General pathophysiology - metabolism

Question 1

pseudo-ruminant

Answer 1

is a classification of animals based on their digestive tract differing from the ruminants. Hippopotami and camels are ungulate mammals with a three-chambered stomach (ruminants have a four-chambered stomach) while equids and rhinoceroses are monogastric herbivores.

Like ruminants, some pseudoruminants may use foregut fermentation to break down cellulose in fibrous plant species (while most others are hindgut fermenters with a large cecum).

rabbits, guinea pigs, horses

Question 2

Protein digestion begins in the stomach with the action of an enzyme called

Secreted by what cells?

Answer 2

pepsin

Pepsin is an endopeptidase that breaks down proteins into smaller peptides.

Gastric chief cells secrete pepsin as an inactive zymogen called pepsinogen.

Question 3

Almost all the plasma proteins are synthesized in the liver with the exception of

Answer 3

immunoglobulins, which are synthesized by plasma cells.

The metabolism of plasma proteins also mainly occurs in the liver.

Question 4

The functions of proteins in cells and tissues

Answer 4

A. Physical/Structural
B. Biochemical
C. Anti-infective agents
D. Liver and muscle proteins are energy and nitrogen reserves

Question 5

2. The functions of soluble proteins in the extracellular space

Answer 5

A. Physical (Maintenance of the viscosity of body fluids (plasma, secretions; Generating oncotic pressure of body fluids)

B. Biochemical (buffering, enzyme, transport etc.)

3. Humoral protection against infection (Ig)

Question 6

The average half-life of proteins is about

Answer 6

80 days, while that of the bone marrow, liver, kidneys and plasma is 10 days.

It is considerably shorter in muscle, skin, collagen and bone tissue as well as in the haemoglobin of mature erythrocytes.

Question 7

trypsin

Answer 7

proteolytic enzyme produced in the pancreas in the precursor form of inactive trypsinogen.

Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces.

Question 8

chymotrypsin

Answer 8

is a digestive enzyme synthesized in the pancreas that plays an essential role in proteolysis, or the breakdown of proteins and polypeptides.

As a component in the pancreatic juice, chymotrypsin aids in the digestion of proteins in the duodenum by preferentially cleaving peptide amide bonds.

Question 9

carboxypeptidase

Answer 9

pancreatic enzyme

is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide.

This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins.

Question 10

aminopeptidases

Answer 10

are enzymes that catalyze the cleavage of amino acids from the amino terminus (N-terminus) of proteins or peptides (exopeptidases).

Question 11

dipeptidases

Answer 11

are enzymes secreted by enterocytes into the small intestine. Dipeptidases hydrolyze bound pairs of amino acids, called dipeptides.

Dipeptidases are secreted onto the brush border of the villi in the small intestine, where they cleave dipeptides into their two component amino acids prior to absorption.

Question 12

Nitrogen balance =

Answer 12

the difference between the total nitrogen intake by an organism and its total nitrogen loss.

Organisms have no stores of amino acids, therefore the magnitude of the nitrogen balance is determined by the difference between synthesis and breakdown of proteins.

Protein metabolism is affected by dietary and hormonal factors.

Question 13

Positive nitrogen balance

Answer 13

This means that the intake of nitrogen into the body is greater than the loss of nitrogen from the body, so there is an increase in the total body pool of protein.

Predominance of anabolic processes is related to the action of androgen and
(o)estrogen hormones, insulin and somatotropin.

Question 14

Negative nitrogen balance

Answer 14

This means that the amount of nitrogen excreted from the body is greater than the amount of nitrogen ingested.

Catabolic processes are related to the action of cortisol , thyroxine and progesterone.
Negative nitrogen balance is associated with burns, serious tissue injuries, fever, hyperthyroidism, wasting diseases, and during periods of fasting.

Question 15

Endogenous protein reserve is

Answer 15

a labile (metabolisable, easily mobilisable) protein fraction of the organism.

Such protein will be used as a source of nitrogen in case the diet does not provide adequate protein, and will be restored as soon as the protein content in the diet is sufficient.

Reserves of nitrogenous compounds are primarily created by the liver, gastrointestinal wall and muscle tissue. In fattening bulls, such protein reserves comprise about 5% of the total proteins of the organism.

up to 25% of body protein can be lost before fatal or extreme adverse effects

Question 16

PROTEINEMIA

Answer 16

The presence of protein in the blood.

The blood plasma/serum protein concentration of production animals generally ranges between 50 and 90 g/l, depending on the species, breed, age and diet as well as the fluctuations in the volume of protein and plasma.

Question 17

Relative hypoproteinemia

Answer 17

Hypoproteinemia is a condition where there is an abnormally low level of protein in the blood.

Relative hypoproteinemia is occurs when plasma protein concentrations are lower than normal, but the absolute content of protein in the vascular space is normal. This is a dilutional hypoproteinemia and is attributable to either excessive fluid therapy or excessive water intake.

Question 18

Hyperthyreosis

Answer 18

another word for hyperthyroidism

Hyperthyreosis is characterized by an increase in the activity of the thyroid gland. Enlargement of the thyroid gland is known as thyroid goiter.

Question 19

hydremia

Answer 19

an abnormally watery state of the blood.

Question 20

Relative hyperproteinemia

Answer 20

= decrease in the volume of plasma – dehydration (exicosis = loss of fluid)

e.g.
-Deprivation of water, water starvation
-Chronic diarrhea
-Excessive sweating (hyperhidrosis)

Question 21

Absolute hyperproteinemia

Answer 21

means you have abnormally high levels of protein in your blood plasma.

• γ- globulinemia due to infection
• β- and γ-globulinemia due to tissue breakdown

Question 22

Absolute hypoproteinemia

Answer 22

Absolute hypoproteinemia occurs when there is a reduction in the amount of plasma proteins in the vascular space in the presence of normal or almost normal plasma volume.

The reduced protein concentration can be the result of impaired production or accelerated loss.

• Loss due to blood loss, formation of exudate
  and transudate
• Protein deficiency/starvation
• Decline in synthesis (liver
  diseases/damage, endocrine disorders)
• Loss of plasma proteins due to proteinuria, enteritis, obstruction of lymphatic drainage and increased venous pressure

Question 23

(BLOOD) PLASMA PROTEIN CONCENTRATIONS IN DOGS AND CATS, g/l

Answer 23

54-78 g/L

Question 24

(BLOOD) PLASMA PROTEIN CONCENTRATIONS IN large ANIMALS, g/l

Answer 24

horses, pigs, cows
52 - 89 g/L

Question 25

Albumin is ? Approximately ?% of albumin is in the intracellular/extravascular space.

Answer 25

the main protein in blood plasma; also present in milk. Its half-life is inversely proportional to the plasma albumin concentration (that is, a decreased albumin content results in increased half-life, whereas increasing albumin concentrations cause the metabolic rate to increase by up to 50%). Approximately 60% of albumin is in the intracellular/extravascular space. Reduction in the plasma albumin levels results in the reabsorption of albumin into blood. Interstitial albumin acts as a (pH) buffer.

Question 26

Decreased osmotic pressure in the interstitial space and plasma stimulates

Answer 26

stimulates albumin synthesis

Question 27

Immunoglobulins, also known as antibodies, are glycoprotein molecules produced by

Answer 27

plasma cells

Question 28

The primary factor that controls immunoglobulin synthesis is

Answer 28

antigenic stimulation:

Question 29

describe dysproteinemia

Answer 29

is a clinical state characterized by abnormal, often excessive, synthesis of immunoglobulin (Ig) molecules or subunits. Dysproteinemia results from clonal proliferation of plasma cells or B lymphocytes.

Question 30

Acute inflammatory dysproteinemia

Answer 30

- Causes tissue damage of different origins - The shifts are quantitatively related to the stage of development/progress and expression of the disease - Variations in the plasma protein concentrations are the result of the changes in the synthesis rate, whereas increase and decrease in concentrations are in equilibrium.

Question 31

3 points about chronic inflammatory dysproteinemia

Answer 31

- Occurs in the chronic stage of inflammation, in the case of malignant tumours and liver diseases. - Involves an in crease in the levels of immunoglobulins usually along with hyperproteinemia. Levels of different immunoglobulin classes increase differently. - It is arguable whether the changes in the plasma protein patterns are disease-specific or not.

Question 32

*Increased oncotic pressure inhibits

Answer 32

albumin synthesis. *Albumin synthesis depends on appropriate supply of amino acids and energy.

Question 33

Urea is

Answer 33

the major end product of nitrogen metabolism. The urea cycle describes the conversion reactions of ammonia into urea, these reactions occur in the liver. Uric acid / Creatinine / Indican

Question 34

Indican

Answer 34

Indican is a tryptophan metabolite that is excreted mostly in the feces but also in small amounts in the urine as a result of absorption and detoxification of indole produced by bacterial action on tryptophan in the intestines. The presence of indican in the urine indicates amino acid malabsorption.

Question 35

Normal BUN range in farm animals

Answer 35

blood urea nitrogen 3.3–6.7 mmol/L

Question 36

Increase in BUN may be due to (4)

Answer 36

- Liver diseases; fever - Abnormal losses of fluids and electrolytes (ileus, diarrhoea, sweating, extensive burns) lead to dehydration of tissues and intensification of lytic processes in tissues - Kidney disorders may cause 2–10-fold increase – retentional hyperazotemia - Mechanical damage of tissues – productional hyperazotemia Increase in BUN causes autointoxication or uremia.

Question 37

azotemia

Answer 37

high concentrations of N compounds in blood can be pre-renal, renal or post-renal can lead to uremia

Question 38

creatinine

Answer 38

metabolic nitrogen product is a breakdown product of creatine phosphate from muscle and protein metabolism. It is released at a constant rate by the body.

Question 39

isosthenuria

Answer 39

refers to the excretion of urine whose specific gravity is neither greater nor less than that of protein-free plasma, typically 1.008-1.012. Isosthenuria reflects damage to the kidney's tubules or the renal medulla.

Question 40

causes of pre-renal azotemia (5)

Answer 40

dehydration heart dieases (hypotension - low filtration rate) shock a diet rich in protein (only elevated BUN) bleeding in the GI tract (only elevated BUN) (When GI bleeding occurs, the blood is digested to protein. This protein is transported to the liver via the portal vein, and metabolized to BUN in the urea cycle. Higher BUN values are therefore associated with the digestion of blood.)

Question 41

causes of renal azotemia

Answer 41

renal failure

Question 42

causes of post-renal azotemia

Answer 42

urinary tract obstruction bursting of the bladder

Question 43

uremia

Answer 43

is the term for high levels of urea in the blood. Uremia is often a sign of end-stage renal (kidney) disease and typically preceded by azotemia. "Azotemia is a similar, less severe condition with high levels of urea, where the abnormality can be measured chemically but is not yet so severe as to produce symptoms. Uremia describes the pathological and symptomatic manifestations of severe azotemia."

Question 44

if there are no clinical signs, only azotemia, then the patient is not considered

Answer 44

uremic

Question 45

what are the most imporant substrates for proteins.

Answer 45

amino acids can also serve as an energy source via oxidation of their carbon chain

Question 46

lactocyte

Answer 46

A milk-producing cell in the mammary epithelium. are capable of synthesizing all non-essential AA, whereas the nitrogen required for the synthesis is obtained from the arginine and glycine that have absorbed in excess in the udder as well as from ornithine and citrulline. Up to 50% of the free AA of arterial blood are absorbed in the udder. The overall AA requirement for milk secretion in the early phase of lactation exceeds that for growth and foetal development by three to four times.

Question 47

Nucleoproteins

Answer 47

complex proteins having nucleic acids as prosthetic groups. Nucleoproteins stimulate metabolic processes; are main carriers of genetic information in the nucleus; determine cellular metabolic pathways and regulate protein synthesis in the cytoplasm; affect catalytic reactions via the adenylate system. Free nucleotides function as coenzymes.

Question 48

Mononucleotides are made up of three components:

Answer 48

1. Carbohydrate (pentose sugar) 2. Heterocyclic nitrogenous base (purine- or pyrimidine bases) 3. Phosphoric acid (orthophosphoric acid)

Question 49

The purine bases

Answer 49

adenine and guanine can be found in both RNA and DNA.

Question 50

The pyrimidine nitrogen bases

Answer 50

are cytosine, thymine and uracil.

Question 51

Nucleoside

Answer 51

is a nitrogenous base (purine or pyrimidine) bound to a pentose sugar ribose or deoxyribose.

Question 52

nucleoprotein metabolism

Answer 52

Nucleoproteins are degraded into its main constituents – proteins and nucleic acids. Nucleic acids are hydrolyzed to a mixture of purine and pyrimidine bases. In the liver, purines are oxidised to uric acid that is absorbed into the blood and excreted through the kidneys in humans and primates. In most other mammals, the enzyme uricase further oxidizes uric acid to allantoin. In birds, uric acid is the end-product of the whole of nitrogen metabolism.

Question 53

Hyperuricemia

Answer 53

the presence of elevated levels of uric acid in the blood Uric acid may accumulate in the tissues and form uric acid or monosodium urate (MSU) crystals. Gout (in birds) – crystals may build up in the joints, ligaments, fascias/fasciae, but also skin, kidneys and muscles. Gout is a disorder that causes sudden attacks of intense pain preceded by a period of high uric acid levels in the blood. Gout can be triggered by acidosis or the poor supply of blood to the joints and ligaments.

Question 54

allantoin

Answer 54

is a major metabolic intermediate in most organisms including animals, plants and bacteria. It is produced from uric acid, which itself is a degradation product of nucleic acids, by action of urate oxidase (uricase)

Question 55

ruminants possess what system for nitrogen recycling?

Answer 55

Ruminants, possessing the rumino-hepatic re-circulation of nitrogen, are thought to adapt easily to quite significant fluctuations in dietary nitrogen: feeding low-nitrogen diets reduces renal excretion of endogenous urea synthesized in the liver. Urea will be recycled from the blood into the rumen either with the saliva or by diffusion through the ruminal wall.

Question 56

nitrite poisoning

Answer 56

Use of nitrogen-containing mineral and organic fertilizers may lead to the accumulation of toxic levels of nitrate in forages, e.g. sunflower, rye, cabbage, oats, beet tops etc. Nitrite poisoning occurs when green forage diets that are rich in nitrates but low in soluble hydrocarbons are fed. Treatment – use of acid to lower rumen pH.

Question 57

reduction of nitrate to

Answer 57

nitrite by bacteria takes place, mediated by nitrate reductase

Question 58

The main biological target of nitrite poisoning is

Answer 58

hemoglobin, the divalent iron of which is oxidized to the trivalent form. This leads to the formation of methaemoglobin that does not bind oxygen, and results in a functional anemia with hypoxia. Symptoms of poisoning occur when 30% of the hemoglobin is oxidized; 60% is lethal. Antidote: 4% methylene blue acts by providing an artificial electron acceptor for NADPH methemoglobin reductase so hemoglobin may return to a state in which it can bind O2 again.

Question 59

In monogastric animals, all carbohydrates are absorbed as

Answer 59

monosaccharides.

Question 60

In ruminants, the end products of the fermentation of dietary carbohydrates are what and name 3

Answer 60

the low molecular weight volatile fatty acids (acetic, propionic, butyric acids).

Question 61

amylase

Answer 61

salivary and pancreatic is an enzyme that catalyses the hydrolysis of starch into sugars.

Question 62

Blood glucose levels under physiological conditions, Ruminants

Answer 62

2.22 – 3.89 mmol/L

Question 63

Blood glycose levels under physiological conditions, Pig; chicken

Answer 63

pig 2.50 – 4.17 mmol/L Chicken 7.22 – 14.43 mmol/L

Question 64

Blood glycose levels under physiological conditions, horse

Answer 64

3.06 – 5.28 mmol/L

Question 65

Blood glycose levels under physiological conditions, dog

Answer 65

3.39 – 5.00 mmol/L

Question 66

what other compound mediates the absorption of glucose

Answer 66

Na+ Sodium-glucose cotransporter (SGLT) activity mediates apical sodium and glucose transport across cell membranes.

Question 67

glucose is excreted in urine in higher amounts than normal is called

Answer 67

Glycosuria

Question 68

Gluconeogenesis takes place mainly in

Answer 68

the liver and, to a lesser extent, in the kidneys

Question 69

Gluconeogenesis is especially important for

Answer 69

ruminants as carbohydrates are fermented/converted into volatile fatty acids in the forestomach, and very small amounts of glycose are absorbed into the blood through the intestinal wall.

Question 70

Gluconeogenesis is stimulated by

Answer 70

glucocorticoids that enhance the expression of enzymes involved in gluconeogenesis.

Question 71

where is glucagon secreted from?

Answer 71

in the pancreas by the islets of Langerhans: the A cells produce glucagon

Question 72

where is insulin secreted from?

Answer 72

in the pancreas by the islets of Langerhans: the B cells produce insulin

Question 73

islets of Langerhans D cells do what

Answer 73

D cells store somatostatin that inhibits insulin and glucagon secretion

Question 74

adrenaline secreted by

Answer 74

adrenal medulla The action of epinephrine results in hyperglycemia.

Question 75

glucocorticoids secreted by

Answer 75

adrenal cortex

Question 76

Glucagon stimulates the liver to

Answer 76

convert stored glycogen into glucose in response to low blood sugar levels aka glycogenolysis

Question 77

2 major functions of insulin

Answer 77

stimulates the peripheral cells to take up glucose stimulates the production of glycogen (storage) Glyconeogenesis is the formation of glycogen in the liver.

Question 78

How exactly does insulin encourage the uptake of glucose by peripheral cells?

Answer 78

Insulin acts by increasing the number of glucose transporters present on the plasma membrane.

Question 79

How does insulin inhibit lipolysis?

Answer 79

. Binding of insulin to fat cells inhibits lipolysis by activating lipase activity. Transfer of fatty acids into fat cells and synthesis of triglycerides will increase.

Question 80

describe diabetes mellitus

Answer 80

Diabetes is a metabolic disease that results from partial or complete deficiency of insulin, characterised by hyperglycaemia, glycosuria and impaired fat metabolism, polydipsia, weight loss, acidosis

Question 81

Primary diabetes

Answer 81

decreased pancreatic islet β-cell mass (autoimmune diseases, viral infections)

Question 82

Secondary diabetes

Answer 82

decrease in the number of insulin receptors (obesity) – excess levels of insulin circulating in the blood; lack of relevant effect

Question 83

Physiological effects of insulin deficiency (5)

Answer 83

- Inhibition of glycogen synthesis from glucose. - Inhibition of protein synthesis from AA; AA used for the synthesis of carbohydrates. - Carbohydrates are not converted to fat. - Despite hyperglycaemia, use and oxidation of glucose in tissues is impaired. - Fat is used as the primary energy source.

Question 84

Excessive use of fat as an energy source causes

Answer 84

fatty infiltration of the liver, and ketone bodies accumulate in the blood. Ketone bodies are excreted in urine (ketonuria) and cause the pH of the extracellular environment to become acidic.

Question 85

ketone bodies (3)

Answer 85

acetone, acetoacetate, β-hydroxybutyrate Intense gluconeogenesis uses substantial amounts of oxaloacetic acid, whereas acetyl coenzyme A produced during lipolysis is unused and goes on to form the ketone bodies – acetate, acetoacetate, and 3-hydroxybutyrate in the liver.

Question 86

Diabetic coma is due to

Answer 86

the accumulation of toxic ketone bodies in the blood.

Question 87

Diabetic polyuria is caused by

Answer 87

decreased/disturbed renal tubular reabsorption of glucose that leads to high osmotic pressure of primary urine; large volumes of water are excreted with the sugar.

Question 88

Diabetes insipidus

Answer 88

A rare form of diabetes caused by a deficiency of the pituitary hormone vasopressin (ADH), which regulates kidney function. Disturbed reabsorption of water in the kidneys, which leads to excretion of large amounts of severely dilute urine (not containing sugar). Due to the hypothalamic-pituitary dysfunction, the release of the antidiuretic hormone drops, that causes reduced tubular reabsorption of water.

Question 89

Carbohydrates comprise ? % of the diets fed to ruminants

Answer 89

Carbohydrates comprise 70 – 80 % of the diets fed to ruminants. Reticulorumen serves as the site for microbial fermentation of ingested carbohydrates into volatile fatty acids and other products. About 20% of the energy is lost to methane and heat produced during fermentation. Very small amounts of carbohydrates are absorbed through the intestine.

Question 90

Ruminants need ? times higher insulin doses to generate/produce hyperglycaemia, compared to humans.

Answer 90

Ruminants need ten times higher insulin doses to generate/produce hyperglycaemia, compared to humans. The levels of VFA in blood have a stronger and faster effect on insulin release compared to those of glucose or ketone bodies. Insulin has a strong effect on the utilisation of VFA and acetate in the tissues.

Question 91

consequences of insuline deficiency

Answer 91

slide 48

Question 92

Characteristic signs of ketosis comprise

Answer 92

increase in the level of ketone bodies and free fatty acids in body fluids, and hypoglycemia. Excess ketone bodies are disposed of by kidneys, udder, and lungs. Ketosis affects the structure and metabolic functions of the liver (fatty liver/steatosis).

Question 93

Insufficient gluconeogenesis to sustain a normal blood glucose concentration results in

Answer 93

hypoglycemia and decomposition of fats as a source of energy. In the course of lipolysis, the catabolism of fatty acids occurs through a process called beta-oxidation that requires the presence of oxaloacetic acid. Intense gluconeogenesis uses substantial amounts of oxaloacetic acid, whereas acetyl coenzyme A produced during lipolysis is unused and goes on to form the ketone bodies – acetate, acetoacetate, and 3-hydroxybutyrate in the liver.

Question 94

Excess dietary protein may lead to

Answer 94

ketosis in dairy cows. Excess protein induces urea synthesis in the liver with concurrent intensification of hepatic gluconeogenesis. Intense gluconeogenesis uses substantial amounts of oxaloacetic acid, whereas acetyl coenzyme A produced during lipolysis is unused and goes on to form the ketone bodies – acetate, acetoacetate, and 3-hydroxybutyrate in the liver.

Question 95

Physiological ketosis clinical signs

Answer 95

No clinical signs or symptoms; moderate hypoglycemia and ketonemia

Question 96

Subclinical ketosis or latent ketosis;

Answer 96

excretion of ketone bodies by urine and milk

Question 97

Alimentary ketogenesis occurs in

Answer 97

the ruminal epithelium – butyric acid is metabolised by the ruminal epithelium into beta-hydroxybutyric acid/beta-hydroxybutyrate. In case of a normal diet, beta￾hydroxybutyric acid produced in the rumen is metabolised by the mammary glands and muscles. Hypoglycemia does not accompany alimentary ketosis.

Question 98

how many more times energy is stored in one gram of lipids compared to carbohydrates or proteins.

Answer 98

two times more energy is stored in one gram of lipids compared to carbohydrates or proteins.

Question 99

Lipid metabolism can be divided into two basic pathways:

Answer 99

* the exogenous pathway, which is associated with the metabolism of exogenous (dietary) lipids, and the * endogenous pathway, which is associated with the metabolism of endogenously produced lipids

Question 100

name emulsifying agents (2)

Answer 100

bile acids & pancreatic lipases

Question 101

chylomicrons.

Answer 101

spesh mechanism for lipid transport Inside the enterocyte, fatty acids and monoglyceride are transported into the endoplasmic reticulum, where they are used to synthesize triglyeride. Beginning in the endoplasmic reticulum and continuing in the Golgi, triglyceride is packaged with cholesterol, lipoproteins and other lipids into particles called chylomicrons. Chylomicrons are extruded from the Golgi into exocytotic vesicles, which are transported to the basolateral aspect of the enterocyte. The vesicles fuse with the plasma membrane and undergo exocytosis, dumping the chylomicrons into the space outside the cells.

Question 102

Lipemia (lipidaemia)

Answer 102

the presence of an excess of neutral fats in the blood (> 1.14 – 2.85 mmol/L)

Question 103

Alimentary or physiological lipemia

Answer 103

caused by high-fat diet; in birds, during the egg laying period (lipids are involved in egg yolk formation).

Question 104

Pathological lipemia

Answer 104

caused by the factors which considerably contribute to depletion of glycogen reserves and fat mobilisation * Transport lipemia – reserve fat is transported to liver for oxidation (starvation, carbohydrate deficiency, asphyxia, constant pain, heavy physical load/work)

Question 105

Hyperlipidemias are also classified according to

Answer 105

which types of lipids are elevated, that is hypercholesterolemia, hypertriglyceridemia or both in combined hyperlipidemia. Elevated levels of lipoprotein may also be classified as a form of hyperlipidemia.

Question 106

causes of pathological lipemia

Answer 106

acute and chronic diffuse liver diseases, parenchymal jaundice, nephrosis, starvation, fatigue and infectious diseases

Question 107

Fatty infiltration

Answer 107

abnormal accumulation of fat droplets in the cytoplasm of cells called steatosis when its in the liver

Question 108

Fatty dystrophy

Answer 108

fatty infiltration is accompanied by cytoplasmic changes.

Question 109

Fatty transformation

Answer 109

conversion of cytoplasmic proteins into fat.

Question 110

Lipuria (lipiduria)

Answer 110

the presence of fat in the urine due to fatty dystrophy of the renal tubular epithelium.

Question 111

Hypercholesterolemia is

Answer 111

a condition characterised by very high levels of cholesterol in the blood (normal levels 2.6 – 5.2 mmol/L).

Question 112

Hypercholesterolemia is associated with

Answer 112

conditions like fat mobilisation, intoxication, kidney and liver diseases, diabetes, atherosclerosis, uremia, etc.

Question 113

There can be other causes of atherosclerotic changes beside elevated cholesterol levels – for example,

Answer 113

deficiency of phospholipids, alterations in blood/serum protein fractions, etc. In rabbits, such changes may result from a high-cholesterol diet.