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SYLLABUS

FOR STUDENTS OF THE FACULTY MEDICINE NR.2

Name of the Course: Biochemistry Code of the course: F.03.O.023, F.04.O.029 The type of course: Compulsory discipline The total number of hours – 170 hours including lectures – 68 hours, practical classes – 102 hours Number of credit-tests provided for the course: 11 credits Teaching staff: Tagadiuc Olga, MD, PhD, associate prof., head of the Department Rîvneac Elena, PhD, associate prof., respons. for English groups Gavriliuc Ludmila, MD, PhD, prof. Bobcova Svetlana, PhD., associate prof. Simionic Eugen, PhD, lecturer Timercan Tatiana, lecturer

Chi in u 2014

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I. The purpose of the Clinical biochemistry discipline is to:

study of the structure of chemical compounds and constituents of living matter, the

fundamental metabolic processes underlying the functioning of living organisms, diseases caused by deficiencies of enzymes involved in metabolic processes; molecular mechanisms of inherited and acquired diseases;

obtaining skills of biochemical investigations to apply them in practice; training skills in analysis and interpretation of laboratory data; developing the capacity of selection and indication of biochemical investigations in

dependence on the history and clinical picture. II. The objectives of the discipline Biochemistry in training medical students: a) at the level of knowledge and understanding :

• to learn the structure and physico-chemical properties of the main chemical compounds of medical interest; • to know basic metabolic processes of viability and reproduction in the human body; • to know structural and metabolic particularities of organs and organ systems in physiological conditions and in major hereditary and acquired diseases; • to understand neuro-endocrine mechanisms of metabolism regulation that underlie the maintenance of normal body activity; • to understand the influence of different factors (vitamins, drugs) on the main metabolic processes; • to know normal physiological variations of the key biochemical indices; • to understand the clinical and diagnostic value of the changes in biochemical parameters; • to select a proper biochemical examination for determination of a clinical diagnosis.

b) at the level of application: • to determine biochemical parameters to use in clinical diagnostics; • to be able to use the main tools in biochemical laboratory (simple and automatic pipettes, pH meters, spectrophotometers, centrifuges etc.). • to assess usefulness of certain biochemical investigations in the diagnostics of diseases; • to apply algorithms of biochemical investigation specific to a certain diseases; • to give reasons for the need of certain biochemical investigations in specific biochemical disorders; • to give a correct interpretation of biochemical test results.

c) at the level of integration: • to appreciate the importance of Biochemistry in medical context and its integration with basic and clinical disciplines; • to understand the relationships and interdependence of structural biochemistry, general clinic; • to assess the progress of metabolic processes and their disorders that determine the development of various pathologies; • to demonstrate different mechanisms regulating metabolic processes both in norm and in pathology; • to assess the utility of evaluation of some biochemical parameters in certain nosologic units;

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• to apply biochemical investigations algorithms in dependence on subjective and objective condition of the patient; • to evaluate the results of laboratory investigations in conformity with clinical examination and functional data for making a diagnosis; • to define purposes of a scientific research in biochemistry, to develop specific research projects and to base their applicability in clinical practice.

III. Conditioning and preliminary requirements:

Biochemistry is a biological and medical discipline; it’s study at the university will

enable future doctors to know the molecular basis of metabolic and physiological processes, biochemical mechanisms regulating all vital functions, to understand the causes and pathogenesis of hereditary and acquired diseases, to give reasons of the necessity of biochemical investigations, to interpret laboratory results and to correlate them with clinical and functional data for a diagnosis, correction of hygiene and nutrition and indications for a therapy adapted to the biochemical mechanisms producing pathology.

The discipline requires deep knowledge of chemistry and biology, obtained during the undergraduate studies and in bioorganic chemistry, molecular biology, human genetics, and histology, obtained in previous years of study.

IV. Basic contents of the course: A. Theoretical classes: I semester

Theme Hours 1 The role of biochemistry in the medical education system. Chemical structure,

classification and biological role of proteins. 2

2 Physical and chemical properties of proteins. Methods of separation, purification and determination of proteins.

2

3 Chemical nature and structure of enzymes. Mechanism of action of enzymes. Nomenclature and classification of enzymes. Vitamins as coenzymes.

2

4 Enzyme properties. Regulation of enzyme activity. Enzymes in diagnostics and therapy. Methods of separation, purification and determination of enzyme activity.

2

5 Nucleic acids: chemical structure, biological role, physical and chemical properties.

2

6 The central dogma of molecular genetics. Replication. DNA repair. Mutations. 2 7 Transcription. Reverse transcription. Transcription regulation. Gene

engineering. 2

8 Protein biosynthesis. Regulation of protein biosynthesis. Protein polymorphism. Hereditary diseases and their biochemical diagnostics.

2

9 General metabolism. Energy metabolism. Oxidative decarboxylation of pyruvic acid.

2

10 Krebs cycle: the role; reactions; regulation 11 Biological oxidation. Respiratory chain and oxidative phosphorylation.

Microsomal oxidation. 2

12 Carbohydrates: biological role and classification. Digestion and absorption of carbohydrates. Diseases caused by disorders of digestion and absorption of

2

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carbohydrates. Glycogen metabolism.

13 Aerobic and anaerobic glycolysis: reactions, regulation, energy balance. Alcoholic fermentation. Shuttle systems malate-aspartate and glycerol phosphate.

2

14 Gluconeogenesis: reactions, regulation, energy balance. 2 15

Pentose phosphate pathway. Fructose and galactose metabolism. 2

16 Regulation of carbohydrate metabolism. Disorders in carbohydrate metabolism. Methods for assessing glucose metabolism.

2

17 Lipids: classification, chemical structure, properties, biological role. Biological membranes.

2

II semester

Theme Hours 1 Digestion and absorption of lipids. Disorders in digestion and absorption of

lipids. Structure and functions of bile acids. Resynthesis of lipids in the intestinal epithelium. Plasma lipid transport. Lipoprotein metabolism. Biomedical role of lipoproteins.

2

2 Tissue catabolism of lipids. Beta-oxidation of fatty acids. Energy efficiency of fatty acids oxidation. Oxidation of glycerol. Catabolism of phospholipids and glycolipids. Hereditary tissue lipidoses.

2

3 Lipid biosynthesis. Biosynthesis of fatty acids, triglycerides, phospholipids, cholesterol. Biosynthesis and use of ketone bodies

2

4 Regulation of lipid metabolism. Hereditary and acquired pathology of lipid metabolism. Eicosanoids: representatives, synthetic pathways, role in inflammation, thrombogenesis. Liposoluble vitamins.

2

5 Biological membranes. Structure, functions, properties. Membrane transport: types, clinical and pharmacological implications.

2

6 Simple protein metabolism. Dynamic state of proteins. Nitrogen balance. Digestion and absorption of proteins. Amino acids putrefaction in the intestine.

2

7 General pathways of metabolism of amino acids: deamination, transamination and decarboxylation.

2

8 End products of nitrogen metabolism. Ammonia detoxification. Ureogenesis. Ammonia toxicity: mechanisms and clinical implications. Hyperammonaemia and uremia.

2

9 Specific features of some amino acid metabolism. Biosynthesis of non-essential amino acids. Hereditary pathology of some amino acids.

2

10 Regulation and pathology of simple proteins metabolism. Relationship between the metabolism of carbohydrates, lipids and proteins.

2

11 Purine and pyrimidine nucleotide metabolism. Gout. 2 12 Structure, digestion and metabolism of chromoproteins. Icteric syndrome:

molecular mechanisms and biochemical diagnosis. 2

13 Hormones, biological role, classification, mechanism of action. Neuro-hormonal regulation of metabolism. Hypothalamic-pituitary hormones. Parathyroid hormone.

2

14 Pancreas and thyroid hormones. Structure, biosynthesis, regulation of secretion, metabolic role. Diabetes mellitus: types, mechanisms of onset, metabolic

2

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disorders, diagnosis. Hypo-and hyperfunction of the thyroid gland.

15 Adrenal hormones. The structure, biosynthesis and regulation of secretion, metabolic role. Hypo-and hyperfunction of adrenal cortex. Sex hormones. Structure, metabolic role.

2

16 Biochemistry of blood. Composition of blood plasma. Plasma proteins, blood enzymes, residual nitrogen, non-proteic nitrogenous substances, mineral compounds.

2

17 The blood transport of gases. Acid-base balance. Clotting: coagulation factors, mechanisms. Anticoagulant and fibrinolytic systems. Coagulopathies, trombocytopathies.

2

B. Practical classes: I semester

N Theme Hours

1. Introductive conversation. Importance of biochemistry for medical disciplines. Amino acids - structure, classification, biomedical role. Color reactions of amino acids and proteins.

3

2

Protein structure. Classification of proteins. The general characteristic of simple and conjugated proteins. Identification of amino acids by paper chromatography method.

3

3

Physical and chemical properties of proteins. Methods of separation and purification of proteins. Methods of separation, purification and determination of proteins.Dialysis of proteins.

3

4

Chemical nature and structure of enzyme. Vitamins as coenzymes. Mechanisms of enzymes action. Isoenzymes - biomedical implications. Identification of vitamins B1, B2, B6, PP (B5).

3

5 General properties of enzymes. Principles of enzyme activity determination. alpha-amylase activity determination.

3

6 Test on chapter I "Protein Chemistry" and "enzymes" 3 7

Nucleic acids: the role, the chemical structure. Biosynthesis of DNA (replication). DNA repair. Quantitative determination of DNA.

3

8. Transcription. Reverse transcription. Transcription regulation. Quantitative determination of RNA.

3

9. Genetic code. Protein biosynthesis. Determination of total protein in serum. 3 10 Test on chapter "Nucleic acids" 3 11 Metabolism: role, phases, stages. Oxidative decarboxylation of pyruvic acid.

Krebs cycle. Determination of pyruvate in the urine. 3

12 Biological oxidation. Respiratory chain and oxidative phosphorylation. Qualitative and quantitative determination of catalase. Determination of Krebs cycle dehydrogenases activity.

3

13 Carbohydrates classification and biological role. Digestion and absorption of carbohydrates. Glycogen metabolism. Determination of carbohydrates in biological fluids.

3

14 Glucose metabolism.Glycolysis and aerobic oxidation of glucose. Gluconeogenesis. Determination of the fructose-1,6-diphosphate aldolase activity in blood serum.

3

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15 Pentose phosphate pathway. Fructose and galactose metabolism. Reaction of

aldoses and ketoses differentiation. 3

16

Regulation of carbohydrate metabolism. Hereditary and acquired disorders of carbohydrate metabolism. Glucose determination in blood serum..

3

17

Test on chapters "Bioenergetics" and "Carbohydrate metabolism". 3

II semester:

Theme Hours 1 Structure, classification and functions of lipids. Biological membranes.

Determination of triglycerides in blood serum. 3

2 Digestion and absorption of lipids in the digestive tract. Plasma lipoproteins. Oxidation of lipids (triglycerides, glycerol, fatty acids). Determination of bile acids. Determination of lipase activity in serum.

3

3 Lipid biosynthesis in tissues: the biosynthesis of fatty acids, triglycerides, phospholipids, cholesterol. Biosynthesis and use of ketone bodies. Determination of ketone bodies in urine. Determination of cholesterol in blood serum.

3

4 Liposoluble vitamins. Eicosanoids. Regulation of lipid metabolism. Lipid metabolism pathology. Determination of beta-lipoproteins in blood serum.

3

5 Test on chapter: "Lipid metabolism" 3 6 Simple protein metabolism. Nitrogen balance. Digestion and absorption of

proteins. Amino acids putrefaction in the intestine. Decarboxylation of amino acids in the tissues. Determination of gastric acidity.

3

7 General pathways of metabolism of amino acids: deamination and transamination. The end products of nitrogen metabolism. Ammonia toxicity - medical implications. Ammonia detoxification mechanisms. Determination of aminotransferases activity in serum (ALAT and ASAT). Determination of urea in blood serum and urine.

3

8 Specific metabolism of amino acids. Biosynthesis of amino acids. Adjusting simple protein metabolism and pathology. Determination of creatinine in blood serum and urine. Homogentisic acid determination in urine.

3

9 Purine and pyrimidine nucleotides metabolism. Gout. Determination of uric acid in blood serum and in urine.

3

10 Chromoproteins structure and metabolism. Icteric syndrome. Relationships between the metabolism of carbohydrates, lipids and proteins. Determination of serum total and direct bilirubin.

3

11 Test on chapter “Metabolism of simple and conjugated proteins." 3 12 Hormones, biological role, classification, mechanism of action. Hormonal

regulation of metabolism. Hypothalamic-pituitary hormones, parathyroid hormones. Determination of inorganic phosphate in serum. Determination of calcium in blood serum.

3

13 Pancreas and the thyroid hormones. Adrenal hormones. Sex hormones. Structure, biosynthesis, metabolic role and regulation of their secretion. Reaction of 17-ketosteroids identification in urine. Determination of adrenaline.

3

14 Blood biochemistry. The chemical composition of blood plasma. Plasma proteins, blood enzymes, non-protein nitrogenous substances, mineral

3

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substances. Determination of total protein and albumins concentration in blood serum.

15 The blood transport of gases. Acid-base balance. Clotting: coagulation factors, mechanisms. Anticoagulant and fibrinolytic systems. Hemoglobin determination.

3

16 Test on chapter "Hormones. Blood ". 3 17 Admission to the examination 3

V. Recommended bibliography:

A. compulsory:

1. Nelson D.L., Cox M.M. Lehninger Principles of Biochemistry. Sixth Edition. 2012. 2. Bhagavan N.V., Ha Chung-Eun. Essentials of Medical Biochemistry: With Clinical Cases.

Academic Press; 1st edition, 2011. 3. Campbell P.N. Smith A.D. Biochemistry illustrated. International edition, 2000 4. Murray R.K., Granner D.K., Mayer P.A., Rodwell V.W. Harper’s illustrated

Biochemistry. 26-th international edition, 2003 5. Mardashko O.O., Yasinenko N.Ye. Biochemistry. Texts of lectures. Odessa, 2003. 418 p.

Accesibile în sala de lectura a bibliotecii USMF. 6. Champe Pamela C., Harvey Richard A. Biochemistry. Lippincott’s Illustrated Reviews. 7. Gavriliuc Ludmila. Biochemistry. Lectures for students of Medical Departments. Chisinau

2011. 135 pag. 8. Gavriliuc Ludmila, Tagadiuc Olga. Biochemistry. Guide for laboratory lessons (methodic

material). Chisinau, 2010. 133 pag.

B. Supplementary:

1. Lehninger A.L. Principles of Biochemistry The Johns Hopkins University School of Medicine, Worth Publishers Inc., 2007.

2. Metzler D.E. Biochemistry. The chemical reactions of living cells. Second edition, vol.1-2. Academic Press, 2003

3. Marshall W.J. Clinical Chemistry. 4th edition, Mosby press, UK, London, 2000 4. Stryer L. Biochemistry. Freeman and Company, San-Francisco, USA, 2000. 5. Gavriliuc Ludmila. Biochemistry. Tests for students (Methodic material). Chisinau, 2010.

169 pag. 6. Rivneac Elena. Biochemistry. Lectures for students of stomatological department. http://biochimie.usmf.md/index-4.html

VI. The methods of teaching and learning used:

Biochemistry is a compulsory subject and it is taught in accordance with the standard classical university method: theoretical classes and practical classes. The theoretical classes are held by the teaching staff. At first during practical classes theoretical issues are discussed as it is described in methodological indications; problems and tests based on clinical cases are solved; interactive methods of teaching and learning are applied; then laboratory works are carried out and

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discussion of the importance of determined clinical and biochemical diagnostic indices takes place; the work is finished by filling in the protocols.

VII. Suggestions for individual activity:

From the pedagogical point of view, one of the least effective methods of learning is passive listening to the lectures, even if they are well structured and explained. If you want to learn Biochemistry successfully, you should work actively with the material. For this purpose you can follow a few tips:

Before coming to classes, it is useful to get acquainted with the material to listen to. Don’t take notes of lectures automatically, but go through the information provided by

the professor. If you do not understand the material enough, ask the teacher, colleagues, refer to the

manuals. In preparation for practical classes, tests, exams make notes, diagrams, work in

groups. After you have learned the material, test your knowledge doing tests and solving

problems given at the end of each theme and chapter or in the tests collections. Participate actively in discussions during practical lesson, only when you are able to

formulate your ideas clearly and when you are understood by your professor and group mates you may be sure that you have acquired the material.

Try to find a link between the information obtained in biochemistry and the one obtained in other basic subjects.

Focus upon the medical aspects; apply knowledge gained in biochemistry to clinical disciplines.

VIII. Methods of assessment:

Current assessment

The university course of Biochemistry includes 6 tests: Semester I: Test no. 1: Proteins. Enzymes. Test no. 2: Nucleic acids. Test no. 3: General metabolism. Carbohydrate metabolism. Semester I: Test no. 4: Lipid metabolism. Test no. 5: Simple and combined protein metabolism. Test no. 6: Hormones. Blood.

The test consists of two parts: a written/oral test and a computer test. The written test consists of 6-10 items (depending on the test); students have up to 1 hour and 30 minutes to do it. A computerized test consists of 30 questions of each version (simple choice and multiple choice). Students are given 30 minutes to do it. Each test is assessed by grades from 0 to 10. The test can be done one time, but in case of failure – the second time in the last week of the semester. Annual mark is the average mark of all tests.

Only the students who have an annual mark equal to 5 and over and no more than 1 missed practical lesson are admitted to the final examination in Biochemistry.

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Final assessment: The final exam in Biochemistry consists of a multiple-choice test (option "Test Editor") and oral exam. The multiple-choice test consists of 100 questions, 40 of which are simple choice and 60 - multiple choice. The students have 2 hours to do the test; knowledge is assessed with marks at the range from 0 to10. The oral test is based on question papers containing 4 questions. The students have 30 minutes to prepare a response to the questions. Knowledge is assessed with marks at the range from 0 to10. Questions for the examination (tests and list of questions for the oral test) are approved at the Department meeting and offered to students at least one month before the examination. The final mark consists of 3 components: the annual average mark (coefficient 0.5), oral test (coefficient 0.3) and multiple-choice test (coefficient 0.2).

Marks rounding method :

The sum of notes from current assessments and final examination

Final mark

5 5 5,1-5,5 5,5 5,6-6,0 6 6,1-6,5 6,5 6,6-7,0 7 7,1-7,5 7,5 7,6-8,0 8 8,1-8,5 8,5 8,6-9,0 9 9,1-9,5 9,5 9,6-10 10

Absence at the examination without good reason shall be recorded as "absent" and is equivalent to the grade 0 (zero). The student has the right to two repeated examination.

IX. Language of instruction: Romanian, Russian, English, French.