensated for, mutation in genes that encode

enzymes do not manifest an autosomal dominant pattern of inheritance. By contrast, two major categories

of nonenzyme proteins are affected in autosomal dominant disorders:

Less common than loss-of-function mutations are gain-of-function mutations. As the name indicates, in this

type of mutation the protein product of the mutant allele acquires new properties not normally associated with

the wild-type protein. The transmission of disorders produced by gain-of-function mutations is almost always

autosomal dominant, as illustrated by Huntington disease ( Chapter 28 ). In this disease the trinucleotide-

repeat mutation affecting the Huntington gene (see later) gives rise to an abnormal protein, called huntingtin,

that is toxic to neurons, and hence even heterozygotes develop a neurologic deficit.

To summarize, two types of mutations and two categories of proteins are involved in the pathogenesis of

autosomal dominant diseases. The more common loss-of-function mutations affect regulatory proteins and

subunits of multimeric proteins, the latter acting through a dominant-negative effect. Gain-of-function

mutations are less common; they often endow normal proteins with toxic properties, or more rarely increase

a normal activity (e.g., activating mutation in the erythropoetin receptor associated with a pathologic

increase in red cell production).

Autosomal Recessive Disorders

Autosomal recessive traits make up the largest category of mendelian disorders. Because autosomal recessive

disorders result only when both alleles at a given gene locus are mutated, such disorders are characterized by

the following features: (1) The trait does not usually affect the parents of the affected individual, but siblings may

show the disease; (2) siblings have one chance in four of having the trait (i.e., the recurrence risk is 25% for each

birth); and (3) if the mutant gene occurs with a low frequency in the population, there is a strong likelihood that

the affected individual (proband) is the product of a consanguineous marriage. The following features generally

apply to most autosomal recessive disorders and distinguish them from autosomal dominant diseases:

• Although new mutations associated with recessive disorders do occur, they are rarely detected clinically.

Since the individual with a new mutation is an asymptomatic heterozygote, several generations maypass before the descendants of such a person mate with other heterozygotes and produce affected



offspring.

• The expression of the defect tends to be more uniform than in autosomal dominant disorders

• Complete penetrance is common.

• Onset is frequently early in life

•

Although new mutations associated with recessive disorders do occur, they are rarely detected clinically.Since the individual with a new mutation is an asymptomatic heterozygote, several generations may

pass before the descendants of such a person mate with other heterozygotes and produce affected

offspring.

• Many of the mutated genes encode enzymes. In heterozygotes, equal amounts of normal and defective

enzyme are synthesized. Usually the natural “margin of safety” ensures that cells with half the usual

complement of the enzyme function normally.

Autosomal recessive disorders include almost all inborn errors of metabolism.

TABLE 5-2 -- Autosomal Recessive Disorders

System Disorder

Cystic fibrosis

Phenylketonuria

Galactosemia

Homocystinuria

Lysosomal storage diseases[*]

"1-Antitrypsin deficiency

Wilson disease

Hemochromatosis

Metabolic

Glycogen storage diseases[*]

Sickle cell anemiaHematopoietic

Thalassemias

Endocrine Congenital adrenal hyperplasia

Ehlers-Danlos syndrome (some variants)[*] Skeletal

Alkaptonuria[*]

Neurogenic muscular atrophies

Friedreich ataxia

Nervous

Spinal muscular atrophy

* Discussed in this chapter. Many others are discussed elsewhere in the text.

X-Linked Disorders

All sex-linked disorders are X-linked, and almost all are recessive. Several genes are located in the “male-

specific region of Y”; all of these are related to spermatogenesis. [13] Males with mutations affecting the Y-

linked genes are usually infertile, and hence there is no Y-linked inheritance. As discussed later, a few



additional genes with homologues on the X chromosome have been mapped to the Y chromosome, but no

disorders resulting from mutations in such genes have been described.

X-linked recessive inheritance accounts for a small number of well-defined clinical conditions. The Y

chromosome, for the most part, is not homologous to the X, and so mutant genes on the X do not have

corresponding alleles on the Y. Thus, the male is said to be hemizygous for X-linked mutant genes, so

these disorders are expressed in the male. Other features that characterize these disorders are as follows:

• An affected male does not transmit the disorder to his sons, but all daughters are carriers. Sons of

heterozygous women have, of course, one chance in two of receiving the mutant gene.

• The heterozygous female jusually does not express the full phenotypic change becuase of the

paired normal allele. Because of the random inactivation of one of the X chromosomes however,

females have a variable proportion of cells in which the mutant X chromosome is active. Thus, it is

remotely possible fort he normal allele to be inactivated in most cells, permitting full expression of

heterozygous X linked conditions. More commonly, the female expresses the disorder partially

(G6PD deficiency).

TABLE 5-3 -- X-Linked Recessive Disorders

System Disease

Musculoskeletal Duchenne muscular dystrophy

Hemophilia A and B

Chronic granulomatous disease

Blood

Glucose-6-phosphate dehydrogenase deficiency

AgammaglobulinemiaImmune

Wiskott-Aldrich syndrome

Diabetes insipidusMetabolic

Lesch-Nyhan syndrome

Nervous Fragile-X syndrome[*]

* Discussed in this chapter. Others are discussed in appropriate chapters in the text.

otein

pe/Function Example Molecular Lesion

Phenylalanine hydroxylase Splice-site mutation: reduced amount

Hexosaminidase Splice-site mutation or frameshift mutation with stop codon: reduced amou

ZYME

Adenosine deaminase Point mutations: abnormal protein with reduced activity

ZYME

HIBITOR

"1-Antitrypsin Missense mutations: impaired secretion from liver to serum

Low-density lipoprotein receptor Deletions, point mutations: reduction of synthesis, transport to cell surface

density lipoprotein

CEPTOR

Vitamin D receptor Point mutations: failure of normal signaling



There are only a few X-linked dominant conditions. They are caused by dominant disease-associated

alleles on the X chromosome. These disorders are transmitted by an affected heterozygous female to half

her sons and half her daughters and by an affected male parent to all his daughters but none of his sons, if

the female parent is unaffected. Vitamin D–resistant rickets is an example of this type of inheritance.

BIOCHEMICAL AND MOLECULAR BASIS OF SINGLE-GENE (MENDELIAN) DISORDERS

Mendelian disorders result from alterations involving single genes. The genetic defect may lead to the formation

of an abnormal protein or a reduction in the output of the gene product. Virtually any type of protein may be

affected in single-gene disorders and by a variety of mechanisms ( Table 5-4 ). To some extent the pattern of

inheritance of the disease is related to the kind of protein affected by the mutation, as was discussed earlier and

is reiterated subsequently. The mechanisms involved in single-gene disorders can be classified into four

categories: (1) enzyme defects and their consequences; (2) defects in membrane receptors and transport

systems; (3) alterations in the structure, function, or quantity of nonenzyme proteins; and (4) mutations resulting

in unusual reactions to drugs.

TABLE 5-4 -- Biochemical and Molecular Basis of Some Mendelian Disorders

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Enzyme Defects and Their Consequences

Mutations may result in the synthesis of a defective enzyme with reduced activity or in a reduced amount of a

normal enzyme. In either case, the consequence is a metabolic block. Figure 5-6 provides an example of an

enzyme reaction in which the substrate is converted by intracellular enzymes, denoted as 1, 2, and 3, into an end

product through intermediates 1 and 2. In this model the final product exerts feedback control on enzyme 1. A

minor pathway producing small quantities of M1 and M2 also exists. The biochemical consequences of an

enzyme defect in such a reaction may lead to three major consequences:

ANSPORT

Deletions: reduced amount

Defective mRNA processing: reduced amount

ygen Hemoglobin

Point mutations: abnormal structure

ns Cystic fibrosis transmembrane conductance

regulator

Deletions and other mutations: nonfunctional or misfolded proteins

RUCTURAL

Collagen Deletions or point mutations cause reduced amount of normal collagen or

defective collagen

tracellular

Fibrillin Missense mutations

Dystrophin Deletion with reduced synthesisll membrane

Spectrin, ankyrin, or protein 4.1 Heterogeneous

MOSTASIS Factor VIII Deletions, insertions, nonsense mutations, and others: reduced synthesis

Rb protein DeletionsROWTH

GULATION Neurofibromin Heterogeneous



• Accumulation of the substrate, depending on the site of block, may be accompanied by accumulation of

one or both intermediates. Moreover, an increased concentration of intermediate 2 may stimulate the

minor pathway and thus lead to an excess of M1 and M2. Under these conditions tissue injury may

result if the precursor, the intermediates, or the products of alternative minor pathways are toxic in high

concentrations. For example, in galactosemia, the deficiency of galactose-1-phosphate uridyltransferase( Chapter 10 ) leads to the accumulation of galactose and consequent tissue damage. Excessive

accumulation of complex substrates within the lysosomes as a result of deficiency of degradative

enzymes is responsible for a group of diseases generally referred to as lysosomal storage diseases.

• An enzyme defect can lead to a metabolic block and a decreased amount of end product that may be

necessary for normal function. For example, a deficiency of melanin may result from lack of tyrosinase,

which is necessary for the biosynthesis of melanin from its precursor, tyrosine. This results in the clinical

condition called albinism. If the end product is a feedback inhibitor of the enzymes involved in the early

reactions, the deficiency of the end product may permit overproduction of intermediates and their

catabolic products, some of which may be injurious at high concentrations. A prime example of a

disease with such an underlying mechanism is Lesh-Nyhan syndrome

• Failure to inactivate a tissue damaging substrate is best exemplified by a-antitrypsin deficiency. They

are unable to inactivate neutrophil elastase in their lungs. Unchecked activity of this protease leads to

destruction of elastin in the walls of lung alveoli, leading to emphysema.

DISORDERS ASSOCIATED WITH DEFECTS IN ENZYMES

Lysosomal Storage Diseases

Lysosomes are key components of the “intracellular digestive tract.” They contain a battery of hydrolytic enzymes, whichhave two special properties. First, they function in the acidic milieu of the lysosomes. Second, these enzymes constitute aspecial category of secretory proteins that are destined not for the extracellular fluids but for intracellular organelles. Thislatter characteristic requires special processing within the Golgi apparatus, which is reviewed briefly. Similar to all othersecretory proteins, lysosomal enzymes (or acid hydrolases, as they are sometimes called) are synthesized in theendoplasmic reticulum and transported to the Golgi apparatus. Within the Golgi complex they undergo a variety of post-translational modifications, of which one is worthy of special note. This modification involves the attachment of terminalmannose6-phosphate groups to some of the oligosaccharide side chains. The phosphorylated mannose residues serve

as an “address label” that is recognized by specific receptors found on the inner surface of the Golgi membrane.Lysosomal enzymes bind these receptors and are thereby segregated from the numerous other secretory proteins withinthe Golgi. Subsequently, small transport vesicles containing the receptor-bound enzymes are pinched off from the Golgiand proceed to fuse with the lysosomes. Thus, the enzymes are targeted to their intracellular abode, and the vesicles are

shuttled back to the Golgi ( Fig. 5-10 ). As indicated later, genetically determined errors in this remarkable sortingmechanism may give rise to one form of lysosomal storage disease.

The lysosomal acid hydrolases catalyze the breakdown of a variety of complex macromolecules. These

large molecules may be derived from the metabolic turnover of intracellular organelles (autophagy), or they

may be acquired from outside the cells by phagocytosis (heterophagy). With an inherited deficiency of a

functional lysosomal enzyme, catabolism of its substrate remains incomplete, leading to the accumulation of

the partially degraded insoluble metabolite within the lysosomes. Stuffed with incompletely digested

macromolecules, these organelles become large and numerous enough to interfere with normal cell

functions, giving rise to the so-called lysosomal storage disorders ( Fig. 5-11 ). In addition to “missing

enzymes,” lysosomal storage diseases can result from lack of any protein essential for normal function of

lysosomes. Examples are:



•

Lack of an enzyme activator or protector protein.

• Lack of a substrate activator protein. In some instances, proteins that react with the substrate to facilitate its hydrolysis may be missi

• Lack of a transport protein required for egress of the digested material from the lysosomes.

PHENYLKETONURIA (PKU)



PKU is characterized by abnormalities of phenylalanine metabolism, resulting in hyperphenylalaninemia. PKU is

an autosomal recessive condition, and the vast majority of PKU is caused by bi-allelic mutations of the gene

encoding the enzyme phenylalanine hydroxylase (PAH). Nevertheless, the great diversity in clinical presentation

underscores the genetic complexities that underlie even classic “mendelian” diseases like PKU.[25] At the

molecular level, more than 500 diseaseassociated alleles of the PAH gene have been identified in populations

worldwide. Each mutation induces a particular alteration in the enzyme resulting in a corresponding quantitative

effect on residual enzyme activity ranging from complete absence to 50% of normal values. The degree of

hyperphenylalaninemia and clinical phenotype is inversely related to the amount of residual enzyme activity.

Infants with mutations resulting in a lack of PAH activity present with the classic features of PKU, while those with

up to 6% residual activity present with milder disease. Moreover, some mutations result in only modest elevations

of blood phenylalanine levels without associated neurologic damage. This latter condition, referred to as benign

hyperphenylalaninemia, is important to recognize, because the individuals may well have positive screening tests

but do not develop the stigmata of classic PKU. Measurement of serum phenylalanine differentiates benign

hyperphenylalaninemia and classic PKU, with the concentrations being typically above 600 µM in PKU (normal

phenylalanine concentrations, by contrast, are less than 120 µM).

The biochemical abnormality in PKU is an inability to convert phenylalanine into tyrosine. In normal children, lessthan 50% of the dietary intake of phenylalanine is necessary for protein synthesis. The rest is irreversiblyconverted to tyrosine by PAH in the liver as part of a complex metabolic pathway, the hepatic PAH system ( Fig.10-15 ), which, in addition to the enzyme PAH, has two other components: the cofactor tetrahydrobiopterin (BH 4)and the enzyme dihydropteridine reductase, which regenerates BH4. Although neonatal hyperphenylalaninemiacan be caused by deficiencies in any of these components, about 98% of cases are attributable to abnormalitiesin PAH and the remaining 2% to abnormalities in synthesis or recycling of BH4. BH4 is not only an essentialcofactor for PAH but is also required for tyrosine and tryptophan hydroxylation. Concomitant defects in BH 4 recycling disturb the synthesis of neurotransmitters. As a result, in patients with BH 4 recycling defects neurologic

damage is not arrested despite normalization of phenylalanine levels. Although they account for a small minorityof patients with hyperphenylalaninemia, it is important to recognize these PKU variants because the ongoingneurologic disturbances cannot be treated by dietary control of phenylalanine levels alone .

Individuals with “classic” PKU have a severe deficiency of PAH, leading to hyperphenylalaninemia and its

pathologic consequences. With a block in phenylalanine metabolism due to lack of PAH, minor shunt

pathways come into play, yielding phenylpyruvic acid, phenyllactic acid, phenylacetic acid, and o-

hydroxyphenylacetic acid, which are excreted in large amounts in the urine in PKU. Some of these

abnormal metabolites are excreted in the sweat, and phenylacetic acid in particular imparts a strong musty

or mousy odor to affected infants. It is believed that excess phenylalanine or its metabolites contribute to

the brain damage in PKU. Affected infants are normal at birth but within a few weeks develop a rising

plasma phenylalanine level, which in some way impairs brain development. Usually by 6 months of life

severe mental retardation becomes evident; fewer than 4% of untreated PKU children have intelligence

quotient values greater than 50 or 60. About one third of these children are never able to walk, and two

thirds cannot talk. Seizures, other neurologic abnormalities, decreased pigmentation of hair and skin, and

eczema often accompany the mental retardation in untreated children. Hyperphenylalaninemia and the

resultant mental retardation can be avoided by restriction of phenylalanine intake early in life. Hence,

several screening procedures are routinely used for detection of PKU in the immediate postnatal period.

Many clinically normal female PKU patients who are treated with dietary control early in life reach

childbearing age. If such individuals were to discontinue dietary treatment, the result would be marked

hyperphenylalaninemia. Between 75% and 90% of children born to such women are mentally retarded and

microcephalic, and 15% have congenital heart disease, even though the infants themselves are

heterozygotes. This syndrome, termed maternal PKU , results from the teratogenic effects of phenylalanine

or its metabolites that cross the placenta and affect specific fetal organs during development. The presenceand severity of the fetal anomalies directly correlate with the maternal phenylalanine level, so it is



imperative that maternal dietary restriction of phenylalanine be initiated before conception and continue

throughout pregnancy .

Although dietary restriction of phenylalanine is usually successful in reducing or preventing the mental

retardation associated with PKU, there are problems with long-term compliance (resulting in a decline in

mental or behavioral status) and nutritional imbalances involving trace minerals, fatty acids, and lipids. A

subset of patients with PAH missense mutations are responsive to pharmacologic dosages of BH 4; some

recent analyses have predicted that as many as half of prevalent PAH mutations in some populations may

be “BH4 responsive.”[26] Since there are no primary abnormalities of BH 4 in these patients, it is believed that

this cofactor acts as a “molecular chaperone,” preventing the degradation of misfolded PAH protein.

Permanent restitution of PAH activity through gene therapy remains the ultimate goal; recent studies in

animal models of PKU have produced encouraging results.[27]

GALACTOSEMIA

Galactosemia is an autosomal recessive disorder of galactose metabolism. Normally, lactose, the majorcarbohydrate of mammalian milk, is split into glucose and galactose in the intestinal microvilli by lactase.Galactose is then converted to glucose in three steps ( Fig. 10-16 ). Two variants of galactosemia have beenidentified. In the more common variant there is a total lack of galactose-1-phosphate uridyl transferase (alsoknown as GALT ) involved in reaction 2. The rare variant arises from a deficiency of galactokinase, involved inreaction 1. Because galactokinase deficiency leads to a milder form of the disease not associated with mentalretardation, it is not considered in this discussion. As a result of the transferase lack, galactose-1-phosphate

accumulates in many locations, including the liver, spleen, lens of the eye, kidneys, heart muscle, cerebral cortex,and erythrocytes. Alternative metabolic pathways are activated, leading to the production of galactitol (a polyolmetabolite of galactose) and galactonate, an oxidized by-product of excess galactose, both of which alsoaccumulate in the tissues. Long-term toxicity in galactosemics has been variously imputed to these metabolicintermediates.[28] Heterozygotes may have a mild deficiency but are spared the clinical and pathologicconsequences of the homozygous state.The clinical picture is variable, probably reflecting the heterogeneity of mutations in the galactose-1-phosphate

uridyl transferase gene leading to galactosemia. The liver, eyes, and brain bear the brunt of the damage. Theearly-to-develop hepatomegaly is due largely to fatty change, but in time widespread scarring that closely

resembles the cirrhosis of alcohol abuse may supervene ( Fig. 10-17 ). Opacification of the lens (cataract) develops, probably because the lens absorbs water and swells as galactitol, produced by alternative metabolicpathways, accumulates and increases its tonicity. Nonspecific alterations appear in the central nervous system,including loss of nerve cells, gliosis, and edema, particularly in the dentate nuclei of the cerebellum and theolivary nuclei of the medulla. Similar changes may occur in the cerebral cortex and white matter.

These infants fail to thrive almost from birth. Vomiting and diarrhea appear within a few days of milk

ingestion. Jaundice and hepatomegaly usually become evident during the first week of life and may seem to

be a continuation of the physiologic jaundice of the newborn. The cataracts develop within a few weeks,

and within the first 6 to 12 months of life mental retardation may be detected. Even in untreated infants,

however, the mental deficit is usually not as severe as that seen in PKU. Accumulation of galactose and

galactose-1-phosphate in the kidney impairs amino acid transport, resulting in aminoaciduria. There is an

increased frequency of fulminant Escherichia coli septicemia, possibly arising from depressed neutrophil

bactericidal activity. Hemolysis and coagulopathy in the newborn period can occur as well.

The diagnosis of galactosemia can be suspected by the demonstration in the urine of a reducing sugar

other than glucose, but tests that directly identify the deficiency of the transferase in leukocytes and

erythrocytes are more reliable. Antenatal diagnosis is possible by the assay of GALT activity in cultured

amniotic fluid cells or determination of galactitol level in amniotic fluid supernatant. More than 140 mutations

have been documented in GALT ; among these, a glutamine-to-arginine substitution at codon 188

(Gln188Arg) is the most prevalent mutation in non-Hispanic whites, while a serine-to-leucine substitution atcodon 135 (Ser135Leu) is the most common mutation in African Americans.



Many of the clinical and morphologic changes of galactosemia can be prevented or ameliorated by early

removal of galactose from the diet for at least the first 2 years of life . Control instituted soon after birth

prevents the cataracts and liver damage and permits almost normal development. Even with dietary

restrictions, however, it is now established that older patients are frequently affected by a speech disorder

and gonadal failure (especially premature ovarian failure) and, less commonly, by an ataxic condition.

CYSTIC FIBROSIS (MUCOVISCIDOSIS)

Cystic fibrosis is a disorder of ion transport in epithelial cells that affects fluid secretion in exocrine glands and the

epithelial lining of the respiratory, gastrointestinal, and reproductive tracts. In many infants this disorder leads to

abnormally viscous secretions, which obstruct organ passages, resulting in most of the clinical features of this

disorder, such as chronic lung disease secondary to recurrent infections, pancreatic insufficiency, steatorrhea,

malnutrition, hepatic cirrhosis, intestinal obstruction, and male infertility . These manifestations may appear at any

point in life from before birth to much later in childhood or even in adolescence.

With an incidence of 1 in 2500 live births, cystic fibrosis is the most common lethal genetic disease that affects

Caucasian populations. The carrier frequency in the United States is 1 in 20 among Caucasians but significantly

lower in African Americans, Asians, and Hispanics. Although cystic fibrosis follows an autosomal recessive

transmission, recent data suggest that even heterozygote carriers have a higher incidence of respiratory and

pancreatic diseases as compared with the general population.[29,][30] In addition, despite the classification of

cystic fibrosis as a “mendelian” disorder, there is a wide degree of phenotypic variation that results from diverse

mutations in the gene associated with cystic fibrosis, the tissue-specific effects of this gene, and the influence of

newly recognized disease modifiers.[31]

The Cystic Fibrosis–Associated Gene: Normal Structure and Function.

In normal duct epithelia, chloride is transported by plasma membrane channels (chloride channels). The primarydefect in cystic fibrosis results from abnormal function of an epithelial chloride channel protein encoded by thecystic fibrosis transmembrane conductance regulator (CFTR) gene on chromosome 7q31.2 . The 1480–aminoacid polypeptide encoded by CFTR has two transmembrane domains (each containing six "-helices), twocytoplasmic nucleotide-binding domains (NBDs), and a regulatory domain (R domain) that contains proteinkinase A and C phosphorylation sites ( Fig. 10-18 ). The two transmembrane domains form a channel through

which chloride passes. Activation of the CFTR channel is mediated by agonist-induced increases in cyclicadenosine monophosphate (cAMP), followed by activation of a protein kinase A that phosphorylates the Rdomain. Adenosine triphosphate (ATP) binding and hydrolysis occurs at the NBD and is essential for the openingand closing of the channel pore in response to cAMP-mediated signaling. Several important facets of CFTR



function have emerged in recent years:

The Cystic Fibrosis Gene: Mutational Spectra and Genotype-Phenotype Correlation.

Since the CFTR gene was cloned in 1989, more than 1300 disease-associated mutations have been identified.

Various mutations can be grouped into six “classes” based on their effect on the CFTR protein:

• Class I: Defective protein synthesis. These mutations are associated with complete lack of CFTR protein at the apical surface of epithelial cells.

• Class II: Abnormal protein folding, processing, and trafficking . These mutations result in defective processing of the protein from the endoplasmic reti

cell surface. The most common class II mutation is a deletion of three nucleotides coding for phenylalanine at amino acid position 508 ( #F508). Worl

lack of CFTR protein at the apical surface of epithelial cells.

• Class III: Defective regulation. Mutations in this class prevent activation of CFTR by preventing ATP binding and hydrolysis, an essential prerequisite

• Class IV: Decreased conductance. These mutations typically occur in the transmembrane domain of CFTR , which forms the ionic pore for chloride tr

milder phenotype.

• Class V: Reduced abundance. These mutations typically affect intronic splice sites or the CFTR promoter, such that there is a reduced amount of no

• Class VI: Altered regulation of separate ion channels. As previously described, CFTR is involved in the regulation of multiple distinct

the conductance by CFTR as well as regulation of other ion channels. For example, the #F508 mutation is both a class II and classSince cystic fibrosis is an autosomal recessive disease, affected individuals harbor mutations on both alleles.However, the combination of mutations on the two alleles can have a remarkable effect on the overall phenotype,as well as on organ-specific manifestations ( Fig. 10-20 ). Thus, two “severe” (class I, II, and III) mutations thatproduce virtual absence of membrane CFTR are associated with the classic cystic fibrosis phenotype (pancreaticinsufficiency, sinopulmonary infections, and gastrointestinal symptoms), while the presence of a “mild” (class IVor V) mutation on one or both alleles results in a less severe phenotype. This general dictum of genotype-phenotype correlation is most consistent for pancreatic disease, wherein the presence of a “mild” mutation in oneallele can revert to the pancreatic insufficiency phenotype conferred by homozygosity for “severe” mutations. Bycontrast, genotype-phenotype correlations are far less consistent in pulmonary disease, reflecting an effect of

secondary modifiers (see below). As genetic testing for CFTR mutations has expanded, it has becomeincreasingly evident that patients who present with a variety of apparently unrelated clinical phenotypes may alsoharbor CFTR mutations. These include individuals with idiopathic chronic pancreatitis, late-onset chronic

pulmonary disease, idiopathic bronchiectasis, and obstructive azoospermia caused by bilateral absence of thevas deferens (see detailed discussion of individual phenotypes later). Most of these patients do not demonstrate

other features of cystic fibrosis, despite the presence of bi-allelic CFTR mutations, and are classified asnonclassic or atypical cystic fibrosis.[34] Identifying these individuals is important not only for subsequentmanagement, but also for the purposes of genetic counseling.



Genetic and Environmental Modifiers.

Although cystic fibrosis remains one of the best-known examples of the “one gene, one disease” axiom, there is

increasing evidence that genes other than CFTR modify the frequency and severity of organ-specific

manifestations.[35] The severity of pulmonary manifestations in cystic fibrosis is associated with polymorphicvariants at several genes, the best known examples of which are mannose-binding lectin 2 (MBL2 ) and

transforming growth factor !1 (TGFB1). MBL is a key effector of innate immunity involved in opsonization and

phagocytosis of microorganisms, and polymorphisms in the MBL2 gene that are associated with lower circulating

levels of the protein confer a threefold higher risk of end-stage lung disease. TGF! is a direct inhibitor of CFTR

function.[36,][37] A large multicenter study of patients homozygous for the #F508 CFTR mutation found two

specific polymorphisms in the 5$ end of the TGFB1 gene to be associated with severe pulmonary phenotypes. [38]

Similarly, several putative genetic modifiers have been identified that influence the incidence of meconium ileus

in cystic fibrosis, although the precise genes associated with the linked chromosomal regions have not yet been

identified.[39]

Environmental modifiers may also cause significant phenotypic differences between individuals who share the

same CFTR genotype. This is best exemplified in pulmonary disease, where CFTR genotype and phenotype

correlations can be perplexing. As stated above, defective mucociliary action because of deficient hydration of

the mucus results in an inability to clear bacteria from the airways. Pseudomonas aeruginosa species, in

particular, colonize the lower respiratory tract, first intermittently and then chronically. Concurrent viral infections

predispose to such colonization. The static mucus creates a hypoxic microenvironment in the airway surface

fluid, which in turn favors the production of alginate, a mucoid polysaccharide capsule. Alginate production

permits the formation of a biofilm that protects the bacteria from antibodies and antibiotics, allowing them to

evade host defenses, and produce a chronic destructive lung disease. Antibody- and cell-mediated immune

reactions induced by the organisms result in further pulmonary destruction, but are ineffective against theorganism. It is evident, therefore, that in addition to genetic factors (e.g., class of mutation), a plethora of

environmental modifiers (e.g., virulence of organisms, efficacy of therapy, intercurrent and concurrent infections

by other organisms, exposure to smoking and allergens) can influence the severity and progression of lung

disease in cystic fibrosis.

Exocrine pancreatic insufficiency occurs in the majority (85% to 90%) of patients with cystic fibrosis and is

associated with “severe” CFTR mutations on both alleles (e.g., #F508/ #F508 ), whereas 10% to 15% of

patients with one “severe” and one “mild” CFTR mutation ( #F508/R117H) or two “mild” CFTR mutations

retain enough pancreatic exocrine function so as not to require enzyme supplementation

( pancreassufficient phenotype). Pancreatic insufficiency is associated with protein and fat malabsorption

and increased fecal loss. Manifestations of malabsorption (e.g., large, foul-smelling stools, abdominal

distention, and poor weight gain) appear during the first year of life. The faulty fat absorption may induce

deficiency of the fat-soluble vitamins, resulting in manifestations of avitaminosis A, D, or K.

Hypoproteinemia may be severe enough to cause generalized edema. Persistent diarrhea may result in

rectal prolapse in up to 10% of children with cystic fibrosis. The pancreas-sufficient phenotype is usually not

associated with other gastrointestinal complications, and in general, these individuals demonstrate excellent

growth and development. “Idiopathic” chronic pancreatitis occurs in a subset of patients with pancreas-

sufficient cystic fibrosis and is associated with recurrent abdominal pain with life-threatening complications.

These patients have other features of cystic fibrosis, such as pulmonary disease. By contrast, “idiopathic”

chronic pancreatitis can also occur as an isolated late-onset finding in the absence of other stigmata of



cystic fibrosis ( Chapter 19 ); bi-allelic CFTR mutations (usually one “mild,” one “severe”) are demonstrable

in the majority of these individuals who have nonclassic or atypical cystic fibrosis. Endocrine pancreatic

insufficiency (i.e., diabetes) is uncommon in cystic fibrosis and is usually accompanied by substantial

destruction of pancreatic parenchyma.

Cardiorespiratory complications, such as persistent lung infections, obstructive pulmonary disease, and cor

pulmonale, are the most common cause of death (!80%) in patients in the United States. By age 18, 80%

of patients with classic cystic fibrosis harbor P. aeruginosa. With the indiscriminate use of antibiotic

prophylaxis against Staphylococcus, there has been an unfortunate resurgence of resistant strains of

Pseudomonas in many patients. Individuals who carry one “severe” and one “mild” CFTR mutation may

develop late-onset mild pulmonary disease, another example of nonclassic or atypical cystic fibrosis.

Patients with mild pulmonary disease usually have little or no pancreatic disease. Adult-onset “ idiopathic ”

bronchiectasis, has been linked to CFTR mutations in a subset of cases. Recurrent sinonasal polyps can

occur in up to 25% of individuals with cystic fibrosis; hence, children who present with this finding should be

tested for cystic fibrosis.

Significant liver disease occurs late in the natural history of cystic fibrosis and is gaining in clinical

importance as life expectancies increase. In fact, after cardiopulmonary and transplantation-related

complications, liver disease is the most common cause of death in cystic fibrosis. Most studies suggest that

symptomatic or biochemical liver disease has its onset at or around puberty, with a prevalence of

approximately 13% to 17%. However, asymptomatic hepatomegaly may be present in up to a third of

individuals. Obstruction of the common bile duct may occur due to stones or sludge; it presents with

abdominal pain and the acute onset of jaundice. As previously noted, diffuse biliary cirrhosis develops in

less than 10% of individuals with cystic fibrosis.

Approximately 95% of males with cystic fibrosis are infertile, as a result of obstructive azoospermia. As

mentioned earlier, this is most commonly due to congenital bilateral absence of the vas deferens, which is

caused in 80% of cases by bi-allelic CFTR mutations.

In most cases, the diagnosis of cystic fibrosis is based on persistently elevated sweat electrolyte

concentrations (often the mother makes the diagnosis by recognizing her infant's abnormally salty sweat),

characteristic clinical findings (sinopulmonary disease and gastrointestinal manifestations), an abnormal

newborn screening test, or a family history. A minority of patients with cystic fibrosis, especially those with

at least one “mild” CFTR mutation, may have a normal or near-normal sweat test (<60 mM/L).

Measurement of nasal transepithelial potential difference in vivo can be a useful adjunct test under these

circumstances; individuals with cystic fibrosis demonstrate a significantly more negative baseline nasal

potential difference than controls. Sequencing the CFTR gene is, of course, the “gold standard” for

diagnosis of cystic fibrosis. Therefore, in patients with suggestive clinical findings or family history (or both),

genetic analysis may be warranted.

There have been major improvements in the management of acute and chronic complications for cystic

fibrosis, including more potent antimicrobial therapies, pancreatic enzyme replacement, and bilateral lung

transplantation. Newer modalities for restituting endogenous CFTR function have also emerged in recent

years. In principle, cystic fibrosis, like other single-gene disorders, should be amenable to gene therapy,

and several adenoviral gene therapy vectors are currently undergoing early-phase clinical trials.

Improvement in management of cystic fibrosis has resulted in enhancement of median life expectancy to



above 36 years as of 2006,[41] and increasingly, a lethal disease of childhood is changing into a chronic

disease of adults.

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Defects in Receptors and Transport Systems

Many biologically active substances have to be actively transported across the cell membrane. This transport is

generally achieved by one of two mechanisms—through receptormediated endocytosis or by a transport protein.

A genetic defect in a receptor-mediated transport system is exemplified by familial hypercholesterolemia, in which

reduced synthesis or function of LDL receptors leads to defective transport of LDL into the cells and secondarily

to excessive cholesterol synthesis by complex intermediary mechanisms. In cystic fibrosis the transport system

for chloride ions in exocrine glands, sweat ducts, lungs, and pancreas is defective. By mechanisms not fully

understood, impaired chloride transport leads to serious injury to the lungs and pancreas ( Chapter 10 ).

Alterations in Structure, Function, or Quantity of Nonenzyme Proteins

Genetic defects resulting in alterations of nonenzyme proteins often have widespread secondary effects, as

exemplified by sickle cell disease. The hemoglobinopathies, sickle cell disease being one, all of which are

characterized by defects in the structure of the globin molecule, best exemplify this category. In contrast to the

hemoglobinopathies, the thalassemias result from mutations in globin genes that affect the amount of globin

chains synthesized. Thalassemias are associated with reduced amounts of structurally normal "-globin or !-

globin chains ( Chapter 14 ). Other examples of genetically defective structural proteins include collagen,spectrin, and dystrophin, giving rise to osteogenesis imperfecta ( Chapter 26 ), heredit-ary spherocytosis (

Chapter 14 ), and muscular dystrophies ( Chapter 27 ), respectively.

DISORDERS ASSOCIATED WITH DEFECTS IN STRUCTURAL PROTEINS

Marfan Syndrome

Marfan syndrome is a disorder of connective tissues, manifested principally by changes in the skeleton,

eyes, and cardiovascular system.[15] Its prevalence is estimated to be 1 in 5000. Approximately 70% to

85% of cases are familial and transmitted by autosomal dominant inheritance. The remainder are sporadic

and arise from new mutations.

Pathogenesis.

Marfan syndrome results from an inherited defect in an extracellular glycoprotein called fibrillin-1. As alluded to in

Chapter 3 , fibrillin is the major component of microfibrils found in the extracellular matrix. These fibrils provide a

scaffolding on which tropoelastin is deposited to form elastic fibers. Although microfibrils are widely distributed in

the body, they are particularly abundant in the aorta, ligaments, and the ciliary zonules that support the lens;

these tissues are prominently affected in Marfan syndrome.

Fibrillin occurs in two homologous forms, fibrillin-1 and fibrillin-2, encoded by two separate genes, FBN1 and

FBN2 , mapped on chromosomes 15q21.1 and 5q23.31, respectively. Mutations of FBN1 underlie Marfan

syndrome; mutations of the related FBN2 gene are less common, and they give rise to congenital contractural

arachnodactyly , an autosomal dominant disorder characterized by skeletal abnormalities. Mutational analysis has



revealed more than 600 distinct mutations of the FBN1 gene in individuals with Marfan syndrome. Most of these

are missense mutations that give rise to abnormal fibrillin-1. While many clinical manifestations of Marfan

syndrome can be explained by changes in the mechanical properties of the extracellular matrix resulting from

abnormalities of fibrillin, several others such as bone overgrowth cannot be attributed to changes in tissue

elasticity. Recent studies indicate that loss of microfibrils gives rise to abnormal and excessive activation oftransforming growth factor ! (TGF-!), since normal microfibrils sequester TGF-! and thus control the

bioavailability of this cytokine. Excessive TGF-! signaling has deleterious effects on vascular smooth muscle

development and the integrity of extracellular matrix. This hypothesis is supported by two sets of observations.

First, in a small number of individuals with clinical features of Marfan syndrome (MFS2) there are no mutations in

FBN1 but mutations in genes that encode TGF-! receptors. Second, in mouse models of Marfan syndrome

generated by mutations in Fbn1, administration of antibodies to TGF-! prevents alterations in the aorta and mitral

valves.[16] Human trials with a similar strategy seem to be promising.

Clinical Features

Although mitral valve lesions are more frequent, they are clinically less important than aortic lesions. Loss of

connective tissue support in the mitral valve leaflets makes them soft and billowy, creating the so-called floppy

valve ( Chapter 12 ). Valvular lesions, along with lengthening of the chordae tendineae, frequently give rise to

mitral regurgitation. Similar changes may affect the tricuspid and, rarely, the aortic valves. Echocardiography

greatly enhances the ability to detect the cardiovascular abnormalities and is therefore extremely valuable in the

diagnosis of Marfan syndrome. The great majority of deaths are caused by rupture of aortic dissections, followed

in importance by cardiac failure.

While the lesions just described typify Marfan syndrome, it must be emphasized that there is great variation in the

clinical expression of this genetic disorder. Patients with prominent eye or cardiovascular changes may have few

skeletal abnormalities, whereas others with striking changes in body habitus have no eye changes. Althoughvariability in clinical expression may be seen within a family, interfamilial variability is much more common and

extensive. Because of such variations, the clinical diagnosis of Marfan syndrome must be based on major

involvement of two of the four organ systems (skeletal, cardiovascular, ocular, and skin) and minor involvement

of another organ.

To account for the variable expression of the Marfan defect, it has been hypothesized that Marfan syndrome is

genetically heterogeneous. With one exception, however, all studies thus far point to mutations in the FBN1

gene, on chromosome 15q21.1, as the cause of this disease. [15] Thus, variable expressivity is best explained on

the basis of allelic mutations within the same locus. Because the FBN1 gene is large and many different

mutations have been identified, direct diagnosis by DNA sequencing is not currently feasible, but this may

change in the near future as new technologies are being developed.

Ehlers-Danlos Syndromes (EDS)

EDSs comprise a clinically and genetically heterogeneous group of disorders that result from some defect in

the synthesis or structure of fibrillar collagen. Other disorders resulting from mutations affecting collagen

synthesis include osteogenesis imperfecta ( Chapter 26 ), Alport syndrome ( Chapter 20 ), and

epidermolysis bullosa ( Chapter 25 ).

Biosynthesis of collagen is a complex process that can be disturbed by genetic errors that may affect any

one of the numerous structural collagen genes or enzymes necessary for post-transcriptional modifications

of collagen. Hence, the mode of inheritance of EDS encompasses all three mendelian patterns. On the

basis of clinical and molecular characteristics, six variants of EDS have been recognized.[17] These are



listed in Table 5-5 . It is beyond the scope of this book to discuss each variant individually; instead, we first

summarize the important clinical features that are common to most variants and then correlate some of the

clinical manifestations with the underlying molecular defects in collagen synthesis or structure.

TABLE 5-5 -- Classification of Ehlers-Danlos Syndromes

DS Type[*] Clinical Findings Inheritance Gene Defects

lassical (I/II) Skin and joint hypermobility, atrophic scars, easy bruising Autosomal

dominant

COL5A1, COL5A2

ypermobility (III) Joint hypermobility, pain, dislocations Autosomal

dominant

Unknown

ascular (IV) Thin skin, arterial or uterine rupture, bruising, small joint hyperextensibility Autosomal

dominant

COL3A1

yphoscoliosis (VI) Hypotonia, joint laxity, congenital scoliosis, ocular fragility Autosomal

recessive

Lysyl hydroxylase

rthrochalasia (VIIa, b) Severe joint hypermobility, skin changes (mild), scoliosis, bruising Autosomal

dominant

COL1A1, COL1A2

ermatosparaxsis (VIIc) Severe skin fragility, cutis laxa, bruising Autosomal

recessive

Procollagen N -pept

EDS types were previously classified by R

As might be expected, tissues rich in collagen, such as skin, ligaments, and joints, are frequently involved in

most variants of EDS. Because the abnormal collagen fibers lack adequate tensile strength, skin is

hyperextensible, and the joints are hypermobile. These features permit grotesque contortions, such as

bending the thumb backward to touch the forearm and bending the knee forward to create almost a right

angle. It is believed that most contortionists have one of the EDSs. A predisposition to joint dislocation,

however, is one of the prices paid for this virtuosity. The skin is extraordinarily stretchable, extremely fragile,

and vulnerable to trauma. Minor injuries produce gaping defects, and surgical repair or intervention is

accomplished with great difficulty because of the lack of normal tensile strength. The basic defect in

connective tissue may lead to serious internal complications. These include rupture of the colon and large

arteries (vascular EDS), ocular fragility with rupture of cornea and retinal detachment (kyphoscoliosis EDS),

and diaphragmatic hernia (classical EDS).

The biochemical and molecular bases of these abnormalities are known in several forms of EDS. These are

described briefly, because they offer some insights into the perplexing clinical heterogeneity of EDS.

Perhaps the best characterized is the kyphoscoliosis type, the most common autosomal recessive form of

EDS. It results from mutations in the gene encoding lysyl hydroxylase, an enzyme necessary for

hydroxylation of lysine residues during collagen synthesis.[18] Affected patients have markedly reduced

levels of this enzyme. Because hydroxylysine is essential for the cross-linking of collagen fibers, a

deficiency of lysyl hydroxylase results in the synthesis of collagen that lacks normal structural stability.

The vascular type of EDS results from abnormalities of type III collagen.[19] This form is genetically

heterogeneous, because at least three distinct types of mutations affecting the COL3A1 gene encoding



collagen type III can give rise to this variant. Some affect the rate of synthesis of pro "1 (III) chains, others

affect the secretion of type III procollagen, and still others lead to the synthesis of structurally abnormal type

III collagen. Some mutant alleles behave as dominant negatives (see discussion under “Autosomal

Dominant Disorders”) and thus produce severe phenotypic effects. These molecular studies provide a

rational basis for the pattern of transmission and clinical features that are characteristic of this variant. First,because vascular-type EDS results from mutations involving a structural protein (rather than an enzyme

protein), an autosomal dominant pattern of inheritance would be expected. Second, because blood vessels

and intestines are known to be rich in collagen type III, an abnormality of this collagen is consistent with

severe defects (e.g., spontaneous rupture) in these organs.

In two forms of EDS—arthrochalasia type and dermatosparaxis type—the fundamental defect is in the

conversion of type I procollagen to collagen. This step in collagen synthesis involves cleavage of

noncollagen peptides at the N terminus and C terminus of the procollagen molecule. This is accomplished

by N terminal–specific and C terminal–specific peptidases. The defect in the conversion of procollagen to

collagen in the arthrochalasia type has been traced to mutations that affect one of the two type I collagen

genes, COL1A1 and COL1A2 . As a result, structurally abnormal pro "1 (I) or pro "2 (I) chains that resist

cleavage of N-terminal peptides are formed. In patients with a single mutant allele, only 50% of the type I

collagen chains are abnormal, but because these chains interfere with the formation of normal collagen

helices, heterozygotes manifest the disease. By contrast, the related dermatosparaxis type is caused by

mutations in the procollagen-N-peptidase genes, essential for the cleavage of collagens. In this case the

enzyme deficiency leads to an autosomal recessive form of inheritance.

Finally, the classical type of EDS is worthy of brief mention, since molecular analysis of this variant

suggests that genes other than collagen genes may be involved in the pathogenesis of EDS. In 30% to

50% of these cases, mutations in the genes for type V collagen (COL5A1 and COL5A2 ) have been

detected.[20] Surprisingly, despite a phenotype typical of EDS, no other collagen gene abnormalities have

been found in the remaining cases.

To summarize, the common thread in EDS is some abnormality of collagen. These disorders, however, are

extremely heterogeneous. At the molecular level, a variety of defects, varying from mutations involving

structural genes for collagen to those involving enzymes that are responsible for post-transcriptional

modifications of mRNA, have been detected. Such molecular heterogeneity results in the expression of

EDS as a clinically variable disorder with several patterns of inheritance.

DISORDERS ASSOCIATED WITH DEFECTS IN RECEPTOR PROTEINS

Familial Hypercholesterolemia

Familial hypercholesterolemia is a “receptor disease” that is the consequence of a mutation in the gene encoding

the receptor for LDL, which is involved in the transport and metabolism of cholesterol . As a consequence of

receptor abnormalities there is a loss of feedback control and elevated levels of cholesterol that induce premature

atherosclerosis, leading to a greatly increased risk of myocardial infarction. [21]

Familial hypercholesterolemia is one of the most frequently occurring mendelian disorders. Heterozygotes with

one mutant gene, representing about 1 in 500 individuals, have from birth a two-fold to three-fold elevation of

plasma cholesterol level, leading to tendinous xanthomas and premature atherosclerosis in adult life ( Chapter 11



). Homozygotes, having a double dose of the mutant gene, are much more severely affected, and may have five-

fold to six-fold elevations in plasma cholesterol levels. These individuals develop skin xanthomas and coronary,

cerebral, and peripheral vascular atherosclerosis at an early age. Myocardial infarction may develop before age

20. Large-scale studies have found that familial hypercholesterolemia is present in 3% to 6% of survivors of

myocardial infarction. An understanding of this disorder requires that we briefly review the normal process of cholesterol metabolism

and transport. Approximately 7% of the body's cholesterol circulates in the plasma, predominantly in the form of

LDL. As might be expected, the amount of plasma cholesterol is influenced by its synthesis and catabolism, and

the liver plays a crucial role in both these processes ( Fig. 5-7 ). The first step in this complex sequence is the

secretion of very-low-density lipoproteins (VLDLs) by the liver into the bloodstream. VLDL particles are rich in

triglycerides, but they contain lesser amounts of cholesteryl esters. When a VLDL particle reaches the capillaries

of adipose tissue or muscle, it is cleaved by lipoprotein lipase, a process that extracts most of the triglycerides.

The resulting molecule, called intermediate-density lipoprotein (IDL), is reduced in triglyceride content and

enriched in cholesteryl esters, but it retains two of the three apoproteins (B-100 and E) present in the parent

VLDL particle (see Fig. 5-7 ). After release from the capillary endothelium, the IDL particles have one of two

fates. Approximately 50% of newly formed IDL is rapidly taken up by the liver by receptor-mediated transport.

The receptor responsible for the binding of IDL to the liver cell membrane recognizes both apoprotein B-100 and

apoprotein E. It is called the LDL receptor , however, because it is also involved in the hepatic clearance of LDL,

as described later. In the liver cells, IDL is recycled to generate VLDL. The IDL particles not taken up by the liver

are subjected to further metabolic processing that removes most of the remaining triglycerides and apoprotein E,

yielding cholesterol-rich LDL particles. It should be emphasized that IDL is the immediate and major source of

plasma LDL. There seem to be two mechanisms for removal of LDL from plasma, one mediated by an LDL

receptor and the other by a receptor for oxidized LDL (scavenger receptor), described later. Although many cell

types, including fibroblasts, lymphocytes, smooth muscle cells, hepatocytes, and adrenocortical cells, possesshigh-affinity LDL receptors, approximately 70% of the plasma LDL seems to be cleared by the liver, using a quite

sophisticated transport process ( Fig. 5-8 ). The first step involves binding of LDL to cell surface receptors, which

are clustered in specialized regions of the plasma membrane called coated pits. After binding, the coated pits

containing the receptor-bound LDL are internalized by invagination to form coated vesicles, after which they

migrate within the cell to fuse with the lysosomes. Here the LDL dissociates from the receptor, which is recycled

to the surface. In the lysosomes the LDL molecule is enzymatically degraded; the apoprotein part is hydrolyzed to

amino acids, whereas the cholesteryl esters are broken down to free cholesterol. This free cholesterol, in turn,

crosses the lysosomal membrane to enter the cytoplasm, where it is used for membrane synthesis and as a

regulator of cholesterol homeostasis. The exit of cholesterol from the lysosomes requires the action of two

proteins called NPC1 and NPC2 (see “Niemann-Pick Disease, Type C”). Three separate processes are affected

by the released intracellular cholesterol, as follows:

Cholesterol suppresses cholesterol synthesis within the cell by inhibiting the activity of the enzyme 3-hydroxy-3-

methylglutaryl coenzyme A (HMG CoA) reductase, which is the rate-limiting enzyme in the synthetic pathway

Cholesterol activates the enzyme acyl-coenzyme A : cholesterol acyltransferase, favoring esterification and

storage of excess

Cholesterol suppresses the synthesis of LDL receptors, thus protecting the cells from excessive accumulation of

cholesterol.

As mentioned earlier, familial hypercholesterolemia results from mutations in the gene specifying the receptor

for LDL. Heterozygotes with familial hypercholesterolemia possess only 50% of the normal number of high-

affinity LDL receptors, because they have only one normal gene. As a result of this defect in transport, the



catabolism of LDL by the receptor-dependent pathways is impaired, and the plasma level of LDL increases

approximately two-fold. Homozygotes have virtually no normal LDL receptors in their cells and have much

higher levels of circulating LDL. In addition to defective LDL clearance, both the homozygotes and

heterozygotes have increased synthesis of LDL. The mechanism of increased synthesis that contributes to

hypercholesterolemia also results from a lack of LDL receptors (see Fig. 5-7 ). Recall that IDL, the immediateprecursor of plasma LDL, also uses hepatic LDL receptors (apoprotein B-100 and E receptors) for its transport

into the liver. In familial hypercholesterolemia, impaired IDL transport into the liver secondarily diverts a greater

proportion of plasma IDL into the precursor pool for plasma LDL.

The transport of LDL via the scavenger receptor seems to occur at least in part into the cells of the

mononuclear phagocyte system. Monocytes and macrophages have receptors for chemically altered (e.g.,

acetylated or oxidized) LDL. Normally the amount of LDL transported along this scavenger receptor

pathway is less than that mediated by the LDL receptor–dependent mechanisms. In the face of

hypercholesterolemia, however, there is a marked increase in the scavenger receptor–mediated traffic of

LDL cholesterol into the cells of the mononuclear phagocyte system and possibly the vascular walls (

Chapter 11 ). This increase is responsible for the appearance of xanthomas and contributes to the

pathogenesis of premature atherosclerosis.

The molecular genetics of familial hypercholesterolemia is extremely complex. More than 900 mutations,

including insertions, deletions, and missense and nonsense mutations, involving the LDL receptor gene

have been identified. These can be classified into five groups ( Fig. 5-9 ): Class I mutations are relatively

uncommon, and they lead to a complete failure of synthesis of the receptor protein (null allele). Class II

mutations are fairly common; they encode receptor proteins that accumulate in the endoplasmic reticulum

because their folding defects make it impossible for them to be transported to the Golgi complex. Class III

mutations affect the LDL-binding domain of the receptor; the encoded proteins reach the cell surface but fail

to bind LDL or do so poorly. Class IV mutations encode proteins that are synthesized and transported to the

cell surface efficiently. They bind LDL normally, but they fail to localize in coated pits, and hence the bound

LDL is not internalized. Class V mutations encode proteins that are expressed on the cell surface, can bind

LDL, and can be internalized; however, the pH-dependent dissociation of the receptor and the bound LDL

fails to occur. Such receptors are trapped in the endosome, where they are degraded, and hence they fail to

recycle to the cell surface.



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28. Disenzymatic Hypoenergosis

Inherited or acquired mutational enzymatic hits involved in several biochemical pathways

(glycolysis, Beta oxidation, TCA cycle, Oxidative Phosphorylation, Transmembranetransport, Mitochondrial Ox Decarboxylation)

Glycolysis - inherited enzymatic mutations (involving muscle or erythrocyte enzymopathies)

1. Muscle - enzymatic defect (6-phosphofructokinase) results in decreased muscle phosphorylations - Evolves into a glycogen storage disease type V (McArdlov

Syn.) or type VII - pain + cramps after physical exsertion similar to ischemia

(cladicatio intermittens) - Spasm is the result from lack of ATP which is needed

to return Ca++ from sarcoplasm back into sacroplasmic reticulum.

2. Erythrocyte - contain no mitochondria so they rely on glycolysis as sole source for

energy (i.e. membrane pump activation) - Enzymatic defect pyruvate kinase stunts

glycolysis => decreases ATP production => decrease Na/K pump activity =>

creating electrolyte inbalance => H20 influx => hemolysis => anemia

Mitochondria - inherited (mother) or acquired enzymatic defect

1. Inherited - acyl - CoA dehydrogenase gene mutation => defective Beta Oxidation

of Fatty Acids => encephalopathy =>death often due to viral infection (Reye's

Syn)

" With decreased Beta Ox energy needs are taken over by glycolysis thereforeno there is no disease unless organism is subjected to decrease glycolysis, for



example in starvation. During starvation the body uses Ketone Bodies as

energy source, but due to enzymopathy within Beta oxidation the organism

cannot supplement energy demand with Ketone Bodies

1. Acuired mutational hits due to damage to Mitochondrial DNA, decrease

Cofactors or over activity of inhibitor enzymes - caused by : Toxic exposure(Cianide poisining which blocks cyto-c oxidase and thus electron transport chain)

=> ultimate result is Oxidative Uncoupling, the dissociation between Oxidation

and Phosphorylation => increaase permiability of inner Mito membrane results inloss of proton gradient => loss of driving force needed to create ATP => O2

oxidation creates Heat not energy.2. Thyroid Hormones - Hyperthyroidism => decrease energy metabolism efficiency

=> uncoupling and increase of futile cycles => same as above (hyperthermia)3. Cofactors - needed for Biochemical pathways (without them the pathways stops)

" Vit B1 - thiamin = Pyuruvate Dehydrogenase

" Riboflavin = FAD

" Niacin = NADH

29. Substrate Hypoenergosis

Basically you need materials (substrate) to build a product (energy) and without those

materials your fucked

For example - decrease in glucose ( starvation, lack of insulin, insulin resistance,

hypophosphatemia whatever the hell that is) => decrease availability for enegry production

leads to decrease ATP.

Body adapts to lack of glucose by gluconeogenisis, ketogenesis, fatty acid utilization if the

body cannot adapt then we get hypoenegosis.

Starvation - decrease in nutrients mainly glucose - body compensates with

" Liver : gluconeogenesis => glucose; Beta Ox => keton bodies

" Fat : Lipolysis (main energy source in muscles is fatty acids and KB)

" ketone bodies extremely important during starvation supply the heart and skeletal

muscle. note that high [ketone bodies] leads to toxicity

" Main hormones during starvation: glucagon (especially during hypoglycemia),

catecholamines, cortisol, and GH

" Prolonged stavration: Decreased insulin secretion => decrease influx glucose into cells,

decreased glycolysis - Increased glucagon => increased gluconeogenesis and glycolysis

1. In Fatty Tissue - the hormone activity increase the amount of Fatty

acid utilizatoin for muscles and myocardium and also produciton of

KB

2. Carnitin-acyl-transfrease 1 is key enzyme for FA oxidation - enzyme

transports acyl CoA thru inner mito membrane - enzyme depends on

carnitine (stimulatory, glucagon increase carnitine) and Malonyl CoA

(inhibitory)

3. Brain and muscle need ketone bodies to fxn during insufficiency of

Carbohydr...4. Ketosis develops due to limited glycolysis and insufficient usage of



carbohydrates ( this is not just for starvation but also hypoglycemia

(iatrogenic), Diabetes Mel.)

" Alanine is the most important substrate for Gluconeogenesis

" Breakdown of proteins for glucneo. is the main cause of death in starvation

" Hypoglycemia => hypoenergosis disrupts brain fxn, if prolonged =>

hypoglycemic coma

=> increase use of FAcids=> increase production of KBs => ketoacidosis

In Kids : decrease muscle mass

less amt. of Alanine available for gluconeogen => faster onset ketoacidosis also candevelop from vomiting, diarrhea,gluc. dysfxn

Ethanol Poisining : oxidation of ethanol => acetylaldehide => acetate (rxn catabloized by

alcohol DHase andaldehyde DHase / NAD reduced to NADH creating an increase ratio of

NADH:NAD)

During ethanol poisining increase in pyruvate creates lactate => Lactic

acidosis

developes. Since alcoholics r not likely to eat well they tend to develp

hypoglycemia

Diabetes Mel -

" decreas insulin (and glycogen used up) => not only increases KB but also decrease

the muscles ability to use them at a faster rate therefore you have a excess of KB =>

life threating

" otherwise the situation is similar to starvation but different cause

30. Hypoenergosis of the specific tissues.

BRAIN

" uses 25% glucose (majority of energy is for fxn 10% is used to keep function, 20%

O2, and 15% Heart minute volume

" Does not have big storage for glucose so anything that impedes blood flow will yeild

substrate insufficiency, not to mention hypoxia (irreversible damage can happenwithin 4-5 min)

" hypoxia damages capillary endotel => increase permeability => risk for brain oedema

" Any metabolic dysfunction ( ie - ketoacidosis, liver damage, uremia) => decrease

enegry metabolism => hypoenergosis/ coma

Heart

" need for O2 => increase bl. flow thru coronaries if malfxn (atherosclerosis) => hypoia

of myocardium

" depending on the hearts ability to adapt and the extent of the negative stim. there are

different degerees of injury from Pectoris major to MI

" ischemia => anaerobic metab used for energy => accumulation of lactic acid, loss of phosphate => pain, decr permeability/contraction, arrythmia, Vent Fib



" Chronic hypoxia => heart better able to adapt but develp hypertrophy, dilation,

fibrosis

Kidneys

" Most of the energy used for active transport

" acute ischemia, kidney react by constricting afferent arterioles => acute kidneyinsufficiency

Lungs

" Hypoxia in lungs causes vasoconstriction or arterioles => decrease PO2 in alveoli

" Cor Pulmonal, Pulmonary hypertension

Liver - centrolobular necrosis due to the anatomic arangement of blood flow through theliver there is a watershed region from the periphery to the center of the Liver Lobule

Skeletal Muscle

Hypoenergosis => muscle spasm (inorder for muscle to relax Ca needs to return tosacroplamic

reticulum via Ca++ pump which needs ATP to fxn

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• A605,*01 &'2 A/('1C

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?@BCQ>ODE CO`CO>ADA ?CI Q@ NL@A@GB= ,FKAS KG@]NOCDG@H FIN>ECOE@?DC CGH FIN>`CO@?DC AKMM@AB BF@ N>AADQDODBI >J #M

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• L65)40&(')1)0/&

7IN@L?CMG@A@?DC DA C NOCA?C #M E>GE@GBLCBD>G e :=! ?$a<) Ze !=;U ??>O<)[= ,F@ ?CV>L ECKA@ DA L@GCO JCDOKL@=1I?NB>?A DGEOKH@ FIN>B@GAD>GS L@ANDLCB>LI H@NL@AAD>GS CGH ECLHDCE CLL@AB=

%DCMG>ADA DA QI A@LK? #M O@P@OA= ,L@CB?@GB DGEOKH@A &/ CH?DGDABLCBD>G >J 'C MOKE>GCB@ CGH N>AADQOI JKL>A@?DH@h

F@?>HDCOIADA ECG Q@ F@ONJKO DG A@P@L@ ECA@A=1I?NB>?CBDE FIN@L?CMG@A@?DC DA JCDLOI KGE>??>G= &B >EEKLA ?>AB E>??>GOI DG NCBD@GBA bDBF L@GCO JCDOKL@ CJB@L

DGM@ABD>G >J #M_E>GBCDGDGM HLKMAS AKEF CA CGBCEDHA >L NKLMCBDP@A=

• A605,*01= A/('1= &'2 E/&('*1/1

(B NOCA?C #M E>GE@GBLCBD>GA >J U B> !; ?$a<) Z:=U B> U ??>O<)[S BF@ $'4 AF>bA NL>O>GMCBD>G >J BF@ 60 DGB@LPCOS

bDH@GDGM >J BF@ 801 E>?NO@]S CGH DGEL@CA@H ,_bCP@ C?NODBKH@= %@@N B@GH>G L@JO@]@A HDACNN@CL CA BF@ NOCA?C #M

O@P@O CNNL>CEF@A !; ?$a<) ZU=; ??>O<)[h FIN>B@GAD>GS L@ANDLCB>LI H@NL@AAD>GS CGH GCLE>ADA H@P@O>N bDBF DGEL@CADGM

FIN@L?CMG@A@?DC= 'CLHDCE CLL@AB ?CI >EEKL bF@G QO>>H #M O@P@OA @]E@@H !: B> !U ?$a<) ZW=; B> X=U ??>O<)[=

7IN@L?CMG@A@?DC DA HDCMG>A@H bF@G A@LK? #M O@P@OA CL@ e :=! ?$a<) Ze !=;U ??>O<)[=

:= 6F>ANFCB@d

6F>ANF>LKA DA >G@ >J BF@ ?>AB CQKGHCGB @O@?@GBA DG BF@ FK?CG Q>HI= #>AB NF>ANF>LKA DG BF@ Q>HI DA E>?NO@]@H

bDBF >]IM@G CA NF>ANFCB@ Z62T[= (Q>KB YUw >J BF@ L>KMFOI U;; B> X;; M >J 62 T DG BF@ Q>HI DA E>GBCDG@H DG Q>G@S

bF@L@ DB DA CG D?N>LBCGB E>GABDBK@GB >J FIHL>]ICNCBDB@= &G A>JB BDAAK@AS 62T DA ?CDGOI J>KGH DG BF@ DGBLCE@OOKOCL

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NF>ANF>ODNDHA= 62T DA COA> DGP>OP@H DG C@L>QDE CGH CGC@L>QDE @G@LMI ?@BCQ>ODA?= 05' :SR_HDNF>ANF>MOIE@LCB@ Z:SR_

%64[ NOCIA C ELKEDCO L>O@ DG 2: H@ODP@LI B> BDAAK@= (H@G>ADG@ HDNF>ANFCB@ Z(%6[ CGH (,6 E>GBCDG 62T CGH KA@

EF@?DECO Q>GHA Q@Bb@@G 62T ML>KNA B> AB>L@ @G@LMI= &G>LMCGDE 62T DA C ?CV>L DGBLCE@OOKOCL CGD>G QKB DA COA> NL@A@GB DG

NOCA?C= ,F@ G>L?CO NOCA?C DG>LMCGDE 62T E>GE@GBLCBD>G DG CHKOBA LCGM@A JL>? :=U B> T=U ?M<H) Z;=Y! B> !=TU

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62T QCOCGE@= 62T H@NO@BD>G ECG >EEKL DG PCLD>KA HDA@CA@A CGH G>L?COOI L@AKOBA DG E>GA@LPCBD>G >J 62 T QI BF@ `DHG@IA=

5>G@ 62T A@LP@A CA C L@A@LP>DLS bFDEF ECG QKJJ@L EFCGM@A DG NOCA?C CGH DGBLCE@OOKOCL 62 T=

• Lb@[@L[A@L:DJZN:

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b@C`G@AAS L@ANDLCB>LI JCDOKL@S CGH F@CLB JCDOKL@h A@D^KL@A CGH E>?C ECG >EEKL= %DCMG>ADA DA QI A@LK? 62T O@P@OA=,L@CB?@GB E>GADABA >J 62T AKNNO@?@GBCBD>G=

• J,/*7*(6 &'2 @&,%*5%61/*7*(6

7IN>NF>ANFCB@?DC >EEKLA DG :w >J F>ANDBCOD^@H NCBD@GBA QKB DA ?>L@ NL@PCO@GB DG E@LBCDG N>NKOCBD>GA Z@MS DB >EEKLA

DG KN B> !;w >J F>ANDBCOD^@H NCBD@GBA bDBF COE>F>ODA?[= 7IN>NF>ANFCB@?DC FCA GK?@L>KA ECKA@AS QKB EODGDECOOI

ADMGDJDECGB FIN>NF>ANFCB@?DC >EEKLA DG L@OCBDP@OI J@b EODGDECO A@BBDGMAS AKEF CA BF@ L@E>P@LI NFCA@ >J HDCQ@BDE`@B>CEDH>ADAS CEKB@ COE>F>ODA?S CGH A@P@L@ QKLGA= 7IN>NF>ANFCB@?DC ?CI COA> >EEKL DG NCBD@GBA HKLDGM L@J@@HDGM

CJB@L NL>O>GM@H ?COGKBLDBD>GS CGH DG A@P@L@ EFL>GDE L@ANDLCB>LI CO`CO>ADA=

(EKB@ FIN>NF>ANFCB@?DC bDBF NOCA?C 62T | ! ?M<H) Z| ;=R: ??>O<)[ DA ?>AB >JB@G ECKA@H QI BLCGAE@OOKOCL AFDJBA >J

62TS >JB@G AKN@LD?N>A@H >G EFL>GDE 62T H@NO@BD>G=

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HDA>LH@LAS AKEF CA FIN>?CMG@A@?DC CGH FIN>`CO@?DCh BF@>NFIOODG@ DGB>]DECBD>Gh CGH O>GM_B@L? HDKL@BDE

CH?DGDABLCBD>G= 1@P@L@ EFL>GDE FIN>NF>ANFCB@?DC KAKCOOI L@AKOBA JL>? C NL>O>GM@H G@MCBDP@ 62 T QCOCGE@= 'CKA@A

DGEOKH@ EFL>GDE ABCLPCBD>G >L ?COCQA>LNBD>GS @AN@EDCOOI DJ E>?QDG@H bDBF P>?DBDGM >L E>ND>KA HDCLLF@CS >L O>GM_B@L?

DGM@ABD>G >J OCLM@ C?>KGBA >J 62T_QDGHDGM COK?DGK?S KAKCOOI DG BF@ J>L? >J CGBCEDHA= &GM@ABD>G >J COK?DGK? DA

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DG NCBD@GBA bDBF @GH_ABCM@ L@GCO HDA@CA@=

• A605,*01 &'2 A/('1C

(OBF>KMF FIN>NF>ANFCB@?DC KAKCOOI DA CAI?NB>?CBDES CG>L@]DCS ?KAEO@ b@C`G@AAS CGH >AB@>?COCEDC ECG >EEKL DG

A@P@L@ EFL>GDE H@NO@BD>G= 1@LD>KA G@KL>?KAEKOCL HDABKLQCGE@A ?CI >EEKLS DGEOKHDGM NL>ML@AADP@ @GE@NFCO>NCBFIS

E>?CS CGH H@CBF= ,F@ ?KAEO@ b@C`G@AA >J NL>J>KGH FIN>NF>ANFCB@?DC ?CI Q@ CEE>?NCGD@H QI LFCQH>?I>OIADAS

@AN@EDCOOI DG CEKB@ COE>F>ODA?= 7@?CB>O>MDE HDABKLQCGE@A >J NL>J>KGH FIN>NF>ANFCB@?DC DGEOKH@ F@?>OIBDE CG@?DCS

H@EL@CA@H L@O@CA@ >J 2: JL>? F@?>MO>QDGS CGH D?NCDL@H O@K`>EIB@ CGH NOCB@O@B JKGEBD>G=

• Lb@J<@L[A@L:DJZN:

7IN@LNF>ANFCB@?DC DA A@LK? NF>ANFCB@ Z62T[ E>GE@GBLCBD>G e T=U ?M<H) Ze !=TW ??>O<)[= 'CKA@A DGEOKH@ EFL>GDE

L@GCO JCDOKL@S FIN>NCLCBFIL>DHDA?S CGH ?@BCQ>ODE >L L@ANDLCB>LI CEDH>ADA= 'ODGDECO J@CBKL@A ?CI Q@ HK@ B>

CEE>?NCGIDGM FIN>ECOE@?DC CGH DGEOKH@ B@BCGI= %DCMG>ADA DA QI A@LK? 62T= ,L@CB?@GB DGEOKH@A L@ABLDEBD>G >J 62T

DGBC`@ CGH CH?DGDABLCBD>G >J 62T_QDGHDGM CGBCEDHAS AKEF CA 'C ECLQ>GCB@:



7IN@LNF>ANFCB@?DC M@G@LCOOI L@AKOBA JL>? C H@EL@CA@ DG L@GCO @]EL@BD>G >J 62 T= (HPCGE@H L@GCO DGAKJJDED@GEI Z4*0 |

:; ?)<?DG[ L@HKE@A @]EL@BD>G AKJJDED@GBOI B> DGEL@CA@ NOCA?C 62T= %@J@EBA DG L@GCO @]EL@BD>G >J 62T DG BF@ CQA@GE@ >J

L@GCO JCDOKL@ COA> >EEKL DG NA@KH>FIN>NCLCBFIL>DHDA? CGH FIN>NCLCBFIL>DHDA?= 7IN@LNF>ANFCB@?DC ECG COA> >EEKL

bDBF @]E@AADP@ >LCO 62T CH?DGDABLCBD>G CGH >EECAD>GCOOI bDBF >P@L^@CO>KA KA@ >J @G@?CA E>GBCDGDGM 62 T=

7IN@LNF>ANFCB@?DC >EECAD>GCOOI L@AKOBA JL>? C BLCGAE@OOKOCL AFDJB >J 62 T DGB> BF@ @]BLCE@OOKOCL ANCE@ BFCB DA A> OCLM@

BFCB BF@ L@GCO @]EL@B>LI ECNCEDBI DA >P@LbF@O?@H= ,FDA >EEKLA ?>AB JL@aK@GBOI DG HDCQ@BDE `@B>CEDH>ADA ZH@ANDB@ B>BCO

Q>HI 62T H@NO@BD>G[S ELKAF DGVKLD@AS CGH G>GBLCK?CBDE LFCQH>?I>OIADA CA b@OO CA DG >P@LbF@O?DGM AIAB@?DE

DGJ@EBD>GA CGH BK?>L OIADA AIGHL>?@= 7IN@LNF>ANFCB@?DC COA> NOCIA C ELDBDECO L>O@ DG BF@ H@P@O>N?@GB >J A@E>GHCLI

FIN@LNCLCBFIL>DHDA? CGH L@GCO >AB@>HIABL>NFI DG NCBD@GBA >G HDCOIADA= )CABOIS FIN@LNF>ANFCB@?DC ECG Q@ ANKLD>KA DG

ECA@A >J FIN@LNL>B@DG@?DC Z?KOBDNO@ ?I@O>?C >L fCOH@GABL•?uA ?CEL>MO>QKODG@?DC[S FIN@LODNDH@?DCS F@?>OIADAS >L

FIN@LQDODLKQDG@?DC=

• A605,*01 &'2 A/('1C

#>AB NCBD@GBA bDBF FIN@LNF>ANFCB@?DC CL@ CAI?NB>?CBDES COBF>KMF AI?NB>?A >J FIN>ECOE@?DCS DGEOKHDGM B@BCGIS

ECG >EEKL DJ E>GE>?DBCGB FIN>ECOE@?DC DA NL@A@GB= 1>JB_BDAAK@ ECOEDJDECBD>GA CL@ E>??>G DG NCBD@GBA bDBF EFL>GDE L@GCO

JCDOKL@S @AN@EDCOOI DJ BF@ NOCA?C 'C € 62T NL>HKEB DA EFL>GDECOOI e X;=

UR_ 6CBF>NFIAD>O>MDECO *CEB>LA >J BF@ (EDH_5CA@ D?QCOCGE@Ad

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OD?DBA >J N7 PCOK@A LCGMDGM JL>? X=RW KN B> X=TT= 6FIAD>O>MDECOOIS P@G>KA QO>>H E>GBCDGA FDMF@L E>GE@GBLCBD>G >J

FIHL>M@G D>GA BFCG BF@ CLB@LDCO H>@A HK@ B> E>GE@GBLCBD>G MLCHD@GB >J ?@BCQ>ODB@A=

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?CAA aKCGBDBI >J FIHL>M@G D>G H>G>LA ZCEDHA[ DG L@OCBD>G B> BF@ aKCGBDBI >J @O@EBL>G CEE@NB>LA ZQCA@A[= 'IB>NOCA?DE

N7 PCOK@ DA W=\_X=:h O>b@L PCOK@A CL@ DG E@OOA bDBF FDMF@L ?@BCQ>ODE BKLG>P@L LCB@ ZG@KL>GA[= %K@ B> H@AE@GHDGM

CEDHDBI MLCHD@GB Q@Bb@@G BF@ DGBLCE@OOKOCL CGH BF@ @]BLCE@OOKOCL E>?NCLB?@GB BF@L@ DA C E>GABCGB G@B @JJOK] >J CEDH

B>bCLHA BF@ @]BLCE@OOKOCL ANCE@=

(EDH_QCA@ ABCB@ >J BLCGAE@OOKOCL E>?NCLB?@GBA DA L@MKOCB@H QI CEBDP@ BLCGAN>LB >J CEDHA CGH QCA@A >KB >J BF@

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E>?N>ADBD>G >J BLCGAE@OOKOCL E>?NCLB?@GB ECG ECKA@ AIAB@?DE CEDH_QCA@ HDA>LH@LA DG BF@ >LMCGDA? Z

CEDH>ADA<CO`CO>ADA[= %K@ B> N>b@LJKO E>?N@GACB>LI ?@EFCGDA?AS BDAAK@A ECG KGH@LM> CEDH>ADA >L CO`CO>ADA bDBF>KB

?CGDJ@ABDGM CECH@?DC >L CO`CO@?DC=

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>J B@BCGI[=

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UT_ 0@ANDLCB>LI CEDH>ADA CGH CO`CO>ADAd

• 0@ANDLCB>LI CEDH>ADA

&GEL@CA@ DG 6C'2: CGH O>b N7 DG CLB@LDCO QO>>HS bDBF G>L?CO L@GCO JKGEBD>G QDECLQ>GCB@ E>GE@GBLCBD>G DGEL@CA@A=

,F@ QCADE ECKA@ >J L@ANDLCB>LI CEDH>ADA DA FIN>P@GBDOCBD>G= %@N@GHDGM >G BF@ LCB@ >J H@P@O>N?@GBS A@P@LDBI CGH

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ZAODMFBOI H@EL@CA@H N7 bDBF FDMF QDECLQ>GCB@ E>GE@GBLCBD>G[=

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:= (KB>D??KG@ %DA@CA@ c (KB> CGBDQ>HD@A CMCDGAB F>L?>G@ L@E@NB>LA Z4LCP@Ai HDA@CA@[R= 1>?CBDE ?KBCBD>G CGH BK?>L

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!= 60&#(0- c HIAJKGEBD>G >J BF@ MOCGH

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Q[ 1@E>GHCLI FIN>NDBKDBCLDA? c FDMF@L O@P@OA CJJ@EB@H ZFIN>BFCOC?DE BK?>LA[

:= 7-6$01$'0$,&2. Z7-6$06&,+&,(0&1#[d,F@ ?>AB E>??>G ECKA@ DA C NDBKDBCLI MOCGH BK?>L CJJ@EBDGM CGB@LD>L O>Q@ Z?>AB >JB@GCH@G>?C DGP>OPDGM >GOI >G@ F>L?>G@[

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Hormone Excess of secretion Deficit of secretion

GROWTH

HORMONE (IGF-I)

Somatotropic adenoma:

Acromegaly, gigantism, abnormal

glucose tolerance, diabetes mellitus

Pituitary Dwarfism (nanism)

PROLACTIN Prolactinoma:

Amenorrhea, infertility, galactorrhea

Failure of postpartum lactation

ACTH Corticotroph adenoma:

Cushing disease, Nelson syndrome

Secondary hypofunction of adrenal gland

TSH Secondary hyperthyroidism Secondary hypothyroidism

LH/FSH Premature ubert Secondar h o onadism



X9# D%64*/2 (7&'2 261+-'.,/*'

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3Q L65*,%64*/2/10d!= 60&#(0- Z7CAFD?>B> HDA@CA@ ZCKB>D??KG@[[ c AN>LCHDE EL@BDGDA? >L VKP@GDO@FIN>BFIL>DHDA?:= 1$'2.%(0- Z6DBKDBCLI >L FIN>BFCOC?DE JCDOKL@[C[ &. (%+),1d ?I]@H@?CS FIN@LEF>O@AB@L>O@?DC ZHK@ B> H@EL@CA@ >J H@MLCHCBD>G[S E>OHDGB>O@LCGE@S QLCHIECLHDCS E>GABDNCBD>GS JCBDMK@Q[ &.'7&)%0$.d EL@BDGDA? ZCJB@L QDLBF[S VKP@GDO@ FIN>BFIL>DHDA? ZDG >OH@L EFDOHL@G[

A/057) O'*' ,*W/.Q (*/,)4C &B FCNN@GA bF@G BF@L@ DA E>?N@GACB>LI DGEL@CA@ >J ,17A@EL@BD>GS O@CHDGM B> CG DGEL@CA@ DG JKGEBD>GCO ?CAA >J BF@ BFIL>DHS DG >LH@L B> >P@LE>?@ BF@F>L?>G@ H@JDED@GEI= ,F@ ?>AB D?N>LBCGB ECKA@ DA D>HDG@ H@JDED@GEI DG J>>H CGH bCB@L=

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O>AA[S L@NL>HKEBDP@ EFCGM@ CGH PDLDOD^CBD>G

:= #(&.)- ()%21,$02.$ 1$'0$,&2.dC[ 6LD?CLI COH>AB@L>GDA? Z'>GG AIGHL>?@[ c HK@ B> COH>AB@L>G@_A@EL@BDGM CH@G>?C >LCHL@G>E>LBDECO FIN@LNOCADC=

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Q[ 1@E>GHCLI COH>AB@L>GDA? c &B FCNN@GA HK@ B> G>G `DHG@I ECKA@A&B L@AKOBA DG DGEL@CA@H O@P@OA >J NOCA?C L@GDGR= #(&.)- (.%024$. 1$'0$,&2. Z(%0$.24$.&,() 1-.%02#$[dC[ '>GM@GDBCO (HL@GCO 7IN@LNOCADC Z'(7[c,F@ ?KBCBD>G DGP>OP@ BF@ M@G@A @GE>HDGM >G@ >JBF@ FIHL>]IOCA@A DGP>OP@H DG BF@ AIGBF@ADA >J AB@L>DHA ZG> E>LBDA>O AIGBF@AD^@H CGH COO BF@E>LBDA>O NL@EKLA>LA CL@ AFKGB@H DGB> BF@ NL>HKEBD>G >J AB@L>DHA[=

%K@ B> OCE` >J E>LBDA>OS BF@ NL>HKEBD>G >J NDBKDBCLI (',7 Q@E>?@A KGEF@E`@H= ,F@ FDMF O@P@O>J (',7 ECKA@A CHL@GCO FIN@LNOCADC CGH DGEL@CA@ >J CGHL>M@G F>L?>G@A=Q[ (HL@G>M@GDBCO AIGHL>?@ c %K@ B> CHL@GCO E>LBDECO BK?>L >L E>LBDECO FIN@LNOCADC=&B ECKA@A PDLDOD^CBD>G DG b>?@G ZFDLAKBDA?S CEG@S P>DE@ H@@N@GDGMS QL@CAB CBL>NFIS EODB>LDAML>bBFS CGH C?@G>LLF@C[=

3Q L65*+-'.,/*'C

!= 60&#(0-_('+,$d &B ECG >EEKL CJB@L CGI ABL@AA Z(EKB@ CHL@GCO ELDADA[S LCNDH bDBFHLCbCO >J AB@L>DHAS?CAADP@ CHL@GCO F@?>LLFCM@ ZfCB@LF>KA@_*LDH@LDEFA@G AIGHL>?@[=_'702.&' Z(HHDA>GiA HDA@CA@[d HK@ B> CKB>D??KG@ CHL@GCODBDAS >L DGJ@EBD>GA ZBKQ@LEKO>ADASJKGMDS (&%1[S ?@BCABCBDE G@>NOCA?A ZOKGMS QL@CAB ECLEDG>?C[=&B L@AKOBA DG EFL>GDE DGAKJJDED@GEI >J MOKE>E>LBDE>DHA ZO>AA >J CNN@BDB@ CGH b@DMFB O>AASb@C`G@AA[S ?DG@LCO>E>LBDE>DHA ZFIN>GCBL@?DCS FIN@L`CO@?DCS ?@BCQ>ODE CEDH>ADA[ CGHCGHL>M@GA ZO>AA >J CL?NDB CGH NKQDE FCDLDG@AA DG b>?@G[h DGEL@CA@ >J (',7 CGH p_#17ZFIN@LNDM?@GBCBD>G[:= 1$'2.%(0- c(',7 H@JDED@GEI ZFIN>BFCOC?KA >L NDBKDBCLI HDA>LH@LA[=&B L@AKOBA DG H@EL@CA@ A@EL@BD>G >J MOKE>E>LBDE>DHAS FIN>GCBL@?DC bDBF>KB FIN@L`CO@?DC ZHK@B> H@JDEDB >J E>LBDA>O CGH DGEL@CA@ >J (%7 A@EL@BD>G[S CGH G> FIN@LNDM?@GBCBD>G=

X># @:<:DLb<[NE Pa:SE EbAGcS$DN[S

&Q L65)45&4&,%64*/2/10C

!= 60&#(0- c (KB>G>?>KAS AN>GBCG@>KA >P@LNL>HKEBD>G >J 6,7 ZCH@G>?CS NLD?CLIFIN@LNOCADCS ECLEDG>?C[=&B L@AKOBA DG FIN@LECOE@?DCS G>L?CO >L H@EL@CA@H NF>ANFCB@?DCS FIN@LECOEDKLDCS

FIN@LNF>ANFCBKLDC'ODGDECO ?CGDJ@ABCBD>GAdC[ 6CBF>O>MDE @JJ@EBA >J FIN@LECOE@?DC c 4CABL>DGB@ABDGCO HDABKLQCGE@AS '.1 COB@LCBD>GASG@KL>?KAEKOCL CQG>L?CODBD@AQ[ $JJ@EB >J FIN@LECOE@?DC >G `DHG@IA c nDHG@I AB>G@A J>L?CBD>G ZG@NFL>ODBFDCADA[SECOEDJDECBD>G >J BF@ L@GCO DGB@LABDBDK? CGH BKQKO@A ZG@NFL>ECOEDG>ADA[E[ 1`@O@BCO EFCGM@ c &GEL@CA@H CEBDPDBI >J >AB@>EOCABA CGH >AB@>QOCABA Z>AB@DBDA JDQL>AC EIABDEC[:= 1$'2.%(0- c (GI E>GHDBD>GA CAA>EDCB@H bDBF C EFL>GDE H@NL@AAD>G DG A@LK? ECOEDK? O@P@OZEFL>GDE L@GCO JCDOKL@S PDBC?DG % H@JDED@GEIS L@HKE@H ECOEDK? DGBC`@ >L CQA>LNBD>G[=R= ,$0,&(0- c '>?NODECBD>GA >J L@GCO JCDOKL@ ECKADGM NCLCBFIL>DH MOCGHA B> Q@E>?@CKB>G>?>KA CGH KGL@AN>GADP@ B> G>L?CO NFIAD>O>MDE ABD?KOD=T= 61$+%27-6$06(0(,7-02&%&1# Z@EB>NDE A@EL@BD>G >J 6,7[ c ?CODMGCGB BK?>L ZOKGMS`DHG@IS ODP@LS NCGEL@CA[=

3Q L65*5&4&,%64*/2/10C

!= 60&#(0- c %K@ B> AKLMDECO CQOCBD>G >J NCLCBFIL>DH MOCGHAS CKB>D??KG@FIN>NCLCBFIL>DHDA?S E>GM@GDBCO CQA@GE@=,F@ FIN>ECOE@?DC O@CHA B> DGEL@CA@H G@KL>?KAEKOCL DLLDBCQDODBIS DGEL@CA@H DGBLC ELCGDCONL@AAKL@ CGH A@D^KL@AS CGH FIN@LNF>ANFCB@?DC=:= 1$'2.%(0- c FIN@LECOE@?DC

X?# P[S:E:a EbAGcS$DN[S

"# D)1,/1

&Q L65*(*'&2/10C

!= 7IN@LM>GCH>BL>NDE ZNLD?CLI[ c %K@ B> CQG>L?CO B@ABDEKOCL H@P@O>N?@GB=&B L@AKOBA DG B@ABDA CBL>NFIS DGCH@aKCB@ NL>HKEBD>G >J CGHL>M@GA ZAIGHL>?@ >J B@ABDEKOCL

J@?DGD^CBD>G[:= 7IN>M>GCH>BL>NDE ZA@E>GHCLI[ c %@J@EB DG M>GCH>BL>NDG NL>HKEBD>G >L H@J@EB DG



FIN>BFCOC?DE E>GBL>OS HK@ B> DGEL@CA@H A@EL@BD>G >J E>LBDA>O c %@OCI@H NKQ@LBI ZDG EFDOHL@G[>L AB@LDODBI ZDG CHKOBA[3Q L65)4(*'&2/10C

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,F@ ?@EFCGDA?A bFDEF NL>B@EB BF@ FK?CG J@BKA ZbFDEF DA E>GADH@L@H {G>G_A@OJ{[ JL>?CBBCE` QI BF@ D??KG@ AIAB@?S CL@ NCLBDEKOCLOI DGB@L@ABDGM= (OBF>KMF G> E>?NL@F@GADP@@]NOCGCBD>G FCA @?@LM@H B> @]NOCDG BFDA ?IAB@LD>KAS CGH >JB@G L@N@CB@HS OCE` >JL@V@EBD>GS Bb> EOCAADECO L@CA>GA ?CI @]NOCDG F>b BF@ J@BKA DA B>O@LCB@H= ,F@ JDLAB DA BFCBBF@ J@BKA >EEKND@A C N>LBD>G >J BF@ Q>HI NL>B@EB@H QI C G>G_D??KG>O>MDECO QCLLD@LS BF@KB@LKAS bFDEF BF@ D??KG@ AIAB@? H>@A G>B L>KBDG@OI NCBL>O= ,F@ A@E>GH DA BFCB BF@ J@BKADBA@OJ ?CI NL>?>B@ O>ECO D??KG>AKNNL@AACGB DG BF@ ?>BF@LS N@LFCNA QI C NL>E@AA >JCEBDP@ GKBLD@GB H@NO@BD>G= ( ?>L@ ?>H@LG @]NOCGCBD>G J>L BFDA DGHKEBD>G >J B>O@LCGE@ DABFCB AN@EDJDE MOIE>NL>B@DGA @]NL@AA@H DG BF@ KB@LKA HKLDGM NL@MGCGEI AKNNL@AA BF@KB@LDG@ D??KG@ L@AN>GA@=_,F@ J-,%)4/&' G),*)0346*'/. E)+)'1) A61,)0 O)-FGJEAQ DA C FIN>BF@BDECO ?>H@OH@AELDQDGM C ?@BF>H QI bFDEF D??KG@ AIAB@?A CL@ ECNCQO@ >J L@E>MGD^DGM CHHDBD>GCOABCB@A >J L@OCB@HG@AA OD`@ {>bG AN@ED@A{ AKEF CA DA >QA@LP@H DG ?CB@LGCO B>O@LCGE@ >J CL@OCB@H J@BKA,F@ QCADE NL@?DA@ >J BF@ @K_*$%1 FIN>BF@ADA DA BFCB Q>BF A>OKQO@ CGH E@OO AKLJCE@CAA>EDCB@H MOIE>NL>B@DGAS NL@A@GB DG BF@ L@NL>HKEBDP@ AIAB@? CGH @]NL@AA@H >G MC?@B@ASAKNNL@AA CGI N>B@GBDCO D??KG@ L@AN>GA@AS CGH DGFDQDB L@V@EBD>G >J BF@ J@BKAy!z= ,F@ @K_*$%1 ?>H@O JKLBF@L AKMM@ABA BFCB AN@EDJDE ECLQ>FIHLCB@ A@aK@GE@A Z>ODM>ACEEFCLDH@A[CL@ E>PCO@GBOI ODG`@H B> BF@A@ D??KG>AKNNL@AADP@ MOIE>NL>B@DGA CGH CEB CA JKGEBD>GCOML>KNA BFCB AKNNL@AA BF@ D??KG@ AIAB@?=

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• (OO>D??KGDBI AF>KOH G>B Q@ E>GJKA@H bDBF &-,*/00-'/,6 DG bFDEF BF@ Q>HIuA D??KG@AIAB@? CBBCEÀ DBA >bG E@OOAS bDBF>KB Q@DGM NL>P>`@H >L DGJOK@GE@H QI AKQABCGE@A >LE@OOA JL>? CG>BF@L ?@?Q@L >J BF@ AC?@ AN@ED@A=

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• :77*&',/()'VN1*&',/()' DA CG CGBDM@GDE AKQABCGE@ NL@A@GB DG A>?@ ?@?Q@LA >J C

(5%.2%( CGH ECNCQO@ >J ABD?KOCBDGM CGBDQ>HI NL>HKEBD>G 2- +6"(% 3%3*%#( "E +6% (,3%(5%.2%( +6,+ 4,.1 2+ = $]C?NO@A DGEOKH@ QO>>H ML>KN CGBDM@GA >L #CV>L 7DAB>E>?NCBDQDODBI(GBDM@GA ZZL$ &',/()'1[ S DG 7K?CGA #7' CGBDM@GA CL@ `G>bG CA 7K?CG )@K`>EIB@(GBDM@GA ZLa:[=

• 1> DJ CG COO>CGBDM@G DA NL@A@GB@H B> C ?@?Q@L >J BF@ AC?@ AN@ED@A BFCB H>@A G>B FCP@ BF@COO>CGBDM@GS DB bDOO Q@ L@E>MGD^@H CA J>L@DMG=

• (OO>CGBDM@GA CL@ BF@ NL>HKEBA >J N>OI?>LNFDE M@G@A=

• ZL$ &',/()'1 CL@ E@OO AKLJCE@ MOIE>NL>B@DGA ECLLD@H >G BF@ AKLJCE@ >J COO Q>HI E@OOASbFDEF CL@ DGP>OP@H DG CGBDM@G L@E>MGDBD>G DG D??KG@ L@AN>GA@ CGH DG COO>D??KGDBI CL@

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(OO>D??KGDBI ECG >EEKL DG BF@d

!= L@EDND@GB CJB@L BLCGAJKAD>GA >J JOKDHA AKEF CA QO>>H >L NOCA?C=:= L@EDND@GB CJB@L COO>MLCJBA ZMLCJBA[=R= J@BKAS CJB@L ?CB@LGCO CGBDQ>HD@A FCP@ NCAA@H BFL>KMF BF@ NOCE@GBC DGB> BF@ J@BKA=

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• fDBF L@AN@EB B> BF@ aKCGBDBI >J L@CEBDP@ E@OOA DG BF@ NLD?CLI CGBDM@G @GE>KGB@LS L@CEBD>GB> COO>CGBDM@GA DA !S;;; B> !;S;;; BD?@A ABL>GM@L BFCG BF@ L@CEBD>G B> ABCGHCLH GCBKLCO

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:= *>L @]C?NO@ F@CLB CGH `DHG@I BLCGANOCGBA E>GBCDG ?CDGOI #7' EOCAA & CGBDM@GA= 1>L@V@EBD>G QI F>AB DA b@C` Q@ECKA@ ,F DA ABD?KOCB@H b@CÒI=

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D??KG@ E@OOA AKEF CA ,E E@OOA= ,F@A@ EIB>B>]DE , E@OOA QDGH B> #7' EOCAA & CGBDM@GA >J BF@H>G>L BDAAK@ CGH H@ABL>I DB= ,FDA DA BF@ NLDGEDNO@A >J QIABCGH@L O@K`>EIB@ @JJ@EB=

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!= 7>AB<0@EDND@GB >J BF@ G>G OI?NFCBDE BDAAK@ H@P@O>NA F>AB P@LAKA MLCJB L@CEBD>GZ7/40[S bF@L@ FDA D??KG@ AIAB@? CBBCEÀ BF@ H>G>L BDAAK@= 'CKA@A L@V@EBD>G >J H>G>LBDAAK@<>LMCG=

:= 4LCJB P@LAKA 7>AB L@CEBD>G Z4/70[ c BFDA ?CGDJ@ABA DG D??KG>AKNNL@AA@H F>ABAbF> CL@ L@EDND@GB >J Q>G@ ?CLL>b BLCGANOCGB >L QO>>H BLCGAJKAD>G= &G BF@A@ DGABCGE@ABF@ MLCJB E>GBCDGA D??KG>E>?N@B@GB E@OOA BFCB BF@G CBBCE` BF@ F>AB= 'CKA@A ?KOBDNO@>LMCG JCDOKL@=



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(EKB@ &GJOC??CB>LI L@AN>GA@ DA C LCNDH L@AN>GA@ B> DGVKLI >L ?DEL>Q@A CGH >BF@LJ>L@DMG AKQABCGE@A BFCB DA H@ADMG@H B> H@ODP@L BF@A@ QCH Q>IA_ )@K`>EIB@A CGH 6OCA?C6L>B@DGA_ B> BF@ ADB@A >J DGVKLI=

,FL@@ NFCA@A >J CG CEKB@ DGJOC??CB>LI L@CEBD>G ZBFCB ECG Q@ NO>BB@H >G C MLCNF[d!= 6FCA@ >J &GEL@CA@ Z1BCHDK? &GEL@?@GB[ _ H>?DGCGE@ >J NL>_DGJOC??CB>LI NL>E@AA@ACEBDPCB@H QI CEBD>G >J C NL>DGJOC??CB>LI G>]C=

:= ,F@ N@C`<EOD?C] Z(E?@AS 1BCHDK? *CABDMDD[ c 6L>_DGJOC??CB>LI NL>E@AA@A AKQADH@ CBBF@ EOD?C] CGH CGBD_DGJOC??CB>LI NL>E@AA@A DGB@GADJI=

R= %@AE@GHDGM NFCA@ Z1BCHDK? %@EL@?@GB[ _ CGBD_DGJOC??CB>LI NL>E@AA@A CL@ BF@NL@PCO@GB NL>E@AA@A=

1FCN@ >J BF@ EKLP@ NL>HKE@H QI BF@A@ BFL@@ NFCA@A DA H@N@GH@GB >G BF@ >LMCGDA?iAL@CEBDPDBI= ,FDA EKLP@ DA KA@H B> H@B@L?DG@ BF@ EODGDECO ?CGDJ@ABCBD>G >J DGJOC??CB>LIL@CEBD>Gh Q@ DB >G@ >J BF@ J>OO>bDGMd FIN@LL@CEBDPDBIS G>L?>L@CEBDPDBI >L FIN>L@CEBDPDBI1@@ JDM=!W_Th N=!! Z>J FCGH>KB[h 'FCNB@L !WS &GJOC??CBD>GS 6CBF>NFIAD>O>MIS 3= n>PCE=5CADE L@CEBDP@ NCBB@LGA >J CEKB@ O>ECO DGJOC??CBD>Gd

!= &GJDOBLCBD>G bDBF NL>_DGJOC??CB>LI E@OOA CGH BF@DL ABD?KOCBD>G=

:= (EBDPCBD>G >J C?NODJIDGM QD>EF@?DECO NL>_DGJOC??CB>LI ?@EFCGDA?A=

R= 'FCGM@A PCAEKOCL N@L?@CQDODBI CGH L@ADABCGE@=

T= #>L@ >L O@AA COB@L@H BDAAK@ CLEFDB@EBKL@ bDBF EFCGM@H JKGEBD>G >J BF@ DGJOC?@H BDAAK@=



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• %DJJ@L@GB G>]C ECG A>?@BD?@A BLDMM@L DH@GBDECO @O@?@GBCLI ?@EFCGDA?A=

• .>]C DA CG CM@GB ECNCQO@ >J @]@LBDGM C FCL?JKO @JJ@EB >G BF@ Q>HI=

5@O>b DA C ODAB >J BF@A@ @BD>O>MDECO JCEB>LAd([ $]>M@G>KA G>]C@d!= &GJ@EBD>G CGH &GJ@ABCBD>G:= &>GD^CBD>G LCHDCBD>GR= +OBLCPD>O@B LCHDCBD>GT= ,F@L?CO LCHDCBD>GU= #@EFCGDECO BLCK?CW= 'F@?DECO G>]C@

X= &CBL>M@GDE G>]C@Y= *>L@DMG Q>HD@A Z'>LN>LC COD@GA[

5[ $GH>M@G>KA G>]C@d!= .@EL>BDE E@OO H@CBF:= &??KG@ L@CEBD>GR= ,DAAK@ DAEF@?DCT= &GEL@CA@H @GH>M@G>KA NL>HKEBD>G >JLCHDECOAU= 2QABLKEBD>G >J F>OO>b >LMCGA

W= .@KL>M@GDE DGJOC??CBD>GX= $]E@AA >J @GH>M@G>KA AKQABCGE@A CGH?@BCQ>ODB@AY= %DA>LH@LA >J Q>HI E>?NCLB?@GBA

*KLBF@L &GJ>L?CBD>Gd 'FCNB@L !W &GJOC??CBD>GS 6CBF>NFIAD>O>MIS 3= n>PCEh N=W_\ >JFCGH>KBOTM ?#,B)/%*F .+ -B# ")*,@()$ )/E ,#((@()$ $#),-%./ %/ %/+()FF)-%./

&G CEKB@ DGJOC??CBD>G BF@ JDLAB B@G HCIA CL@ H>?DGCB@H QI MLCGKO>EIB@ DGJDOBLCBD>GZG@KBL>NFDOS @>ADG>NFDOAS QCA>NFDOA CGH NL@ECGE@L>KA ?CAB E@OOA[= .@KBL>NFDO DGJDOBLCBD>GDA H>?DGCGB= 4LCGKO>EIB@ DGJDOBLCBD>G ECG Q@ HDPDH@H DGB> JDP@ ABCM@Ad

!= &GDBDCO E>GBCEB:= 0>OODGMR= *DL? CHF@AD>GT= )@K`>HDCN@H@ADAU= (EBDPCBD>G CB BF@ @]BLCE@OOKOCL ANCE@1@@ JDM=!W_X DG FCGH>KB CGH BCQO@ !W=R ZJ>L CHF@AD>G ?>O@EKO@A[

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• (EKB@ DGJOC??CBD>G L@CEBD>G L@AKOBA DGd

!= &GEL@CA@H N@L?@CQDODBI= /CAEKOCL bCOO HC?CM@ ECKA@A @JJOK] >J NOCA?C DGB>

DGBLCE@OOKOCL ANCE@= 1@E>GHOI O>ECO ?@HDCB>LA ECKA@ DGEL@CA@ DG N@L?@CQDODBI >J

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:= 'FCGM@A DG L@ADABCGE@ DG BF@ CL@C >J DGJOC??CBD>G=

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QI BF@DL NL>N@LBD@A CA @DBF@Ld!= D4&'1-2&,) E>GBCDGA O@AA NL>B@DG CGH DGJOC??CBD>G O@AA OD`@OI B> Q@ ECKA@ >J= 2JB@G



BF@ L@AKOB >J HDABKLQCGE@A >J FIHL>ABCBDE >L E>OO>DH >A?>BDE NL@AAKL@=:= JW-2&,) NL>B@DG LDEF @]BLCPCAEKOCL JOKDH= 1@@ N :! >J FCGH>KB J>L JKLBF@L DGJ>L?CBD>G=

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$OCABCA@A %@MLCHCBD>G >J DGB@LE@OOKOCL AKQABCGE@6L>B@CA@A (EBDPCBD>G C?NODJIDGM QD>EF@?DECO AIAB@?

DG BF@ NOCA?C2]IM@G 1N@ED@A 6@L>]DHCBD>G >J ODNDH ?@?QLCG@= 6L>B@DGA

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- OCQDOIACB>LA >J OIA>A>?@A ?@?QLCG@A ZQ@@ N>DA>GA[- HDABKLQ@H CEBDPDBI >J D>G EFCGG@OA CGH ?@?QLCG@ D>G NK?NA ZDGA@EBDEDH@A[

Y= EL@CBD>G >J JL@@ LCHDECOA- CGBLCEDÒDGA`D CGBD_ECGE@L HLKMA- ECLQ>G B@BLCEFO>LDH@- NCLC`PCB ZNG@K?>B>]DE F@LQDEDH@[

!R:= 6CBF>NFIAD>O>MDECO ?@EFCGDA?A >J DGJ@EBDP@ HDA@CA@A

- &GJ@EBD>KA JCEB>LA ABCLB DGJOC??CBD>GA ZN>B@GBDCO G>G_AN@EDJDE NL>B@EBD>GDG C AF>LB BD?@[ CGH D??KG>O>MDECO CGAb@L ZO>GM_B@L? NL>B@EBD>G DG C

O>GM N@LD>H >J BD?@[ _ >JB@G AIG@LMDABDE @JJ@EB



- NCB>M@G@BDE ABCB@ >J E>?NL>?DA@ F>ABA L@NL@A@GB aKCODBCBDP@ CGHaKCGBDBCBDP@ HDABKLQCGE@A DGJOC??CBD>G CGH D??KG@ L@CEBD>G

- EODGDECOOI D?N>LBCGB HDA@CA@A ECG Q@ HDPDH@H DGB>d!= ADBKCBD>G DG bFDEF BF@ NCLBDEDNCGBA CGH BF@ @JJ@EBA M@L? CGH

DGJOC??CBD>G L@CEBD>GA CGH AN@EDJDE D??KG@ L@AN>GA@

E>GBLDQKB@A B> BF@ NFCA@ >J GCBKLCO F@CODGM CGH ECO?DGMAI?NB>?A c CEKB@ >L AKQCEKB@ >L EODGDECO E>KLA@ >J ZB>]DEMCABL>DGB@ABDGCO AIGHL>?@A[

:= ABCB@ >J N@L?CG@GB @]EDBCBD>G CGH ?CDGB@GCGE@S CGH EFCGM@A DGL@CEBDPDBI >J D??KG@ L@AN>GA@A ZE>GBLDQKB@A B> FCL?JKO EFCGM@ADG BF@ NL>E@AA@A >J BDAAK@ CLEFDB@EBKL@ CGH JKGEBD>G[ _ '702.&'&GJ@EBD>KA HDA@CA@A ZBKQ@LEKO>ADA[

- NCB>M@G@BDE E>GA@aK@GE@Ad!= N@LEKBCG@>KA B>]DE AIGHL>?@:= AN@EDJDE B>]DE AIGHL>?@AR= CEKB@ DGJ@EBDP@ DOOG@AAT= 1&01S A@NADAS KLKŽCVS #2%1S #2*1U= EFL>GDE DGJ@EBDP@ HDA@CA@AW= CKB>D??KGDBIX= D??KG>DGAKJJDED@GEIY= PDLCO >GE>M@G@ADA

!RR= 7C@?CB>O>MDECO CGH ?@BCQ>ODE EFCGM@A ECKA@H QI CEBDPDBD@A >J DGJ@EBD>KA JCEB>LA

([ 'FCGM@A DG QO>>H

!= 'FCGM@A DG QO>>H NOCA?CC[ NOCA?CBDE NL>B@DG

- EFCGM@A DG ?KBKCO L@OCBD>GA Q@Bb@@G COQK?DG@A CGH MO>QKODGA- DG CEKB@ DGJ@EBD>G BF@ E>GE@GBLCBD>G >J COQK?DG DA L@HKE@HS CGH DGEL@CA@H

o!S o: CGH q MO>QKODG@A _ DGEL@CA@H AIGBF@ADA >J CEKB@ NFCA@ NL>B@DGA DGODP@L

- DG EFL>GDE DGJ@EBD>GA BF@ E>GE@GBLCBD>G >J BF@ COQK?@G DA H@EL@CA@H >LKGEFCGM@HS q_MO>QKODG DA FDMFS CGH >JB@G BF@ E>GE@GBLCBD>G >J o_MO>QKODG@DA @O@PCB@H

Q[ A@HD?@GBCBD>G >J @LIBFL>EIB@ c CEE@O@LCB@H:= $0-,702'-,$

- bF@G DGJ@EBD>G OCABA O>GM@L BF@G C J@b b@@À BF@ (.$#&( '702.&'&.*$',&2+1 H@P@O>NA

- DG CEKB@ DGJ@EBD>G 7$#2)-,&' (.$#&(- bDBF DGJ@EBD>G BFCB H@ABL>I Q>G@ ?CLL>b (6)(1,&' (.$#&( H@P@O>NA

R= O@KE>EIB@A- #>AB >J CEKB@ QCEB@LDC DGJ@EBD>GA DA CEE>?NCGD@H bDBF O@K`>EIB>ADA

ZDGEL@CA@ DG BF@ GK?Q@L >J G@KBL>NFDO MLCGKO>EDB@A[- A>?@ DGJ@EBD>GA Z?@CAO@AS DGJ@EBDP@ ?>G>GKEO@>ADA[ CL@ J>OO>b@H QI

G@KBL>N@GDC- PDLKA@A ECKA@ )-#672'-,$1

- NCLCADB@A ECKA@ $21&.267&)1T= %&120%$01 &. 5)22% '2(4+)(,&2.



C[ EFCGM@A DG NOCB@O@B c BL>?Q>EIB>N@GDCQ[ HDAA@?DGCB@H DGBLCPCAEKOCL E>@MKOCBD>G Z%&n[

- KGE>GBL>OO@H ZCEKB@ >L EFL>GDE[ CEBDPCBD>G >J QO>>H EO>BBDGM DG OCLM@L CL@CA>J QO>>H QINCAA ZBLDMM@LA DGJ@EBD>KA M@L?AS C`PDLCGD O@KE>EIB@A ===[

- ?DEL>NOCB@O@B CL@ L@N>ADB DG A?COO QO>>H P@AA@OA CGH QO>E` QO>>H JO>b

- EO>BBDGM JCEB>LA CL@ HLCDG@H CGH LDA` >J QO@CHDGM DA DGEL@CA@H5[ #@BCQ>ODE EFCGM@AC[ DGEL@CA@H ECBCQ>OD^C? >J NL>B@DGQ[ EFCGM@A DG @O@EBL>OIB@ CGH bCB@L BLCGAN>LBE[ DGEL@CA@ E>GE@GBLCBD>G >J B>BCO NOCA?CBDE ODNDHA

- CL@ @AN@EDCOOI A@LD>KA DG BF@ A@NBDE E>OOCNA@d• EFCGM@A JDLAB >EEKL N@LDNF@LCOA c H@P@O>N?@GB >J ?KOBDAIAB@? >LMCGDAC?

JCDOKL@ AIGHL>?• >]DHCBD>G >J MOKE>A@ DA HDABKLQ@H _ QO>EÀ @GBLI NILKPCB@ DG nL@QA EIEO@ c

QLC`DGM EL@CBD>G CGH @G@LMI E>GAK?NBD>G

!RT= 6(,24$.$,&' #$'7(.&1#1 2* 60&2. (.% %$4$.$0(,&/$ %&1$(1$1

- ECKA@ DA BF@ NL>B@DG NCLBDEO@ BFCB H> G>B E>GBCDG GKEO@DE CEDH- ?CI FCP@ NL>N@BI@A >J DGJ@EBD>G HDA@CA@A ZPDLKO@GBDES NCBF>M@GDEDBI CGH

B>]DEDBI[- JKGHC?@GBCO HDABKLQCGE@ CLDADGM JL>? BF@ E>GP@LAD>G >J 6L6E ZG>L?CO DG

BF@ QLCDG[ B> 6L6AE _ HDJJ@L@GE@A DG B@LBD@LI CGH aKCLB@LGCLI ABLKEBKL@- 6L6AE AN>GBCG@>KAOI V>DGA CGH EL@CB@A DGA>OKQO@ CMML@MCB@ BFCB BLDMM@L

E@OO CN>NB>ADA _e ECKA@A G@KL>H@M@G@LCBDPG@ HDA@CA@A Z1ECLNDCS `KLKS

'L@KB^J@OHB_tC`>Q HDA@CA@[

!RU= &#+.2)24&'() '7(.4$1 &. &.*$',&2.

([ 5(',$0&() %$*$.1$- A`DG CGH ?KE>AC- ?CEL>NFCM@A ZQCEB@LDC bDBF C AF@OO CL@ G>B AKQV@EB B> NFCM>EIB>ADA _

L@aKDL@ CGBDQ>HD@A[- COB@LGCBDP@ bCI >J CEBDPCBD>G E>?NO@?@GBA- OI?NF G>H@A- #>G>EIB@A CGH G@KBL>NFDOA DG BF@ QO>>H- L@BDEKO>@GH>B@OG E@OO AIAB@? DG ODP@L- FK?>L>KA Z@]BLCE@OOKOCL QCEB@LDC[ CGH E@OOKOCL ZDGBLCE@OOKOCL QCEB@LDC[

&??KG@ ?@EFCGDA?A

5[ /&0() %$*$.1$- A`DG CGH PDADQO@ @NDBF@ODC- DGB@LJ@L>GAS bFDEF EL@CB@ C PDLKA DGJ@EB@H E@OOA Zo ZO@KE>EIB@A[

ZJDQL>QOCABA[ q ZD??KG@[ _e E>NIS OCI>KBS CEBDPCBD>G >J @GÎ?@ASHDJJ@L@GBDCBD>GS ?CGDJ@ABCBD>G >J AKLJCE@ CGBDM@GA _e @GFCGEDGM EIB>B>]DE

CEBDPDBI >J .n E@OOA- ?CEL>NFCM@A



- &??KG@ AIAB@? _ `DOO DGJ@EB@H E@OOA ZEIB>B>]DE , OI?NF>EIB@AS .n E@OOS nE@OOA[

'[ %$*$.1$ (4(&.1, 6(0(1&,$1C[ G>GAN@EDJDE _ NFCM>EIB@ Z?CEL>NFCM@A[

Q[ AN@EDJDE D??KGDBI >J E@OO BIN@A ZCGBDQ>HD@A B> DGBLCE@OOKOCL NCLCADB@A _ &M$[ _@>ADG>NFDOA c L@MKOCB>LI ZL@?>PCO >J AKLNOKA >J NCLBDEDNCGBA >J DGJOC??CB>LIL@CEBD>GA[ CGH EIB>B>]DE Z&M4 CGH 'RQ[ @JJ@EB

%[ %$*$.1$ 2* *+.4&C[ E@OOAQ[ CGBDQ>HD@A

!RW= 6(,2*&3&2)24- 2* 1$6,&' (.% ,29&' '2))(61

([ 1$61 _ AIAB@?DE DGJOC??CB>LI L@AN>GA@ BLDMM@L@H QI N@G@BLCBD>G >J NCBF>M@GACGH ?KOBDNODECBD>G >J ?DEL>>LMCGDA?A DG BF@ QO>>H c A@NBDE E>OOCNA@ DA BF@KOBD?CB@ E>GA@aK@GE@

- DG H@P@O>N?@GB NCLBDEDNCB@ QCEB@LDCS BF@DL B>]DGA CGH PCLD>KA QD>O>MDECOOICEBDP@ AKQABCGE@A _ ECG HC?CM@ BF@ E@OOAd

!= CEBDPCBDGM ?CEL>NFCM@:= HDL@EB CEBD>G >G @GH>BF@ODCO E@OOA >J QO>>H P@AA@OAR= CEBDPCBDGM BF@ HDJJ@L@GB DGB@L?@HDCLD@A DG BF@ NOCA?C

ZE>?NO@?@GBS E>CMKOCBD>G `COD`L@DG_aKDGDG@[T= JL@@DGM CM@GBA JL>? E@OOU= HC?CM@ B> BDAAK@A DG CHPCGE@ AF>E` BFCB >EEKLA COA> Q@ECKA@ >J

D?NCDL@H QO>>H AKNNOI- DG NL>ML@AA >J A@NBDE E>OOCNA@ (',7 DA L@O@CA@HS @GH>LNFDG@ CGH @G`@JCODG- EOCAADJIA DG PCA>FIN>B>GDE E>OOCNA@- NFCA@Ad

!= FIN@L`DG@BDE E>GHDBD>G c L@HKE@ BF@ 1#/ CGH N@LDNF@LCOL@ADABCGE@

:= FIN>HIGC?DE ZFIN>P>O@?DE[ _ FIN>B@GAD>G BFCB H>@A G>BL@AN>GH B> ?@HDECBD>GA CGH ?@BCQ>ODE EFCGM@A

- HKLDGM A@NADA ?CI >EEKLd• FIN>P>O@?DE E>OOCNA@ ZCG@KLIA?A LKNBKL@S O>AA >J ODaKDH

Q@ECKA@ >J HDCLLF@C >L P>?DBDGM[• ECLHD>M@GDE E>OOCNA@ Z@GH>ECLHDBDAS ?DB>ABCBDE ?I>ECLHDBDA[• >QABLKEBD>G E>OOCNA@ Z*@AB@L N@LDECLHDBDA CGH BC?N>GCH@[

5[ ,29&' '2))(61$- @]E@NB BF@ QCADE NCBF>M@G@ADA A@NBDE E>OOCNA@ DGEOKH@A BF@ @JJ@EBA >J

1+6$0(.,&4$. Z@]>B>]DGA CEBDGM OD`@ G>B_AN@EDJDE ?DB>M@GDEA _ BLDMM@LAU_!;w >J COO , OI?NF>EIB@A _ ECKA@ ABL>GM ,F! A@EL@BD>G >J EIB>`DG@A[

!RX= 2+,'2#$ 2* &.*$',&2.

!= *(',201 ,7(, %$,$0#&.$1 2+,'2#$ 2* &.*$',&2.1C[ &.*$',&2+1 4$0#1



- L@ADABCGE@ B> NFCM>EIB>ADA- EFCGM@A DG AKLJCE@ CGBDM@GA ZPDLCO NL>B@DGA ECNCQO@ >J QDGHDGM B> G>L?CO

E@OO E>?N>G@GBA _ 1FL>KHDGM PDLCO CGBDM@GAS NCLCADB@A ?D?DE CGBDM@GDEABLKEBKL@ >J BF@ F>ABA _ ?D?DELI[

- CG@LMI Z@EODNA@H E@OOKOCL D??KGDBI _ A?COON>]S MLCGKO>?CB>ADE DGJ@EBD>GA

ZO@NL>AIS BKQ@LEKO>ADA ?DODCL[[Q[ 721,

- M@G@BDE EFCLCEB@LDABDEA- CM@- G>KLDAF?@GB- >BF@L F>AB HDA@CA@ ZHDCQ@B@AS COE>F>ODE EDLLF>ADAS #CODMGCGB BK?>LAS

DGAKJDED@GB ELKAB (HL@GCO MOCGHAS ANO@@G L@?>P@H[- F>AB bDBF AKNNL@AA@H D??KG@ L@AN>GA@

:= f7&)$ 0$'2/$0&.4!= DGEKQCBD>G:= DGDBDCO ZDGDBDCO[ N@LD>HR= N@LD>H >J H@P@O>N@H HDA@CA@T= N@LD>H >J L@ML@AAD>GA ZbDBFHLCbCO HDA@CA@[ _ BF@ H@B@LD>LCBD>G >J DOOG@AAU= N@LD>H E>GPPCO@AE@GB ZF@CODGM[ _ L@CNN@CLCGE@ >J DOOG@AA

R= 6$0#(.$., &.*$',&2.

C[ ECLLD@L c BF@ NL@A@GE@ CGH C]BLCEBD>G >J ECKA@A bDBF>KB @]B@LGCO ADMGA >J DOOG@AAZACO?>G@OOCS 75/[

Q[ EFL>GDE &GJ@EBD>KA %DA@CA@A _ CEE>?NCGD@H QI BF@ NL@A@GE@ >J ADMGA CGH

AI?NB>?A >J HDA@CA@ g EFL>GDE DGJ@EBD>G ZBKQ@LEKO>ADAS O@NL>AIS AINFDODA[ _H@N@GHA >G BF@ O>ECOD^CBD>G

E[ OCB@GB DGJ@EBD>G c NL@A@GE@ CGH @]BLCEBD>G >J ECKA@A bDBF>KB @]B@LGCO ADMGA >JDOOG@AAS QKB A>?@BD?@A BF@ DGJ@EBD>KA DOOG@A ECG L@CEBDPCB@ Z/71S PCLDE@OOC_^>AB@LS5LDOOuA HDA@CA@ ZOCB@ L@EDHDP AN>B ,INF>DH[S ,>]>NOCA?C M>GHDD[

t@O@GC 6>E@HDEd !RY_!TU

";M# E/1*42)41 *+ .*77&()' 1,4-.,-4) &'2 +-'.,/*'

'2))(4$._,F@ E>OOCM@GA CL@ JDQL>KA ABLKEBKLCO NL>B@DGA BFCB MDP@ B@GADO@ ABL@GMBF=_'>OOCM@GA CL@ E>?N>A@H >J BFL@@ A@NCLCB@ N>OIN@NBDH@ EFCDGA QLCDH@H DGB> C L>N@OD`@BLDNO@ F@OD]=_,F@ E>OOCM@G NL>B@DGA CL@ LDEF DG FIHL>]INL>ODG@ CGH FIHL>]IOIADG@=_(Q>KB R; E>OOCM@G BIN@A FCP@ Q@@G DH@GBDJD@HS A>?@ >J bFDEF CL@ KGDaK@ B> AN@EDJDE E@OOACGH BDAAK@A=_1>?@ E>OOCM@G BIN@A Z@=M=S BIN@A &S &&S &&&S CGH /[ J>L? JDQLDOA QI OCB@LCO EL>AA_ODG`DGM >JBF@ BLDNO@ F@ODE@A=_,F@ JDQLDOOCL E>OOCM@GA J>L? C ?CV>L NL>N>LBD>G >J BF@ E>GG@EBDP@ BDAAK@ DG F@CODGM

b>KGHA CGH NCLBDEKOCLOI AECLA=



_,F@ B@GADO@ ABL@GMBF >J BF@ JDQLDOOCL E>OOCM@GA H@LDP@A JL>? BF@DL EL>AA_ODG`DGMS bFDEF DABF@ L@AKOB >J E>PCO@GB Q>GHA ECBCOI^@H QI BF@ @GÎ?@ OIAIO_>]DHCA@= ,FDA NL>E@AA DAH@N@GH@GB >G PDBC?DG 'h BF@L@J>L@S EFDOHL@G bDBF CAE>LQCB@ H@JDED@GEI FCP@ A`@O@BCOH@J>L?DBD@AS QO@@H @CADOI Q@ECKA@ >J b@C` PCAEKOCL bCOO QCA@?@GB ?@?QLCG@S CGH F@CON>>LOI=

_4@G@BDE H@J@EBA DG E>OOCM@GA ECKA@ HDA@CA@A AKEF CA >AB@>M@G@ADA D?N@LJ@EBC CGH $FO@LA_%CGO>A AIGHL>?@=

$FO@LA_%CGO>A 1IGHL>?@A Z$%1A[_EFCLCEB@LD^@H QI H@J@EBA DG E>OOCM@G AIGBF@ADA >L ABLKEBKL@=_BDAAK@A LDEF DG E>OOCM@GS AKEF CA A`DGS ODMC?@GBAS CGH V>DGBAS CL@ JL@aK@GBOI DGP>OP@H DG?>AB PCLDCGBA >J $%1=_Q@ECKA@ BF@ CQG>L?CO E>OOCM@G JDQ@LA OCE` CH@aKCB@ B@GADO@ ABL@GMBFS A`DG DAFIN@L@]B@GADQO@ CGH V>DGBA CL@ FIN@L?>QDO@=_BF@A@ J@CBKL@A N@L?DB ML>B@AaK@ E>GB>LBD>GAS AKEF CA Q@GHDGM BF@ BFK?Q QCE`bCLH B>B>KEF BF@ J>L@CL? CGH Q@GHDGM BF@ `G@@ KNbCLH B> EL@CB@ CO?>AB C LDMFB CGMO@=_BF@ A`DG DA @]BLC>LHDGCLDOI ABL@BEFCQO@S @]BL@?@OI JLCMDO@ CGH PKOG@LCQO@ B> BLCK?C=_BF@ QCADE H@J@EB DG E>GG@EBDP@ BDAAK@ ?CI O@CH B> A@LD>KA DGB@LGCO E>?NODECBD>GASDGEOKHDGM LKNBKL@ >J BF@ E>O>G CGH OCLM@ CLB@LD@A ZPCAEKOCL $%1[h >EKOCL JLCMDODBIS bDBFLKNBKL@ >J BF@ E>LG@C CGH L@BDGCO H@BCEF?@GB ZÌ>NF>AE>OD>ADA $%1[h CGH HDCNFLCM?CBDEF@LGDCA ZEOCAADE $%1[S C?>GM >BF@LA=_?>O@EKOCL QCADA >J $%1 DGEOKH@d

_H@JDED@GEI >J BF@ @GÎ?@ OIAIO FIHL>]IOCA@_H@JDED@GB AIGBF@ADA >J BIN@ &&& E>OOCM@G L@AKOBDGM JL>? ?KBCBD>GA CJJ@EBDGM BF@'2)R(! M@G@

2AB@>M@G@ADA &?N@LJ@EBC_C ML>KN >J F@L@HDBCLI HDA>LH@LA ECKA@H QI H@J@EBDP@ AIGBF@ADA >J BIN@ & E>OOCM@G=_BF@ ?>O@EKOCL NCBF>O>MI KGH@LOIDGM 2& EFCLCEB@LDABDECOOI DGP>OP@A M@G@ ?KBCBD>GA DGBF@ E>HDGM A@aK@GE@A J>L o! CGH o: EFCDGA >J BIN@ & E>OOCM@G=_BF@ JKGHC?@GBCO CQG>L?CODBI DG COO J>L?A >J 2& DA B>> ODBBO@ Q>G@S L@AKOBDGM DG @]BL@?@A`@O@BCO JLCMDODBI=

";R# Z),&3*7/. 2/1*42)41 *+ ,%) 1I)7),&7 161,)0

!= 21,$2#()('&( CGH 0&'n$,1C[ 0DE`@BA c DA C HDA@CA@ >J EFDOHF>>H= &B DA EFCLCEB@LD^@H QI A>JB@GDGM >J BF@ Q>G@A CA CL@AKOB >J DGCH@aKCB@ DGBC`@ >J PDBC?DG % CGH DGAKJJDED@GB @]N>AKL@ B> AKGODMFB= )CE` >JECOEDK? CGH NF>ANFCB@ DG BF@ HD@B ECG COA> O@CH B> LDE`@BA=

Q[ 2AB@>?COCEDC_ DA BF@ B@L? KA@H B> H@AELDQ@ C AD?DOCL E>GHDBD>G >EEKLLDGM DG CHKOBASM@G@LCOOI HK@ B> C H@JDED@GEI >J PDBC?DG % >L DGAKJJDED@GB AKGODMFB @]N>AKL@= &B DAEFCLCEB@LD^@H QI A>JB@GDGM >J BF@ Q>G@A HK@ B> H@J@EBDP@ Q>G@ H@?DG@LCOD^CBD>G=

:= 21,$262021&1

2AB@>N>L>ADA c DA C HDA@CA@ >J BF@ Q>G@ BFCB ECG O@CH B> DGEL@CA@H LDA` >J JLCEBKL@= &G>AB@>N>L>ADA BF@ Q>G@ ?DG@LCO H@GADBI Z5#%[ DA L@HKE@HS Q>G@ ?DEL>CLEFDB@EBKL@ DA



HDALKNB@HS CGH BF@ C?>KGB CGH PCLD@BI >J G>G_E>OOCM@G>KA NL>B@DGA DG BF@ Q>G@ DACOB@L@H=

Z![ $AA@GBDCO >L &HD>NCBFDE ZECKA@ G>B `G>bG[ZC[ 6>AB?@G>NCKACO_ C OCE` >J @ABL>M@G ECKA@A CG DGEL@CA@ DG >AB@>EOCAB

CEBDPDBI ZCEBDPCBD>G >J &)_!S &)_WS ,.*_oh 0@HKEBD>G >J CN>NB>ADAh AF>LB@GODJ@_ANCG >J >AB@>EOCABA[ CGH L@HKE@A BF@ O@P@O >J ECOEDK? _ ?>L@ JL@aK@GBJLCEBKL@A DG BF@ N@EB>LCO ANDG@ CGH J>L@CL?AZQ[ 1@GDO@ _ H@EL@CA@H CQA>LNBD>G >J ECOEDK?S b@C`@G@H JKGEBD>G >J>AB@>EOCABA _ DGEL@CA@H JL@aK@GEI >J JLCEBKL@A

Z:[ 1@E>GHCLI ZE>GA@aK@GE@ >J NL@_@]DABDGM HDA@CA@ >L HLKM[_ >AB@>N>L>ADA DG ?@G c >EEKLA ?KEF O@AA DG ?@G BFCG b>?@G c FCA BF@ AC?@@BD>O>MI CGH ?@EFCGDA?_ VKP@GDO@ >AB@>N>L>ADA c >EEKLA DG EFDOHL@G Q@J>L@ NKQ@LBIS AN>GBCG@>KA F@CODGM

R= 6(4$,i1 %&1$(1$ ZCOA> `G>bG CA >AB@DBDA H@J>L?CGA[_ DA C EFL>GDE HDA>LH@L BFCB BINDECOOI L@AKOBA DG @GOCLM@H CGH H@J>L?@H Q>G@A

T= 21,$26$,021&1_DA CG @]BL@?@OI LCL@ DGF@LDB@H HDA>LH@L bF@L@QI BF@ Q>G@A FCLH@GS Q@E>?DGM H@GA@L

">U# :')0/&1F ()')4&7 5&,%*()')1/1 &'2 .*'1)`-)'.)1_(G@?DC DA C H@EL@CA@ DG 05' GK?Q@L >L JKGEBD>G=_&G CG@?DC BF@L@ DA C H@EL@CA@ DG BF@ >]IM@G_ECLLIDGM ECNCEDBI >J BF@ QO>>H= ,FDA >EEKLA

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NKO?>GDE PCAEKOCL >QABLKEBD>G ZPCA>E>GABLDEBD>G >J QCACO OKGM CLB@LD>O@A[! A@E>GHCLIAB@G>ADA ZGCLL>bDGM >J NKO?>GDE CLB@LD>O@A[! FIN@LBL>NFIS HDOCBCBD>GS CGH L@OC]CBD>G >JLDMFB P@GBLDEO@S BLDEKANDH DGAKJJDED@GEIS HDOCBCBD>G >J LDMFB CBLDK?S AIAB@?DE P@G>KAFIN@LB@GAD>G bDBF E>GM@ABD>G >J ODP@L CGH N@LDNF@LCO @H@?C=

:= #DBLCO DGAKJJDED@GEI_5O>>H DA @V@EB@H DG AIAB>O@ DGB> C>LBC CGH O@JB CBLDC=_&GEL@CA@H P>OK?@ >P@LO>CH CGH H@EL@CA@H NL@AAKL@ >P@LO>CH ZHK@ B> DGEL@CA@H AD^@H >JO@JB P@GBLDEO@S DB Q@E>?@A G>L?CO[_)@JB P@GBLDEO@ DA ?>L@ ABL@BEFCQO@ BFCG G>L?CO ZHK@ B> H@EL@CA@H BFDE`G@AA >J bCOO[! AIAB>ODE DGAKJJDED@GEI DA A@@G HKLDGM AKN@LG>L?CO HDCAB>ODE JKGEBD>G=C[?DOH_ QO>>H DA L@BKLGDGM >GOI DG OCB@ AIAB>O@Q[A@P@L@_ QO>>H DA L@BKLGDGM DG @CLOI AIAB>O@ ZF>O>AIAB>ODE ?KL?KL[! CQG>L?CODGEL@CA@ DG NL@AAKL@ DG O@JB CBLDK?=_LKNBKL@ >J BF@ EF>LHC >L NCNDOOCLI ?KAEO@A >EEKLA Q@ECKA@ BF@ O@JB CBLDK? ECGG>BABL@BEF JCAB @G>KMF=_bDBF H@EL@CA@ >J ?DGKB@ P>OK?@ QO>>H JO>b DG BF@ `DHG@IA bDOO COA> H@EL@CA@S O@CHDGM B>ACOB CGH bCB@L L@B@GBD>G CGH E>GM@ABDP@ F@CLB DGAKJJDED@GEI H@P@O>NA=_#CL`@H NKO?>GDE FIN@LB@GAD>G H>@A G>B H@P@O>N= 2GOI DG CEKB@ ?DBLCO L@MKLMDBCBD>GNKO?>GCLI @H@?C ECG H@P@O>N Q@ECKA@ BF@ CBLDK? CGH P@GBLDEO@ H> G>B FCP@ @G>KMFBD?@ B> E>?N@GACB@ QI HDOCBCBD>G CGH FIN@LBL>NFI=



&G Q>BF C>LBDE AB@G>ADA CGH C>LBDE L@MKLMDBCBD>G BF@ G@B ABL>`@ P>OK?@ >KBNKB >J BF@F@CLB DA H@EL@CA@H= fDBF DGEL@CA@H P@GBLDEKOCL b>LÒ>CH BF@ P@GBLDEKOCL ?KAEO@FIN@LBL>NFD@A=R= (>LBDE AB@G>ADAC[PCOPKOCLd

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T= (>LBDE DGAKJJDED@GEI_%@P@O>NA Q@ECKA@ >J C HC?CM@H C>LBDE PCOP@ O@CJO@B >L Q@ECKA@ BF@ C>LBDE LDGM DA HDOCB@H=C[CEKB@ Z?>AB JL@aK@GB ECKA@A CL@ DGJ@EBD>KA @GH>ECLHDBDA CGH HIAJKGEBD>G >J CNL>ABF@BDE C>LBDE PCOP@[

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_CHPCGE@H JDQL>ADA_DGB@LABDBDCO DGJDOBLCBD>G_DGBLCE@OOKOCL H@N>ADBA >J J>L@DMG AKQABCGE@A

_BF@ @GH>?I>ECLH DA DGP>OP@H DGd_@GH>?I>ECLHDCO JDQL>ADA CGH FIN@L@>ADG>NFDODE AIGHL>?@

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170-Pathophysiology of the arterial hypotension:

Arterial hypotension is characterized by clinical depression of arterial pressure below100/60 mm hg for persons aged till 25 years and below 105/65 mm hg above 30years. It is divided in primary (essential) and secondary (symptomatic), in each ofwhich excrete acute and chronic forms.

A-Primary Hypotension:

a-Constitutive hypotension : Permanently lower value of arterial pressure with nosigns of illness.

b-Orthostatic hypotension: ("postural hypotension"), is a common form. Occurs aftera change in body position when a person stands up from either a seated or lyingposition. It is usually transient and represents a delay in the normal compensatoryability of the autonomic nervous system.

c-Vasovagal Syncope :it results in a drop in blood pressure leading to decreasedblood flow to the brain resulting in dizziness or fainting. The mechanism is described

as the following:

• When we sit or stand, blood settles in the legs and abdomen• As a result, less blood returns to the heart• The blood vessels leaving the heart have detectors in them called baroreceptorsthat detect a decrease in blood pressure

• The baroreceptors send a message to the brain, which in turn sends a signal to theheart to increase the heart rate, and tighten up the blood vessels• This process occurs constantly in all of us as we adapt to changes in posture• In vasovagal syncope, an abnormal reflex occurs that results in withdrawal of themessage that speeds up the heart and tightens up the vessels, often because of an

overshoot in the reflex that compensates for the fall in blood pressure• The resultant decrease in blood flow to the brain will result in dizziness orlightheadedness if mild, and progress to fainting or loss of consciousness if moresevere• There are several variants of vasovagal syncope that can trigger the same reflex,

including situations such as the sight of blood, injury, blood testing (needles), goingto the washroom and several others that are quite uncommon.

B-Secondary (symptomatic) hypotension:

a-Endocrine:-Addison's disease



-Hypothyroidism-Insufficiency of adenohypophyse

b-Cardiovascular:-Myocardial insufficiency

-Mitral and aortic stenosis-Aortic arch syndrome-Hypovolemia (hemorrhage.)

c-Nervous:-Damage of nerve pathways for arterial pressure maintenance in standing-carotid sinus syndrome (hyperreactivity of the baroreceptors leading to low bloodpressure)-Chronic idiopathic orthostatic hypovolemia :Bradbury-Eggleston syndrome,( adegenerative disorder of the autonomic nervous system characterized by abnormal

low blood pressure in standing position)

d-Infectious and toxic diseases:-causing myocardial damages, hypovolemia or nervous regulation disturbances.

e-Pregnancy, drugs, valsalva experience.

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178. Respiratory rhythm disorder

1. Cheyne-Stroke breathing

Reapeted increase and decrease breath volume and apneic pause.

Due to :

-brain damage

-prolonged time in circulation of blood from lungs to brain in left heart insufficiency.

Hyperventilation of alveolar spaces leads to hypocapnia.

Ventilation in those patients is three times more sensitive to pCO2 so there is a relativehypercapnia in apneic part which causes hyperventilation.

2. Sleep apnea

Sleep apnea is the cause of over 30% of apneic attacks during night sleep. They are 15 to 20

seconds long.

After apnea, there is asphyxia (breathing disrupted due to lung pathway obstruction), leading to

sudden weak up and then breathing.

Due to :

-Central cause : Disorder in brainy rhythm maintenance.

-Obstructive cause : No air flow in sleeping by mechanical obstruction of upper

respiratory tract by relax of muscles that are usually active in maintaining the free flow of

those respiratory pathway)

In apnea phase the patient is hypoxemic, hypercapnic, has pulmonary hypertension, sinus

bradicardia and congestive heart failure (cor pulmonale).

3. Hypoventilation syndrome in obese people (picknick syndrome)



Obesity lead to :

-loss of elasticity of chest and abdomen leading to a decrease of lung permeability

leading to an increase in breathing work, hypoventilation and functional right-left shunt)

-Decrease of vital capacity, total lung capacity and functional residual volume.

Consequences :

-severe hypoxemia

-mild to moderate hypercapnia

-respiratory acidosis

Clinically :

-somnolence and narcolepsy



179. Pathogenesis of respiratory

insufficiency

-Due to pulmonary function damage, exchanges of gas not good enough to maintain

normal partial pressure in blood.

Clinically :

-Acute in pathogenesis without history of pulmonary disease.

-Consequence from chronic lung disease.

-Patients with chronic respiratory insufficiency -> sudden worsening of the lund

disease and following acute insufficiency.

1. Hypoxemic respiratory insufficiency (normal PaCO2)

-> Hypoxia = Lack of O2 for normal oxid need of cells in various tissue.

-> Hypoxemia = Lowering of partial pressure of O2 in the arterial blood.---> Consequence of respiratory dysfunction due to

A) V/Q inbalance

- Increase respiratory muscle work and O2 utilisation

-Compensation with increase pulmonary ventilation > hypoxia,

hypocapnia

-Increase ventilation of death space above critical level

-> more hyperventilation will not lower hypercapnia

B) Diffusion disturbance at the level of alveoliC) A-V shunt

D Hypoventilation of alveolar spaces

2. Hypercapnia respiratory insufficiency (lower PaO2)

-When alveolar ventilation not enough for CO2 production

-Hypercapnia due to :A) Lowering of total ventilation. Absolute hypoventilation

Poisonning, cerebrovascular incident, head injury, chest disorder

B) Increase of total ventilation. Relative hypoventilation Normal or increased total volume, COPD (lowering perfusion due to

degeneration of intraalveolar barriers)

-Increased O2 utilisation and CO2 production due to increased ventilation work.

Worsen hypoxia and hypercapnia, utilisation of 02 for ventilation can be increased

then ability to bring 02 with ventilation.

180. Interrelation between pulmonary and the other organs

dysfunctions.

A) Systemic consequence of pulmonary disease



1. Hypoxemia

-Cardiovascular : dilatation of peripheral blood vessels, increased skeletal

muscle of ventricle.

-Erythrocytic : Increase of blood viscosity

-Physical stress

-CNS disturbance : movement dysbalance-Liver damage (hepatocellular jaundice, hypoprothrombinemia - GI bleeding)

-Ulcer

-Loss of appetite (loss of body and muscular massà-Cluber fingers and hypertrophy, pulmonaey osteorthropathy

2. Hypercapnia

-Peripheral vasodilatation and hypotonia-Dilation of brain vesseks increase blood flow in CNS (CO2 narcosis)

(somnolence, stupor, coma)

B. Pulmonary symptom of systemic disease

1. Cardiogenic disease -> Pulmonary edema

2. Liver cirrosis - chronic hyperventilation, hypocapnic, hypoxemic and respiratory

alcalosis

(A-V fistula, R-L shunt -anastomosis between periesoph, bronchial and pulmo veins)

3. Severe renal insufficiency - uremic pneumonitis (retention of fluid and increase of

hydrostatic pressure in pulmo cappilaries, increase permability of cappilary wall)

4. CNS disease - Cheyne Strockes disease, hyperventilation syndrome

181. Impairment of renal blood flow

-Most common cause of renal failure.

-Due to : -hypotention

-hypovolemia-liver disease, heart failure

-renal artery stenosis

-Decrease of MGF

-Before total failure there is compensatory phase :

-decrease resistance in kidney

-increase plasma filtration

-increase osmotic pressure in peritubilar capillaries ->increase reabsorption



-When overcome all compensatory mechanism, there is failure

-increase plasma concentration of nitrogen compounds

-increase in extracellular fluid volume

-oliguria with concentrate urine

-Prerenal failure is reversible if there is no ischemic acute tubular

necrosis

182. Impairment of the glomerular function

The glomerular basement membrane isn't permeable to anions and molecules biggerthan molecular weight of 70.000

Glomerulopathies are due to :

-Immune complex accumulation (serum sickness); antibodies develop against

glomerular basement membrane (Goodpasture syndrome), bounding of antibodies to

antigens that are in flow, and are not their part (acute postinfection

glomerulonephritis)

-Sclerosis within glomerulus or matrix proliferation

-Decrease of macro glomerular filtration (Nephritic syndrome) or

increase of glomerular capillary wall (Nephrotic syndrome).

-Damage of some other nephron components

-Consequences :

-Decrease on macro glomerular filtration-Change of urine composition (hematuria, proteinuria,

limidemia)

-Nephritic edema -limited to soft tissue(face, foot, wrist) (inacute glomerulonephritis due to decrease of MGF and increase of Na and H20

retention, in chronic disease and nephrotic disease because of increase MGF permeability for proteins) because kidney components are less reabsorbed.

-Renal hypertension

Nephrotic :

-Massive proteinuria

-Hypoalbuminemia-Generalized edema

-Hyperlipidemia

Nephritic :

-Hematuria with dysmophilic red blood cells

-Dysuria, azotemia

-Hypertension



183. Nephrotic syndrome

Definition :

Massive proteinuria (over 3,5grammes per day, hypoalbuminemia, edema, hyperlipidema,hypercholesterolemia)

Due to :

-Minimal glomerular change disease (lipid nephrosis)

Degeneration od foot podocytes.

-Membranous glomerulonephropathy

Subepithelial immunoglobulin-contening deposits, degeneration of foot and thick of

glomerular basement membrane.

-Membranoproliferative glomerulopathy

Proliferation of mesangial, podocytes with degeneration of foot and endothelial cells.

Hypoalbuminemia

-Along with liver disfunction.

Nephrotic edema

-Oncodynamic, also renin-angiotensin system activation.

Hyperlipidemia-Decrease of albumin concentration that transport free fatty acids, increase of

anti-tymocyte serum develops and lipiduria, in urine also fatty cylinders : seen in tubular

cells where cytoplasm is filled with fat.

Hypercoagulation

-Loss of antithrombin III

Protein loss

-Trabsferinne, sometimes vitamin D : hypocalcic, secondary hyperproteinemia.

184. General disorders of tubular function.

Mechanism :

-Primary : acute tubular necrosis, pyelonephritis

-Secondary : consequence of glomerylopathy

-> loss of urine concentration acidity and excretion of acids

Acute tubular necrosis (ATN) :

-Postischemic :

-due to hypoperfusion (hypotension due to sepsis)-local necrosis along tubules with GMB damage



-most are cells of proximal tubules (increase of ATP utilization)

Nephrotoxic :

-due to toxins (antibiotics, metals...)

-Basal membrane preserved

Tubulointerstitial disease due to drugs

-can cause ATN, hypersensitivity reaction and cell damage

-hypersensitivity can be caused by some antibiotics and diuretics that bound to proteins of tubular cells and cause immunological reaction.

-analgesic cellular nephropathy caused by analgesic (paracetamol) that damagekidney by making free radical and inhibiting protein synthesis.

Tubulointerstitial disease caused by inflammation-acute pyelonephritis :

-ascend bacterial infection of pyelonephron and kidney-sudden with strong controvertebral pain, dysuria and fever

-complications ; chronic inflammation, pyelonephron abcess, necrotic

papillitis

-chronic pyelonephritis :

-chronic bacterial inflammation of kidney that leads to scaring

-hypertension and possible renal failure

Urate nephropathy

-Due to hyperuricosuria

-Acute : Accumulation of urates in canals, acute renal failure

-Chronic : Development of gout-Nephrolitiasis : uratic stones

Ph and concentration of urates determins which disorder develops.

Hypercalcemic nephropathy (nephrocalcinosis)

-Dystrophic or metastatic tubular calcification -> Leads to their degeneration

and increases the risk of infection.

Myelomic kidney-Complication of multiple myeloma in 50% of patients.

185. Disorder of specific tubular functions.

The most common hereditary disorders of specific tubular function are not connected

with glomerulonephropathy and don't cause renal failure.

Symptoms are are consequence of some substance loss with urine.

-Pseudohipoaldosteronism Hypovolemia, hypercalemia due to insensitivity oftubular cells to aldosterone.



-Barettes syndrome

Mutation of gene for Sodium-Potassium-Chloride transporter in thick ascending loop,

hypovolemia and compensated hyperaldosterone.

-Nephrologic diabetes insipidus

Kidneys insensible to ADH.-Proximal renal tubular acidosis

Decrease bicarbonates reabsorbtion leading to metabolic acidosis

-Distal renal tubular acidosis

Normal bicarbonate reabsorbtion, decreased ability of acidification of urine in distale

tubule leading to too high pH of urine leading to nephrocalcinosis.

-Renal glucosuria

In chronic dialyzed patients there is a decrease in maximal number of transporters for

glucose, so it appears in urine even with a normal plasma concentration.

-Cystinuria

Dibasic amino-acid lost through kidney, can cause stones.

-Fancony syndrome

Proximal tubule cells disorder, decrease absorption of substances (electrolytes and

nutrients into bloodstream).

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