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Curriculum biochem 2 part

The document outlines the digestion and metabolism of proteins and amino acids, detailing the structure and function of amino acids, the role of proteolytic enzymes, and the processes involved in protein digestion in the stomach and small intestine. It also covers the synthesis and catabolism of nitrogen-containing substances, including the urea cycle and the metabolism of various amino acids, along with hormonal regulation of metabolic processes. Additionally, it discusses the liver's role in metabolism, detoxification, and blood protein synthesis, as well as the metabolism of hemoglobin and related disorders.
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0% found this document useful (0 votes)
8 views7 pages

Curriculum biochem 2 part

The document outlines the digestion and metabolism of proteins and amino acids, detailing the structure and function of amino acids, the role of proteolytic enzymes, and the processes involved in protein digestion in the stomach and small intestine. It also covers the synthesis and catabolism of nitrogen-containing substances, including the urea cycle and the metabolism of various amino acids, along with hormonal regulation of metabolic processes. Additionally, it discusses the liver's role in metabolism, detoxification, and blood protein synthesis, as well as the metabolism of hemoglobin and related disorders.
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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Digestion of proteins.

Common pathways of metabolism of amino acids


Revise:
1. Structure of proteinogenic (standard) amino acids. Essential and nonessential amino acids.
2. Structures and functions of proteins. Peptide bond. Levels of protein structure.

Questions:
1. Nitrogen balance in human body. Changes of nitrogen balance in certain physiological and pathological
conditions.
2. Dietary proteins. Daily requirement for proteins.
3. Nutritional value of proteins. Clinical manifestation of protein deficiency in the diet. Kwashiorkor.
4. Proteolytic enzymes: classification and representatives.
5. Digestion of proteins in the stomach. Gastric juice: chemical composition and role in digestion of proteins
in the stomach.
6. Gastric acid: role, mechanism of synthesis and its regulation. Disorders of HCl production.
7. Pepsin: role in digestion of proteins in the stomach, structure, properties, synthesis, activation, regulation of
secretion. Chymosin and gastrixin.
8. Digestion of proteins in the small intestine. Enzymes and mechanism of their activation. Pancreatitis.
Parietal digestion of peptides.
9. Metabolic fate of free amino acids in the intestine. Mechanisms of amino acid absorption.
10. Catabolism of free amino acids in the large intestine by microbial enzymes. Mucosal intestinal barrier.
11. Intracellular pool of amino acid and its compounds. Glucogenic and ketogenic amino acids.
12. Common pathways of amino acid metabolism.
13. Deamination of amino acids. Oxidative deamination of glutamate and its role in amino acid deamination.
Direct and indirect oxidative deamination. Amino acid deaminases and their role.
14. Transamination of amino acids and its role. Mechanism of transamination of amino acids. Vitamin B6:
dietary sources, daily requirement, biochemical role, functions, signs of deficiency. Alanine
aminotransferase (ALT) and aspartate aminotransferase (AST) and their roles in the enzyme diagnostics.
15. Metabolism of α-keto acid (pyruvate, oxaloacetate, α-ketoglutarate) and its role.
16. Decarboxylation of amino acids. Synthesis of biogenic amines (GABA, histamine, serotonin, dopamine)
and their roles.
17. Catabolism of biogenic amines: role of monoamine oxidase and methyltransferase.

Synthesis of end products of catabolism of nitrogen-containing substances.


Hyperuricemias: those roles and causes
Revise:
1. Structure of nucleosides and nucleotides. Purine and pyrimidine nitrogenous bases.

Questions:
1. Sources of ammonia in tissues. Deamination reactions in the metabolism of biogenic amines, adenosine,
guanine, amino acids.
2. The main metabolic pathways of the ammonia detoxification in the cells. The role of the liver, kidneys and
intestine in the binding and elimination of ammonia.
3. Modern views concerning the toxicity of ammonia.
4. Transport of ammonia to the liver from other tissues. Glucose-alanine cycle.
5. Urea cycle: localization, reactions, energy requirement, net equation and role. Interaction between urea
cycle and the TCA cycle. Diagnostic role of urea levels in blood and urine.
6. Hyperammonemias: causes, clinical manifestations and principles of treatment.
7. Purine nucleotides (IMP, AMP, GMP): structure and role. Sources of nitrogen and carbon atoms for
synthesis of the purine ring. Regulation of the purine nucleotide synthesis.
8. Catabolism of purine nucleotides. Synthesis of uric acid. Xanthine oxidase. Reutilization of hypoxanthine
and guanine, and its role.
9. Primary and secondary hyperuricemias, their causes, clinical manifestation and principles of treatment.
Urolithiasis. Gout. Lesch-Nyhan syndrome.
10. Pyrimidine nucleotides (OMP, UMP, CMP, dTMP): synthesis and its regulation.
11. Mechanism of deoxyribonucleotide synthesis. Ribonucleotide reductase complex of enzymes.
12. Synthesis of dTMP. The role of folic acid and tetrahydrofolate. The use of inhibitors of mononucleotide
synthesis as chemotherapeutic drugs for the treatment of tumors.

Metabolism of some amino acids


For self-study:
1. Disorders of metabolism of Leu, Ile, Val.

Questions:
1. Metabolism of dicarboxylic amino acids (glutamate and aspartate) and their amides. Involvement of these
amino acids into the TCA cycle.
2. Metabolism of tryptophan. Synthesis of serotonin. Hartnup disease.
3. Metabolism of glycine and serine.
4. The interaction between metabolism of glycine, serine, cysteine, and methionine. Role of vitamins B 6, B9
and B12.
5. Homocysteinemia and homocystinuria: causes and principles of treatment.
6. The scheme of cysteine metabolism. Cystinosis: cause and clinical manifestations. Cystinuria.
7. Metabolism of phenylalanine and tyrosine. Hereditary disorders of phenylalanine and tyrosine catabolism.
Phenylketonuria: causes, mechanism of pathogenesis, clinical manifestations, biochemical diagnostics and
principles of treatment.
8. Biosynthesis of catecholamines from tyrosine. The role of cathecholamines.
9. Synthesis of melanins from dihydroxyphenylalanine.
10. Albinism: causes, biochemical aspects of pathogenesis and principles of treatment.
11. Catabolism of tyrosine and its hereditary disorders. Tyrosinemias and alcaptonuria: causes, clinical
manifestations, diagnostics and principles of treatment.
12. Arginine in the synthesis of urea, creatine, nitric oxide (NO) and polyamines (spermine and spermidine).
Histones and their role.
13. Anabolic role of amino acids. Synthesis of creatine and creatine phosphate. The role of creatine phosphate.
Creatinine and its role in diagnostics.

COLLOQUIUM “Metabolism of proteins”

Hormones: definition, classification, biological role. Mechanism of primary effects of hormones.


Hormones of the hypothalamus, pituitary gland, adrenal gland, and thyroid gland.

Questions:
1. Hormones. Hierarchy of regulatory systems.
2. Principles of regulation of metabolic processes. The mechanism of negative feedback in the regulation of
hormone synthesis.
3. Classification of hormones according to chemical structure.
4. Target organs for hormones. Hormonal receptors: peculiarity of structure and intracellular localization.
5. Classification of the hormones according to the mechanism of their regulatory effect.
6. Cytosolic (intracellular) mechanism of hormonal effect on target cells. Examples of such hormones.
7. Membrane-intracellular mechanism of hormonal effect on target cells. Examples of such hormones.
Adapter and effector proteins, second messengers.
8. Adenylate cyclase mechanism of hormonal action: hormones, second messenger, enzymes and processes
regulated by this mechanism. G-protein. The role of activator and inhibitor isoform of α subunit of G
protein. Metabolism of cAMP. Mechanism of protein kinase A activation. The transcription factor CREB.
9. Mechanism of regulatory effect of hormones, which is realized through activation of phospholipase C:
examples of hormones, second messengers (inositol triphosphate, diacylglycerol, and calcium), protein
kinase C. Mechanism of an increase of calcium level in cytoplasm.
10. Receptors associated with tyrosine kinase activity: an enzymatic cascade that is associated with the
activation of Ras-protein.
11. The hypothalamic–pituitary–adrenocortical system: biological role, components, regulation. Derivatives of
proopiomelanocortin - hormones, endorphins, enkephalins. ACTH (structure, regulation of the synthesis
and secretion, mechanism of effects for target organs).
12. Hormones of adrenal cortex. Glucocorticoids (representatives, structure, main stages of synthesis,
regulation of synthesis and secretion, mechanism of effects on the target organs, metabolic effects, using as
medicines). Hypo- and hyperproduction of glucocorticoids: metabolic disorders, clinical manifestation.
Principles of diagnosis and treatment.
13. Hypothalamic-pituitary-thyroid system: biological role, components, regulation.
14. Thyroid-stimulating hormone (structure, regulation of synthesis and secretion, mechanism of effects for
the target organs, metabolic effects).
15. Thyroid hormones (representatives, structure, transport in the blood, main stages of synthesis, regulation of
synthesis and secretion, mechanism of effects on the target organs, metabolic effects, using as medicines).
16. Hypo- and hyperthyroidism: metabolic disorders, biochemical aspects. Principles of diagnosis and
treatment.
17. Growth hormone (structure, regulation of secretion, role). Hypo- and hyperproduction of growth hormone -
metabolic disorders, clinical manifestation.
18. Cytokines: properties, classification, mechanism of regulatory effects on metabolism. The main subgroups
of cytokines:
 interleukins, sources, the functions. Proinflammatory (IL-1, IL-6, IL-8) and anti-inflammatory (IL-4,
IL-10) interleukins;
 tumor necrosis factors, representatives (TNF-α, TNF-β,), sources, and role;
 growth factors: transforming growth factor β (TGFβ), epidermal growth factor, (EGF), insulin-like
growth factor (IGF1), fibroblast growth factor (FGF), endothelial growth factor (VEGF), sources, role;
 colony stimulating factors (G-CSF, M-CSF, GM-CSF), sources, role;
 chemokines: representatives (IL-8, RANTES), sources, role;
 interferons: representatives (IFNα, IFNβ, IFNγ), sources, role.

Insulin; mechanism of metabolic effects. Diabetes mellitus. Epinephrine and glucagon.

Questions:
1. Hormones of the pancreas.
2. Insulin: stages of synthesis, regulation of secretion (the role of glucose-dependent intracellular
mechanisms, nervous system and the adrenergic effects), target organs, mechanism of regulatory effects of
insulin, glucose transporters, their types and tissue localization, molecular effects of insulin - the metabolic
and mitogenic pathway (enzymatic cascade that is associated with the activation of Ras-protein; enzymatic
cascade that is associated with the activation of phosphoinositol-3-kinase and protein kinase B (AKT).
3. Diabetes mellitus type 1 and 2. Similarities and differences of metabolic disorders in both types of diabetes.
Causes of insulin resistance.
4. The biochemical diagnostics of diabetes: glucose tolerance test, concentration of glycosylated hemoglobin
(HbA1c) and C-peptide.
5. The biochemical causes of acute and chronic complications of diabetes. Principles of treatment.
6. Glucagon (structure, synthesis, regulation of synthesis and secretion, mechanism of effects on the target
organs, metabolic effects).
7. Epinephrine (structure, synthesis, regulation of synthesis and secretion, adrenergic receptors, mechanism of
effects on the target organs, metabolic effects, using as medicines). Hyperproduction of epinephrine –
causes, metabolic disorders, principles of diagnostic and treatment.

COLLOQUIUM "Hormones"

Role of the liver in the metabolism of carbohydrates, lipids and proteins. Liver role in detoxification.
Blood proteins. Acute phase proteins and their role.
Revise:
1. The anatomical and histological structure of the liver. Function of liver.

Questions:
1. The role of the liver in the metabolism of proteins and other nitrogen-containing compounds: synthesis of
blood proteins, metabolism of amino acids, detoxification of ammonia and urea synthesis. Diagnostic tests
(urea, creatinine, plasma proteins), physiological range, clinical and diagnostic value.
2. Plasma proteins: albumin, α1- and α2-globulins, β-globulins, γ-globulins.
3. The main proteins of each fraction, their functions:
 α1-globulins - α1-antitrypsin, α1-antichymotrypsin, α1-fetoprotein, orosomucoid,
 α2-globulins - α2-macroglobulin, haptoglobin, ceruloplasmin,
 β-globulins - transferrin, hemopexin
4. Plasma enzymes that are synthesized in the liver - ceruloplasmin, pseudo-cholinesterase, their functions.
Kallikrein-kinin system. Coagulative, fibrinolytic and anticoagulant systems, complement system.
5. Acute phase proteins (C-reactive protein, α1-antitrypsin, haptoglobin, alpha-2 macroglobulin).
6. The role of the liver in carbohydrate metabolism:
 homeostasis of blood glucose, hormonal and metabolic regulation.
 diagnostic tests (blood glucose, glucose tolerance test), physiological range, clinical and diagnostic
value.
7. Role of the liver in lipid metabolism:
 the main stages of the synthesis of triacylglycerols, cholesterol, phospholipids, their hormonal and
metabolic regulation.
 lipoproteins formed in the liver, their structure and the role.
 fatty liver disease, its cause.
 diagnostic tests (cholesterol, TAG, HDL-C, LDL-C, atherogenic index), physiological range, clinical
and diagnostic value.
 diagnostic value of apoA-1, apo B, lipoprotein (a).
8. The role of the liver in the synthesis of biologically active substances (25–hydroxycholecalciferol,
somatomedins), in the formation of bile acids and bile pigments. The synthesis of creatine.
9. The role of the liver in digestion. The composition of bile and its role. Structure and types of bile acids and
the reactions of their synthesis. Causes of disorders of synthesis and secretion of bile.
10. Role of liver in the inactivation of insulin, thyroid and steroid hormones. The role of the liver in the growth
hormone effects.
11. The biotransformation of xenobiotic compounds. The role of the liver, its interaction with other organs.
12. The scheme of the process of microsomal oxidation. NADPH-dependent and NADH-dependent pathways.
Sources of NADH and NADPH, the components of the electron-transport chains. The role of cytochrome
P450. The substrates of microsomal oxidation. Inducers and inhibitors of microsomal oxidation.
13. The process of conjugation. The structure of UDP-glucuronic acid and phosphoadenosine phosphosulfate.
Reactions of formation of conjugated bilirubin and indican. Glycine conjugation, its role.
14. Metabolism ethanol. Alcohol dehydrogenase and MEOS pathways. Toxicity of acetaldehyde. Causes of
lactic acidosis, ketoacidosis and hypoglycemia in alcohol intoxication.
15. Possible amplification of toxic properties of compounds after biotransformation.

The role of the liver in the pigment metabolism. Metabolism of hemoglobin. Porphyrias and thalassemia.
Jaundices. Markers of syndromes of cytolysis, cholestasis, hepatocellular insufficiency.

1. Hemoglobin, its structure and properties, physiological and pathological types of hemoglobin.
2. Regulation of hemoglobin binding to oxygen - cooperative effect, Bohr effect, the role of 2,3-
diphosphoglycerate.
3. Oxygen saturation curve of hemoglobin, the cause of its sigmoidal shape. Changes under different
conditions.
4. The structure and synthesis of heme. Formation of porphobilinogen, scheme of synthesis of protoporphyrin
IX and its transformation into a heme. The role of ferrochelatase. Regulation of the process.
5. Disorders of the synthesis of heme and hemoglobin: porphyria and thalassemia.
6. The degradation of hemoglobin and formation of bilirubin in the reticuloendothelial system. Transport of
bilirubin to the liver.
7. Stages of bilirubin metabolism in the liver. The role of the enzyme UDP-glucuronyl transferase.
8. Stages of bilirubin metabolism in the intestine.
9. Conditions associated with excessive disintegration of hemoglobin. Causes of hemolytic jaundice,
laboratory diagnostics.
10. Conditions associated with impaired outflow of bile. Causes of obstructive jaundice, laboratory diagnostics.
11. Disorders of hepatocyte function. Causes of parenchymal jaundice, laboratory diagnostics.
12. Physiological neonatal jaundice.
13. Pathological jaundice:
 hemolytic jaundice, its causes.
 hereditary disorders excretion of bilirubin - Gilbert's syndrome, Dubin-Johnson syndrome, Crigler-
Najjar syndrome.
 obstructive jaundice due to cystic fibrosis, Niemann–Pick disease, hypoplasia of the biliary tract.
14. Biochemical markers of syndromes:
 hemolysis (haptoglobin, bilirubin)
 cytolysis (aldolase, Gl-6-phosphate DG, LDH-5, ALT, AST, bilirubin)
 cholestasis (alkaline phosphatase, bilirubin, 5'-nucleotidase, gamma-glutamyltransferase).
Biochemistry of blood: transport of oxygen, metabolism of iron, anemias, acid-base balance.

Questions for the extracurricular work:


1. Electrolytes in blood plasma:
 Sodium, potassium, calcium, phosphorus, iron, chloride. Distribution of ions in body fluids. What
factors influence on concentration of these electrolytes in the blood plasma?
 Iodine, copper, magnesium, manganese, zinc, cobalt, selenium. Role in metabolism.

Questions:
1. Metabolism of iron: daily requirement, nutritional sources, mechanism of absorption, transport in the blood,
mechanism of transport across the cell membrane, storage form. Iron-containing proteins.
2. Regulation of iron metabolism. The role of hepcidin and cytokines.
3. Deficit of iron and excess of iron in organism: causes, biochemical effects and clinical manifestations.
Hemochromatosis. Iron deficiency state.
4. Role of blood in transport of oxygen. The scheme of reactions occurring in the erythrocyte in capillaries of
the lungs and in peripheral tissues.
5. Transport of carbon dioxide. The role of carbonic anhydrase. An influence of processes in erythrocytes on
concentration of bicarbonate in plasma.
6. The mechanism of binding of the heme of hemoglobin with oxygen, the role in the regulation of acid-base
balance.
7. Acid-base status of the blood. The role of the constant concentration of H+ ions. Sources of H+ ions in
cells.
8. Key indicators of acid-base balance (pH, pCO2, pO2, HbO2, SO2, anion gap), normal range.
9. Effect of the liver, secretion of stomach, pancreas and intestine on acid-base status of the body.
10. The chemical mechanisms of regulation of acid-base status. The buffer system of blood (phosphate buffer,
proteins, bicarbonate buffer, hemoglobin).
11. Physiological compensation of acid-base imbalance - the role of the lungs, kidneys and bones.
12. Respiratory acidosis and alkalosis, metabolic acidosis and alkalosis, their causes. Changes of the main
indicators of acid-base status in acidosis and alkalosis. Renal tubular acidosis.
13. Changes of acid-base balance and the mechanism of their chemical and physiological compensation:
diabetes, pneumonia, hypoxia, ethanol poisoning, severe vomiting, diarrhea, bronchial asthma attack,
chronic bronchitis, chronic renal insufficiency (decreased renal filtration and reabsorption), traumatic brain
injury leading to stimulation of respiratory center, rise high in the mountains, heart failure.

System of hemostasis
Questions for the extracurricular work:
1. Extravascular fluids, their role in the body. Lymph, its composition, functions.
2. ABO blood groups. Rh factor.
3. Platelets: origin, structure and functions.
4. Endothelium, its structure.

Questions:
1. System of hemostasis: role, components.
2. Role of endothelium in hemostasis.
 Anticoagulant properties of intact endothelium.
 Pro-coagulant properties of activated endothelium.
 Factors secreted by endothelium (von Willebrand factor, plasminogen activator inhibitor (PAI-1),
thrombomodulin, tissue factor pathway inhibitor (TFPI)).
3. Subendothelium and its role in hemostasis (tissue factor, collagen).
4. Role of platelets in the blood clotting process. Platelet receptors (GPIIbIIIa, GPIb), their ligands and
functions. Von Willebrand's disease.
5. Vascular-platelet hemostasis. Stages:
 Adhesion. The main adhesion molecules (von Willebrand factor, collagen).
 Activation. The mechanism of platelet activation, changes in the process of platelet activation (shape
change, increased intracellular calcium concentration, excretion of alpha granules and dense granules,
expression of GPIIbIIIa).
 Aggregation.
6. Plasma coagulation proteins (fibrinogen - I, serine proteases - II, VII, IX, X, XI, XII, cofactors - V, VIII,
transglutaminase - XIII). General characteristics. Hemophilia A and B.
7. Vitamin K-dependent coagulation factors - II, X, VII, IX, protein C, protein S. Mechanism of γ-
carboxylation of Glu residues, regeneration of 2,3-epoxide of vitamin K. Physiological role of γ-
carboxylation. Warfarin, the mechanism of action, the main side effects of warfarin.
8. Vitamin K, food sources, daily requirement, biochemical functions, causes and symptoms of deficiency.
9. The classic coagulation cascade
 Extrinsic pathway.
 Intrinsic pathway.
 Formation of prothrombinase.
 Formation of thrombin. Functions of thrombin.
 The conversion of fibrinogen to insoluble fibrin. The role of thrombin and factor XIII.
 New oral anticoagulants (NOAC) - dabigatran, rivaroxaban, mechanism of action.
10. Anticoagulants:
 Tissue factor pathway inhibitor (TFPI).
 Antithrombin III. The role of heparin.
 Proteins C and S.
11. The cell model of blood coagulation, the basic processes occurring at each stage. Stages:
 Initiation
 Amplification
 Propagation
 Fibrin formation
12. The system of fibrinolysis. Characteristics of fibrinolytic factors (plasminogen, tissue plasminogen
activator, urokinase). Degradation of fibrin under the influence of plasmin. Regulation of fibrinolysis.
Fibrinolysis inhibitors (plasminogen activator inhibitor type 1 (PAI-1), thrombin-activatable fibrinolysis
inhibitor (TAFI)). Streptokinase and tranexamic acid.
13. Laboratory test for hemostasis (platelet count, platelet aggregation, D-dimer, prothrombin time (INR),
APTT, thrombin time, fibrinogen concentration). The concept of viscoelastic tests (thromboelastography /
thromboelastometry).

COLLOQUIUM “Biochemistry of liver and blood”

Biochemistry of kidney. Calcium-phosphorus metabolism and its regulation.


Biochemistry of nervous tissue.
Revise material:
1. The structure of nephron.

Questions:
1. Metabolism of the kidneys. Features and differences of metabolism in renal cortex and in renal medulla.
Aerobic and anaerobic oxidation processes, their localization in the kidney. Gluconeogenesis. Role of
enzymes in kidneys – glycine amidino transferase, glutamate dehydrogenase, glutaminase, alkaline
phosphatase, isoenzymes of lactate dehydrogenase, renin.
2. Role of kidneys in the synthesis of biologically active substances (creatine, erythropoietin, 1,25-
dihydroxycholecalciferol bradykinin, urokinase). The processes of formation of urine: filtration,
reabsorption and secretion.
3. Water balance. The role of the skin, lungs, gastrointestinal tract and kidneys in removing of water. Factors
of water balance in the body - blood osmolality, volume of blood, blood pressure, concentration of sodium
and potassium. The regulation of water reabsorption. The role of antidiuretic hormone. Hypoproduction of
antidiuretic hormone, manifestations.
4. The regulation of sodium reabsorption. Renin-angiotensin-aldosterone system (RAAS). The scheme, role of
the RAAS in sodium reabsorption. The mechanism of arterial hypertension in renal hypoperfusion.
5. The role of the kidneys in maintaining the acid-base status – reabsorption of bicarbonate, secretion of H+,
ammonium, excretion of organic acids.
6. General properties of urine: quantity, color, clarity, relative density, pH. Changes in pathological situations.
Organic and inorganic components of urine. Pathological components - protein, glucose, bile pigments,
ketones, erythrocytes, enzymes.
7. Regulation of phosphorus and calcium metabolism. Parathyroid hormone, calcitonin, calcitriol. Localization
of synthesis, regulation of synthesis and secretion and mechanism of effects.
8. Biochemistry of nervous tissue. Features of the transport of substances through the blood-brain barrier.
Features of brain metabolism. The mechanism of nerve impulse transmission.
Biochemistry of muscle tissue. Biochemistry of myocardium. Laboratory markers of the diseases.
For extracurricular study:
1. The main types of muscle tissue.
2. Structure of cells of muscle tissue.
3. The structure of the muscle fiber
4. Features, stage and the chemistry of muscle contraction. The regulation of contraction and relaxation of
muscles.

Questions:
1. Muscle proteins. The structure of the myofibrils and myofibrillar proteins. Structure and properties of
myosin. Structure of the thick filament. The enzymatic activity of myosin.
2. Thin (actin) filaments, structure, composition. Function of troponin subunits.
3. Myoglobin, its structure and function.
4. Energy supply for muscle contraction.
5. Changes in metabolism during muscular work. Features of metabolism in muscle tissue. Types of muscles.
6. The effect of hormones on muscle metabolism.
7. Features of the biochemistry of the myocardium and the smooth muscle. The regulation of contractility and
relaxation of smooth muscle.
8. Peculiarities of structure and metabolism of myocardium. The role of oxygen for the myocardium.
Metabolic disorder of the heart muscle in patients with coronary disease. Effects of reactive oxygen species
and lipid peroxidation on the myocardium.
9. Myocardial biochemical changes in patients with coronary heart disease. Markers of acute myocardial
infarction.
10. Modern laboratory markers of heart failure. Biochemical markers of prognosis of heart failure.

Biochemistry of the connective tissue and adipose tissue. Biochemistry of the control of the body weight.
Revise:
1. Types of connective tissue.
2. The functions of connective tissue.
3. Types of adipose tissue, its localization and function.

Questions:
1. Fibrous proteins of connective tissue - collagen, elastin: their structure, amino acid composition, functions.
2. Stages of collagen synthesis. Intracellular glycosylation and hydroxylation reaction, the role of the iron ions
and ascorbic acid. Extracellular formation of collagen fiber.
3. Fibronectin, structure, function, ligand-binding sites. Receptor for fibronectin.
4. Types of metalloproteinases (collagenases, gelatinases, stromelysins). Role of metalloproteinases in the
breakdown of proteins of the extracellular matrix. The regulation of their activity.
5. Glycosaminoglycans, types, peculiarities of the structure, properties and functions. Glycoproteins and
proteoglycans.
6. Adipose tissue and its types.
7. Metabolism of carbohydrates and lipids in white adipose tissue, its hormonal regulation. The role of
lipoprotein lipase.
8. Effect of insulin on the metabolism of white adipose tissue. Type 2 diabetes mellitus. Insulin resistance.
9. Endocrine function of white adipose tissue (hormones - leptin, estrogen, resistin, angiotensinogen,
adiponectin; cytokines - interleukin-6, tumor necrosis factor α; acute phase proteins – haptoglobin).
10. Control of body weight: leptin, neuropeptide Y, ghrelin.
11. Brown and beige adipose tissue, their function. Peculiarities of metabolism and regulation of the activity of
brown and beige adipocytes. Role of UCP-protein.

COLLOQUIUM “Biochemistry of tissues”

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