Biochemistry
Biochemistry is the science concerned the chemical reactions occurring in living cells and organisms.
Biochemistry in the medicine is mainly concerned with balance of biochemical reactions occurring in the
body, both in physiological state as in pathology. The program of teaching biochemistry for medical
students consists of lectures, seminars and laboratory classes. The main object comprises five sections:
Structure and Function of Proteins and Enzymes, Metabolism of Carbohydrates, Lipids of Physiological
Significance, Nucleic Acids and special topics (Nutrition, Digestion, Vitamins, Plasma Proteins,
Immunoglobulins, Haemostasis, Xenobiotics). Total program of teaching in Biochemistry includes: 70 hours
lectures, 68 hours seminars, and 42 hours practical classes. At the end of course students must take the
final examination prepared by Board of Medical Examiners.
Teachers:
1. Prof. dr hab. med. Józef Kędziora
2. Dr Jolanta Czuczejko
3. Dr Karolina Szewczyk-Golec
Contact: Dr Jolanta Czuczejko joczu@wp.pl
Syllabus
I.
Department of Biochemistry
II. Head of the Unit: dr hab. n. med.Beata Augustyńska
III. Faculty of Medicine, Medical Program, year II
IV. Course coordinator – dr Jolanta Czuczejko
V. Form of classes - lectures, practicals, seminars
VI. Form of crediting/assessment - Exam , 16 ECTS points
VII. Number of hours - 60 hours of lectures, 120 hours of practicals and seminars
VIII. Aim of the course:
Acquiring knowledge of the chemical processes occuring in human cells. Studying the chemical constituents
of human cells: structure, properties and function of proteins, saccharydes, lipids, nucleic acids, vitamins
and coenzymes. Studying biochemical aspects of metabolic disorders. Analysis of the compartmentation,
integration and regulation of metabolic pathways. Learning about the metabolism of the main human
organs. Emphasising the relationships between medicine and biochemistry and the role of biochemical
knowledge in medical diagnostics.
IX. Topics:
Biochemistry Lectures
Amino acids, peptides, proteins.
1. Nature of Proteins
- Function: Enzymatic catalysis, transport and storage of small molecules, structural elements
of cytoskeleton, immunity (immune defense system)
2. Amino Acids – fundamental units of proteins
- Composition
- Optical activity
- Amphoteric properties
3. Peptides and polypeptides
- Formation
- Amphoteric properties
4. Purification of proteins
5. Conformation of proteins - primary, secondary, tertiary, quaternary structure
6. Protein Structure – Function Relationship
Oxygen transport proteins
A. Myoglobin and Hemoglobin Structure and Function
B. Hemoglobinopathies (HbS, HbC, HbM, thalassemias)
C. Humoral Immunity - five basic classes of immunoglobulin (structure and function): IgM, IgD,
IgG, IgE, IgA
D. Fibrous proteins - collagen
Enzymes, co-enzymes, vitamins.
1. General characteristics of enzyme
Differences between enzymes and chemical catalysts
Measures of enzyme activity
Enzymes nomenclature
2. Enzyme Kinetics
A.
Quantification of enzyme activity
B.
Quantification of chemical reaction by kinetic order
C
Michaelis – Menten kinetic theory of enzyme action
-significance of the Michaelis constant
-Lineweaver Burk transform
3. Enzyme Inhibition
A.
Competitive
B.
Uncompetitive
C.
Medical relevance of enzyme inhibitor
D.
Regulation of enzymes
4. Enzymes in clinical diagnosis
5. Nomenclature of vitamins - water soluble and fat soluble.
6. Coenzymes:
Nicotinamide-adenine dinukleotide (NAD+)
Nicotinamide – adenine dinukleotide phosphate (NADP+)
Flavin mononucleotide (FMN)
Flavin adenine dinukleotide (FAD)
CoA-SH, ACP
Folic acid
Pyridoxal phosphate (PLP)
Thiamin pyrophosphate (TPP)
Biotin
Cobalamine
Ascorbic acid
7. Cofactors: metal ions of Co, Cu, Mg, Mn, Se, Zn, Fe.
Saccharides, glycolysis pathway, tricarboxylic acid cycle, pentose phosphate pathway.
1. Structures of saccharides
A. Open chain form (asymmetric carbon, isomers, epimers, enantiomers, hemiacetals)
B. Cyclic form (acetals, glycosialles) polysacharydes
2. Carbohydrate derivates
A. Phosphoric acid esters of monosacharides
B. Amino sugars
C. Sugar acids
D. Deoxy sugars
3. Glycoproteins - physiologic functions
A. Glycosaminoglycans (heparin, chondroitin sulfate, dermatan sulfate, heparin sulfate, keratin
sulfate, hyaluronic acid)
4. Glycolysis - anaerobic glycolysis, aerobic glycolisys.
5. The pyruvate dehydrogenase (PDH) enzyme complex, PDH regulation
5. Pentose phosphate pathway
6. Uronic acid pathway (glucuronic acid cycle)
7. Citric acid cycle
Oxidative phosphorylation and biologic oxidation.
Mitochondrial Electron Transport
Localization of electron transport chain
1. The outer membrane
2. The itermembrane space present
3. The inner membrane
4. Organization of the electron transport chain - Complex I, II, III, IV
Lipids
1. Nomenclature of lipids and physiologic significance
2. Phospholipids and glycosphingolipids – structure, function and biosynthesis
3. Fatty acids chain biosynthesis
4. Desaturase & elongase enzyme systems
5. Eicosanoids biosynthesis and their physiologic role
6. Cholesterol biosynthesis (regulation of HMG-CoA reductase activity)
7. Cholesterol as a precursor of steroids (corticosteroids, sex hormones, bile acids, vitamin D)
8. Lipid and cholesterol transport and storage – plasma lipoproteins
9. β-oxidation of saturated, unsaturated and odd number of carbon atoms fatty acids
10. Ketogenesis
11. Lipid peroxidation
12. Interrelationships among carbohydrates and lipids metabolism
*Nucleic acids – structure, function, organization. Molecular genetics.
1. Human genome – definition and structure. Nucleosome and chromatin package. Hetero – and
euchromatin. Structure of nucleic acids. Genetic information and genetic code. Organization of genes,
promoters, microsatellite DNA, pseudogenes.
2. DNA replication – DNA polymerases, start of replication, role of starters in DNA synthesis, Okazaki
fragments. Topology of DNA associated with replication and role of helicases.
3. Transcription of genetic information. RNA synthesis by DNA-dependent RNA polymerase. Types of
RNA and their function. Reverse transcriptase.
4. Translation of genetic information. Components of the translation apparatus. Protein
biosynthesis. Protein maturation and posttranslational modifications. Protein degradation and
turnover.
5. Epigenetics – DNA modifications, DNA methylation. Modulation of genes expression. Epigenetics
and cancer.
6. DNA damage and repair. DNA damage in the way of health & on the way to ageing. Oxidative DNA
damage and repair. Measurement of DNA damage. Biological consequences of oxidative DNA
damage. DNA repair pathways. Mutagenesis. Mutations and polymorphisms in genes encoding DNA
repair enzymes.
7. Mitochondrial genome and its metabolism. Organisation of the human mitochondrial genome.
Maternal
inheritance.
High
mutation
rate.
Mutations
in
mtDNA.
*Nutrition, digestion & absorption.
1. Macro- and micronutrients. Digestion and absorption of proteins, carbohydrates and lipids.
Vitamins. Bile acids metabolism.
2. Energy metabolism. Protein-energy intake. Malnutrition. Obesity. Assessment of nutritional
status.
*Blood, hemostasis & thrombosis.
1. The composition of blood. Blood cells and plasma. Oxygenation of blood.
2. Mechanism of blood coagulation.
* Excretory system.
1. Organs of the excretory system. Removal of carbon dioxide excess by lungs. Skin functions. Breakdown of proteins and urea production in liver. Urea cycle.
2. Kidney function. Hormonal control of water and salt
Detoxification processes – liver functions
1. The metabolism of the liver - amino acids, urea cycle, proteins, carbohydrates, lipids
2. Steps of detoxification – cytochrome P450, conjugation (role of reduced glutathione GSH –
biosynthesis of mercapturic acids)
3. Other role of GSH – peroxidase glutathione (GSH-Px), reductase glutathione (GR), transport of
amino acids
Metabolism of amino acids.
Deamination (role of Glu), transamination, decarboxylation, glucogenic and ketogenic aminoacids,
role of aminoacids on biosynthesis, essential and non-essential amino acids
* Hormones and hormonal regulation.
Hormones and the hormonal cascade system. Major polypeptide hormones and their action. Steroid
hormones. Hormone receptors and intracellular hormone signalling.
* lectures conducted by the Department of Clinical Biochemistry
Biochemistry Practicals
Practical 1 Chemical properties of amino acids
The aim of the class: studies on selected properties of amino acids
Theoretical basis: general structure of amino acids, the names (full names and their three-letter
abbrevations) and structures of protein amino acids, characteristics of the chemical groups
attached to amino acid chain (like carboxylic, amino, imino, sulphydryl, imidazol, guanidine,
hydroxyl groups), amphoteric properties of amino acids, classification of amino acids
according to the chemical properties of their side chains (charged, nonpolar hydrophobic,
uncharged polar; aliphatic, cyclic, aromatic; acidic, basic)
Laboratory tests:
1. Ninhydrin reaction – a characteristic reaction for all amino acids.
2. Characteristic reactions for individual amino acids:
a) xantoprotein reaction – detection of aromatic amino acids
b) Millon reaction – detection of tyrosine
c) Adamkiewicz-Hopkins reaction – detection of tryptophan
d) Pauly reaction – detection of histidine
e) Sakaguchi reaction – detection of arginine
f) cysteine reaction – detection of sulphur amino acids (cysteine, cystine)
Practical 2 Some properties of peptides and proteins
The aim of the class: Some physical and chemical properties of peptides and proteins
Theoretical basis: structure and characteristics of the peptide bond, classification of peptides according to
their structures, the physiologic significance of some peptides in human body, the
characteristics of primary, secondary, tertiary and quaternary structures of proteins,
classification of proteins according to their structures, properties and functions, the
amphoteric properties of proteins (the isoelectric point of proteins)
Laboratory tests:
1. Biuret reaction – detection of peptide bonds.
2. Denaturation of protein:
a) thermal denaturation of protein
b) denaturation of proteins with strong acids
c) denaturation of proteins with strong bases
d) precipitation of proteins with ethanol
e) denaturation of proteins with heavy metal salts
f) denaturation of proteins with alkaloid reagents
3. Amphoteric properties of proteins.
Practical 3 Blood proteins
The aim of the class: Some properties of blood proteins
Theoretical basis: the constituents of the blood, the compositions of blood plasma and blood serum,
characteristics of main blood plasma proteins: albumins, globulins and fibrinogen,
electrophoresis as an important method of plasma (or serum) protein fractionation, the
characteristics of individual protein fractions, the physiologic and pathological
concentrations of blood plasma protein, the diagnostic role of alterations in the amount of
total proteins and in mutual quantitative relationships between individual fractions,
examples of methods for protein concentration determination (biuret protein assay, Lowry
protein assay, Bradford protein assay)
Laboratory tests:
1. Determination of plasma protein concentration by biuret method – preparation of a calibration
curve.
2. Polyacrylamide gel electrophoresis of serum proteins.
3. Fractionation of blood plasma proteins by salting out with ammonium sulphate.
Practical 4 Gel filtration
The aim of the class: molecular filtration for protein separation and desalting of protein
solution
Theoretical basis: The separation of proteins contained in solution by different types of chromatography,
the characteristics of molecular filtration (the types of molecular sieves and their structure,
the principles and applications of gel filtration), different methods used for measurement of
protein molecular weight
Laboratory tests:
1. The separation of mixture of substances with different molecular weight (blue dextran,
hemoglobin, potassium chromate) on chromatographic column filled with Sephadex gel.
SEMINAR / TEST I Amino acids, peptides, proteins
The key problems: The structure of protein amino acids. The classification of amino acids according to both
the polarity and the structural features of their side chains (e. g. polar, nonpolar; aliphatic,
aromatic; sulfur-containing; charged, uncharged; acidic, basic). The amphoteric properties of
amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein
amino acids.
The formation, structure and properties of the peptide bond. Some important peptides in the
human organism (glutathione, peptide hormones). The insulin synthesis.
The classification of proteins according to their structure, properties and functions. The
characteristics of primary, secondary, tertiary and quaternary structures of proteins. The
interactions involved in a protein folding into its final conformation (e. g. the attraction
between positively and negatively charged molecules, the hydrophobic effect, hydrogen
bonding, and van der Waals interactions). Posttranslational modifications of amino acids in
proteins. Structure – function relationships in myoglobin, hemoglobin and immunoglobulins.
The structure and synthesis of collagen. Rybonuclease renaturation as an example of the
importance of primary protein structure. The prions as an example of medical importance of
proper protein folding.
Practical 5 The isolation of enzymes from biological materials
The aim of the class: the isolation and purification of yeast saccharase
Theoretical basis: the structure of enzymes, classification of enzymes, the enzymes names, the methods
of isolation and purification of enzymes from biological materials.
Laboratory tests:
1. The isolation and purification of saccharase (sucrase) from yeast.
2. Samogyi-Nelson method – calibration curve preparation.
Practical 6 The kinetics of the enzymatic reaction
The aim of the class: the determination of the initial velocity and Michaelis constant in
reaction catalysed by saccharase
Theoretical basis: the enzyme-catalyzed reaction, the definitions of initial velocity, maximal velocity and
Michaelis constant, the Michaelis-Menten equation, the standard units of enzymatic activity
(katal, international unit), the influence of some factors on the enzyme activity (e. g.
temperature, pH, the concentration of substrate and enzyme, competitive and
noncompetitive inhibitors).
Laboratory tests:
1. The determination of the initial velocity in reaction catalysed by saccharase.
2. The determination of the Michaelis constant in reaction catalysed by saccharase.
Practical 7 The vitamin C concentration in biological materials
The aim of the class: the determination of the ascorbic acid concentration in different
biological materials
Theoretical basis: classification, structure and functions of water-soluble vitamins, classification, structure
and functions of coenzymes.
Laboratory tests:
1. The determination of the ascorbic acid concentration by Folin method in the blood serum and
some other biological materials (e. g. vegetable and fruit juices)
SEMINAR / TEST II Enzymes and coenzymes
The key problems: The definitions: enzyme, coenzyme, cofactor. The isoenzymes of the
diagnostic importance (lactate dehydrogenase (LDH), creatine phosphokinase (CPK)). The
structure of the active site and models for substrate binding. The specificity of enzymes to the
substrates and the catalysed reaction.
The catalytic mechanisms of the enzymatic reactions. The influence of physical and chemical
factors on the enzyme activity (temperature, pH, the enzyme concentration, the substrate
concentration, the product concentration). The kinetics of enzymatic reaction: the initial and
maximal velocities, Michaelis constant, the Michaelis-Menten equation, the Lineweaver-Burk
plot.
Regulation of enzyme activity: allosteric enzymes (allosteric activators and inhibitors, the
examples of allosteric enzymes, the sequential and concerted models for an allosteric enzyme,
the kinetics of allosteric enzyme reaction), feedback regulation and its examples in the human
organism, covalent modification of enzymes (phosphorylation), proteolytic cleavage
(proenzymes, zymogens, autocatalysis), reversible inhibition (competitive and noncompetitive
inhibitors, the mechanism of the inhibition, the kinetics of competitive and noncompetitive
inhibitions, medical significance of inhibition: acetylsalicylic acid, Fluorouracil, methotrexate,
penicillin, allopurinol).
The standard units of enzymatic activity (katal, the international unit, the specific activity of an
enzyme). The classes of enzymes (oxidoreductases, transferases, hydrolases, lyases,
isomerases, ligases).
Coenzymes: their structrures and functions in the reactions. Water-soluble and fat-soluble
vitamins: their structures and functions. The trace elements: some enzymatic reactions that
involve the iron, cobalt, zinc, or copper ions.
Practical 8 Some properties of monosaccharides
The aim of the class: some chemical properties of monosaccharides
Theoretical basis: nomenclature of monosaccharides and their isomerism, the structure of
monosaccharides (Fischer projection and cyclic structure), the chemical properties of
monosaccharides, the examples of biologically important monosaccharides.
Laboratory tests:
1. Fuchsine reaction – characteristic reaction for monosacharides in neutral solution
2. Characteristic reactions for monosaccharides in basic solution – the reducing properties of
saccharides:
a) Fehling reaction
b) Benedict reaction
c) Nylander reaction
d) picric acid reaction
3. Characteristic reactions for monosaccharides in concentrated strong acids solutions
a) Molisch reaction – detection of every monosaccharide
b) Seliwanow reaction – detection of ketoses
c) phloroglucinol reaction – detection of pentoses
4. Phenylhydrazine reaction – the formation of osazones.
5. Ethanol fermentation.
Practical 9 Some properties of di- and polysaccharides
The aim of the class: some properties of biologically important disaccharides and
polysaccharides
Theoretical basis: nomenclature of disaccharides and polysaccharides, their structure and properties, the
examples of biologically important di- and polysaccharides, physiologically significant
saccharide derivatives (e. g. heparine) and glycoproteins
Laboratory tests:
1. Molisch reaction – detection of every di- or polysaccharide
2. Seliwanow reaction – detection of ketose presence in saccharose molecule.
3. The reductive test for some dissacharides:
a) Fehling reaction for lactose, maltose and sucrose
b) picric reaction for lactose, maltose and sucrose
4. Barfoed reaction – the characteristic reaction for reducing disaccharides.
5. Iodine test – the detection of starch.
Practical 10 Saccharides of physiological importance
The aim of the class: preparation of glucose tolerance curve, the estimation of sialic acids
concentration in the blood serum
Theoretical basis: the glucose concentration in the blood, the maintenance of blood glucose levels,
regulation of blood glucose level by hormones, the glucose levels in diabetes mellitus,
glucose tolerance test in healthy persons and diabetes mellitus patients, the physiologic role
of sialic acid
Laboratory tests:
1. Determination of the blood glucose levels in the blood samples obtained during oral glucose
tolerance test conducted on the healthy person – an enzymatic reaction with glucose oxidase.
2. Determination of the blood glucose levels in the blood samples obtained during oral glucose
tolerance test conducted on the diabetes mellitus patient – an enzymatic reaction with glucose
oxidase.
3. The drawing of two glucose tolerance curves – for healthy and diabetes mellitus person.
4. Winzler method – the determination of blood sialic acids concentration.
SEMINAR / TEST III Saccharides
The key problems: Classification of monosaccharides by both the number of contained carbon
atoms (e. g. triose, tetrose etc.) and the type of contained carbonyl group (aldose, ketose), and
their isomerism. Common disaccharides. The structure of important polysaccharides (starch
and glycogen). Physiologically significant saccharide derivatives (especially amino sugars).
Synthesis and functions of sialic acids.
Generation of ATP from glucose: glycolysis (reactions of glycolytic pathway, substrate-level
phosphorylation, regulation of glycolysis). Synthesis of 2,3-bis-phosphoglycerate in a “side
reaction” of the glycolytic pathway. Anaerobic glycolysis – (lactate fermentation, tissues
dependent on anaerobic glycolysis, fate of lactate – Cori cycle, lactic acidemia, ethanol
fermentation). Fructose and galactose metabolisms. Synthesis and degradation of lactose.
Formation and degradation of glycogen. Disorders of metabolisms of fructose, galactose and
glycogen. The pentose phosphate pathway. The directions of the pentose phosphate pathway
reactions due to the cellular needs. Hemolysis caused by reactive oxygen species in the
conditions of glucose-6-phosphate dehydrogenase deficiency. Gluconeogenesis. The
maintenance of blood glucose levels by hormones (regulation of glycolysis and
gluconeogenesis, as well as formation and degradation of glycogen by insulin, glucagon and
noradrenaline).
Practical 11 The electron-transport chain.
The aim of the class: studies on selected enzymes of the electron-transport chain and some
enzymes of antioxidative properties.
Theoretical basis: the oxidative-reduction components of the electron-transport chain and their
structures, the electron-transport chain as a major source of the free radicals in the cell, the
antioxidative defense in the human organism, the enzymatic and non-enzymatic
components of the antioxidative defense
Laboratory tests:
1. Demonstration of the cytochrome c oxidase activity in potato juice.
2. Demonstration of the catalase activity in the hemolysate.
3. Determination of glutathione peroxidase activity in the blood plasma.
4. Determination of ceruloplasmin oxidase activity in the blood serum.
SEMINAR / TEST IV # Oxidative phosphorylation and tricarboxylic acid cycle
The key problems: Oxidative fates of pyruvate – oxidation of pyruvate to acetyl CoA by pyruvate
dehydrogenase. The tricarboxylic acid (TCA) cycle (reaction, enzymes, coenzymes, regulation
of this cycle). The energetics of the TCA cycle. Cellular bioenergetics: the compounds containing
high-energy bonds (ATP and the others nucleoside triphosphates, creatine phosphate, 1,3-bisphosphoglycerate, acetyl CoA). Oxidative fates of NADH, produced from glycolysis (glycerol 3phosphate shuttle and malate-aspartate shuttle). Transfer of compounds through the inner and
outer mitochondrial membranes. The generation of ATP from glucose (complete aerobic
oxidation of glucose, anaerobic glycolysis).
Oxidative phosphorylation. The electron-transport chain. Chemiosmotic model of ATP
synthesis. The structure of protein complexes of the electron-transport chain. Respiratory chain
inhibitors, chemical uncouplers of oxidative phosphorylation. The generation of reactive
oxygen species (ROS) in the cell (the mitochondrial electron-transport chain and other sources).
ROS-mediated cellular injury. Formation of free radicals during phagocytosis and inflammation.
Cellular defences against oxygen toxicity.
Practical 12 * Some properties of lipids.
The aim of the class: some chemical properties of lipids, lipids of physiologic significance.
Theoretical basis: categories of lipids, the nomenclature of both saturated and unsaturated fatty acids,
examples of biologically important fatty acids, the structure of glycerolipids, the structure
of sphingolipids, the role of some important lipids in the human organism, the lipid
peroxidation, the structure of cholesterol, the physiological blood concentrations of both
cholesterol and triacylglycerols, the diagnostic significance of cholesterol, triacylglycerols
and lipoproteins levels in the blood.
Laboratory tests:
1.
2.
3.
4.
5.
6.
7.
Acrolein test – detection of glycerol.
Detection of unsaturated fatty acids.
Saponification reaction of triglicerydes.
Emulsifying action of both the soap and the bile acids.
Kreis test – detection of aldehyde products of lipid peroxidation
Determination of the cholesterol concentration in the blood serum – an enzymatic method.
Determination of the triglycerides concentration in the blood serum – an enzymatic method.
SEMINAR / TEST V * Lipids
The key problems: Saturated and unsaturated fatty acids, their nomenclature and structure. Acylglycerols,
phosphoacylglycerols, sphingolipids, steroids, eicosanoids. Structure and functions of
cholesterol. The cholesterol derivatives (vitamin D, steroid hormones, the bile acids) and their
role in the organism. Transport of cholesterol by the blood lipoproteins. The cholesterol
synthesis and its regulation. Medical significance of elevated cholesterol blood levels.
Dyslipoproteinemias.
Activation of long-chain fatty acids and their transport into mitochondria. β-oxidation of longchain fatty acids, oxidation of unsaturated fatty acids. Energy yield of β-oxidation. Odd-chainlenght fatty acids oxidation. Conversion of propionyl CoA to succinyl CoA. Metabolism of ketone
bodies.
The acetyl CoA transport from mitochondria into cytosol (role of citrate). The sources of NADPH
for fatty acid synthesis. Fatty acid synthesis. Elongation of fatty acids. Desaturation of fatty
acids. Conversion of linoleic acid to arachidonic acid. The synthesis of eicosanoids and their
physiologic significance. Synthesis of triacylglycerols. Synthesis of glycerophospholipids and
sphingolipids. Integration of carbohydrate and lipid metabolism.
Practical 13 * Nucleic acids extraction from yeast
The aim of the class: isolation of nucleic acids from yeast.
Theoretical basis: the structure and nomenclature of nucletides, the structure of nucleic acids: DNA and
RNA, the conditions of nucleic acid separation from yeast
Laboratory tests:
1. The separation and purification of nucleic acids from yeast.
2. Determination of RNA concentration in the sample – orcin method.
3. Determination of DNA concentration in the sample – Feulgen method.
Practical 14 * Some properties of nucleic acids
The aim of the class: studies on the composition and some properties of nucleic acids
Theoretical basis: characteristics of nucleic acids, their structure, metabolism and functions in the human
body
Laboratory tests:
1. The solubility of nucleic acids.
2. Nucleic acid sugar compounds detection:
a) orcin test: detection of ribose
b) diphenylamine test – detection of deoxyribose
3. Nucleic acids hydrolysis
a) detection of purines – by precipitation with Ag+ ions
b) detection of sugar – phloroglucinol reaction
c) detection of phosphate – by reaction with molybdic reagent
4. Absorbsion spectrum of nucleic acids.
SEMINAR / TEST VI * Nucleic acids and their metabolism
The key problems: The nomenclature and structure of purine and pirymidine bases. The structure of
nucleotides. Purine and pyrimidine synthesis and its regulation. The purine nucleotide salvage
pathway. The formation of deoxyribonucleotides. Degradation of purine and pyrimidine bases.
Lesch-Nyhan syndrome, sever combined immunodeficiency disease (SCID), hyperuricemia.
The structure of the nucleic acids. Synthesis of DNA. Transcription: synthesis of RNA. Translation:
synthesis of proteins. Regulation of gene expression. Use of recombinant DNA techniques in
medicine. The molecular biology of cancer.
Practical 15 Enzymes of digestive tract
The aim of the class: studies on some properties of digestive juices
Theoretical basis: the composition of digestive juices, the physical and chemical properties of digestive
juices, the role of the components of digestive juices in the digestion process. The
characteristics of digestive enzymes.
Laboratory tests:
1.
2.
3.
4.
5.
6.
7.
Demonstration of amylase presence in pancreatic juice.
Demonstration of proteolytic enzymes presence in pancreatic juice.
Demonstration of lipase presence in pancreatic juice.
Determination of lipase activity in pancreatic juice.
Detection of some inorganic ions in the saliva.
Measurement of gastric content acidity (free, related and total acidity).
Demonstration of bile acids presence in the bile
a) Hay test
b) Pettenkofer test
Practical 16 * The constituents of the blood
The aim of the class: studies on some properties of some constituents of the blood
Theoretical basis: the constituents of both cellular and noncellular fractions of the blood, major functions
of the blood, the structure of hemoglobin and its role in the respiration (oxygen and carbon
dioxide transport), the oxygen-binding curve of hemoglobin, the allosteric effectors for
oxygen binding to hemoglobin (pH, carbon dioxide, 2,3-bisphosphoglycerate), the Bohr
effect, some examples of hemoglobinopathies (hemoglobin M, hemoglobin S, thalassemias),
the role of the blood proteins in the maintenance of homeostasis, the functions of inorganic
compounds in the blood
Laboratory tests:
1.
2.
3.
4.
5.
6.
7.
8.
Benzidine reaction – detection of the blood.
Distinction of oxyhemoglobin and carboxyhemoglobin.
Preparation of hematin in acidic and basic conditions.
Demonstration of iron presence in hemoglobine molecule.
Determination of hemoglobin concentration – the cyanmethemoglobin method.
Detection of lipids in the blood plasma.
Van der Bergh reaction - detection of bilirubin in the blood serum.
Detection of bilirubin in the bile.
Practical 17 The blood serum enzymes used in clinical diagnosis
The aim of the class: the analysis of some serum enzymes activities and its role in the
diagnosis of disease processes
Theoretical basis: classification of blood diagnostic enzymes, the major enzymes used in clinical diagnosis,
the role of diagnostic enzymology in diagnosis of myocardial infarction and some liver
diseases, absorption spectra of NAD+ and NADH, the usage of these spectra for the assays
of dehydrogenases activities, the coupled enzyme assays
Laboratory tests:
1.
2.
3.
4.
5.
Determination of alanine aminotransferase activity in the blood serum.
Determination of aspartate aminotransferase activity in the blood serum.
Determination of lactate dehydrogenase activity in the blood serum.
Determination of alkaline phosphatase activity in the blood serum.
Determination of -amylase activity in the blood serum.
SEMINAR / TEST VII The blood. Nutrition, digestion, and absorption
The key problems: The composition of digestive juices, the enzymes of digestive tract. Digestion and
absorption of carbohydrates, lipids, proteins, vitamins and minerals. The role of hydrochloric
acid and the bile salts in digestion processes. The production of hydrochloric acid by parietal cell
of the stomach. The biosynthesis and degradation of bile salts. The enterohepatic bile salts
circulation.
Synthesis of heme and regulation of this process. Catabolism of heme. The fates of bilirubin:
transport to the liver, conjugation with glukuronic acid, secretion into bile, reduction to
urobilinogen. The enterohepatic urobilinogen cycle. Hyperbilirubinemias, different causes of
jaundice (hemolytic anemia, hepatitis, obstructive jaundice), the laboratory tests important in
helping to distinguish between prehepatic, hepatic and posthepatic causes of jaundice.
The major functions of the blood, the constituents of the blood. The organic and inorganic
constituents of the blood plasma. The characteristics and functions of plasma proteins. Structure
and functions of red blood cells. Metabolism of the red cell. Reaction of importance in relation
to oxidative stress in blood cells. System for reducing heme Fe3+ back to the Fe2+ state in the red
blood cell. Physiologic roles of hemoglobin and mioglobin, the oxygen dissociation curves for
myoglobin and hemoglobin. The mechanism of binding O2 to myoglobin and hemoglobin. The
cooperative interactions infuencing the binding O2 to hemoglobing, the changes of oxygenbinding curve of hemoglobin (effect of temperature, pH, carbon dioxide concentration, 2,3-bisphosphoglycerate concentration). The Bohr effect. The carbon dioxide transport in the blood.
Binding CO to hemoglobin. Changes of the subunit composition of hemoglobin tetramers during
development (embryonic, fetal and adult subunits). Abnormal hemoglobines. Anemia. The
classification of the causes of anemia.
Practical 18 Urine physiologic parameters
The aim of the class: the analysis of some substances extreted by the kidney from the body
via the urine during physiologic conditions
Theoretical basis: the functions of the kidney (excretion of waste products produced by metabolism, acidbase homeostasis, osmolality regulation, the blood pressure regulation, hormone
secretion), the production of urine, characteristics and composition of the urine, glomerular
filtration rate (GFR), creatinine clearance as a creatinine-based approximation of GFR
Laboratory tests:
1. Determination of urea concentration in the urine – Yatzidis method with Ehrlich’s reagent.
2. Harrison’s test – detection of bilirubin in the urine.
3. Detection of creatinine in the urine:
a) Weyl’s test
b) Jaffe method
4. Determination of creatinine concentration in the urine – Jaffe method.
5. Deniges test – detection of indican in the urine.
6. Ehrlich’s aldehyde test – detection of urobilinogen in the urine.
7. Determination of α-amylase activity in the urine – Winslow’s method.
8. Determination of uric acid concentration in the urine and in the blood serum – enzymatic method.
Practical 19 Diagnostic chemical markers in human urine
The aim of the class: the analysis of some substances excreted by the kidney from the body
via the urine during pathologic conditions
Theoretical basis: the role of the urine analysis in the medical examination, the substances excreted by the
kidney via the urine in selected disease processes, diagnostic urine stripes as a rapid method
of urine analysis
Laboratory tests:
1.
2.
3.
4.
5.
6.
Benzidine method – detection of the blood (or hemoglobin) presence in the urine.
Coagulation urine protein test – detection of the protein presence in the urine.
Benedict’s test – detection of glucose presence in the urine.
Rothera’s test – detection of ketone bodies presence in the urine.
Hay test – detection of the bile salts presence in the urine.
The urine examination using the diagnostic urine stripes.
SEMINAR / TEST VIII Metabolism of amino acids.
The key problems: Fate of amino acid nitrogen. Enzymes important in the process of interconverting amino
acids and in removing nitrogen (dehydratases, transaminases, glutamate dehydrogenase,
glutaminase, deaminases). The convertion of amino acid nitrogen to urea – the urea cycle.
Degradation of amino acid: fate of amino acid carbon skeletons. Glucogenic and ketogenic
amino acids. The role of pyridoxal phosphate, tetrahydrofolate and tetrahydrobiopterin
coenzymes in amino acid metabolism. Some disorders of amino acid catabolism: alkaptonuria,
phenylketonuria, maple syrup urine disease.
The biosyntheses of biologically important compounds from amino acids (sphingosine, choline,
taurine, creatine, catecholamines, hippuric acid, nitric oxide, glutathione,
glycerophospholipids, purines, pirymidines, carnosine, anserine, bile salts, hem, serotonin,
melatonin, nicotinin acid, coenzyme A). Biosynthetic decarboxylations of amino acids to amines
– the biogenic amines and their biological functions.
The one-carbon carriers in the body: tetrahydrofolate (FH4), vitamin B12, S-adenosylmethionine
(SAM). Sources and recipients of one-carbon FH4 pool.The methyl-trap hypothesis. The role of
SAM in the biosynthesis of the compounds of biological importance (creatine,
phosphatidylcholine, adrenaline, melatonin, methylated nucleotides, methylated DNA).
Essential and nonessential amino acids. The synthesis of nonessential amino acids in the human
organism.
SEMINAR IX Integrative seminar 1 – Metabolism of tissues and organs.
The key problems: Carbohydrate, lipid and amino acid metabolism of liver, brain, skeletal muscle, cardiac
muscle cells, and kidney. The sources of ATP for skeletal muscle cells (e. g. creatine phosphate,
purine nucleotide cycle). Major functions of the kidney (excretion of waste products produced
by metabolism, acid-base homeostasis, osmolality regulation, the blood pressure regulation,
hormone secretion, γ-glutamyl cycle). The substances excreted via the urine in normal and
pathologic conditions. The metabolism of liver (detoxification of drugs and metabolites,
glutathione S-transferases, metabolism of ethanol). The functions of glutathione in the
organism.
Intertissue relationships in the metabolism of carbohydrates, lipids and amino acids.
SEMINAR X * Integrative seminar 2 – Metabolism regulation – actions of hormones.
The key problems: Classification of hormones according to their structure, a type of hormone receptor,
and a second messenger. The synthesis of thyroid hormones. The hormones involved in the
glucose maintenance in the blood. The major hormones influencing nutrient metabolism and
their actions on muscle, liver, and adipose tissue. The changes in the fuel metabolism during
fasting state and starvation. The metabolism of carbohydrates, lipids, and amino acids in the
diabetes mellitus type I and type II.
Practical 20 End-of-year practical
* practicals and seminars conducted by the Department of Clinical Biochemistry
# practicals and seminars partially conducted by the Department of Clinical Biochemistry
X. Self-study topics XI. Basic booklist
1. Murray RK, Bender DA et al. "Harper`s Illustrated Biochemistry" 28th edition
2. Lieberman M, Marks AD "Marks` Basic Medical Biochemistry a Clinical Approach". 3rd edition
3. Marks DB "Biochemistry" 3rd edition
XII. Detailed list of required practical skills and confirmation of completing
Assessment record
Student name:
Year of the study, group number:
Academic year:
List of required practical skills
Date
of signature
assessment tutor
Gaining
knowledge
of
molecular,
biochemical
and
physiological mechanisms occuring in human organism
Analysis of laboratory results
Rules and regulations
of comments
The main objective of the course is to provide an understanding of biochemical processes and to
gain relevant basic laboratory skills according to the educational requirement defined in the program of
teaching biochemistry for medical students.
The program (180 hrs) consists of lectures (60 hrs), tests and seminars (40 hrs), and practical
classes (80 hrs) and a closing test. All classes are compulsory. Students should check the schedule carefully
and be on time. If students cannot attend class they must have sick note and arrange for an alternative
date to carry out the lab/seminar.
The performance during each laboratory class will be evaluated by the quality of theoretical
preparation, laboratory skills and written protocol from the experiments.
Seminars: Students must be prepared to give a short presentations of topics which will be given
to them by the teacher after each part of material.
Tests: One-choice tests (30 questions, graded 1 point for a correct answer) will be held at the end
of the each part of the material.
Final examination: Students who has earned credit must take the final examination (50 questions,
one-choice questions test, graded 1 point for a correct answer).
The final examination and partial tests can be retaken according to the schedule and the
percentage of the points according to the following system:
60-67 % - satisfactory
68-75 % - fairly good
76 - 83 % - good
84 - 90% - better than good
90 - 100 % - very good
Histology and cytophysiology
The coursework of Histology and Cytophysiology includes 40 hours of lectures and 80 hours of labs
conducted during two semesters. It is ended with the Final Exam in second semester. Final Exam consist
of practical recognizing of slides and final test. Practical recognizing of slides will be conducted during the
last labs (the presence is obligatory). The final test will be timed in the schedule of session. The labs and
lectures are prepared in a week cycle.
Teachers:
1.
prof. dr hab. Alina Grzanka
2.
3.
mgr Maciej Gagat
mgr Magdalena Izdebska
Contact: mgr Maciej Gagat mgagat@cm.umk.pl
Syllabus
I.
Department of Histology and Embryology
II.
Head of the unit: Assoc. Prof. Alina Grzanka, Ph.D.
III.
Faculty of Medicine, Medical Program, 2nd year, 3rd semester (winter)
IV.
Course coordinator: Assoc. Prof. Alina Grzanka, Ph.D.
V.
Form of classes: lectures, tutorials
VI.
Form of crediting: Exam, 6 ECTS points
VII.
Number of hours: 20 (lectures), 40 (tutorials)
VIII.
Aim of the course:
Lectures
The aim is to present the information on structure and function of cells and tissues. The lectures
also provide students with a brief introduction into the molecular biology of the cell.
Tutorials

continuation of some problems introduced in lectures

acquaintance with scientific research conducted at the Department of Histology and Embryology

work with the cytological and histological preparations

estimation of cellular structures at the electron microscopy level
IX.
Topics of lectures / tutorials:
Lectures:
1. Skin – structure and functions: subcutaneous tissue, dermis, epidermis, skin vascularization and
innervation.
2. Digestive system – structure and functions (part 1): oral cavity, oesophagus.
3. Digestive system – structure and functions (part 2): stomach, small intestine.
4. Glands of digestive system.
5. Respiratory system – structure and functions: nasal cavity, larynx, trachea. Composition and
formation of surfactant.
6. Endocrine system (part 1). Endocrine glands: hypophysis (adenohypophysis, neurohypophysis),
thyroid, parathyroid, thymus, unicellular endocrine glands.
7. Endocrine system (part 2). Endocrine glands: adrenal gland, pituitary gland, pineal gland.
8. Urinary system – structure and functions: kidney, nephron, renal pelvis, glomeruli,
juxtaglomerular apparatus.
9. Central nervous system: structure of the spinal cord and cerebral cortex, cerebral meninges.
10. Peripheral nervous system: peripheral nerves, autonomic nervous system.
11. Photoreceptor and audioreceptor systems.
12. Circulatory system: structure of heart, conduction system of heart.
13. Lymphatic system: lymphatic nodules, tonsils, lymphatic tissues, mucosa-associated lymphatic
tissue (MALT).
14. Female reproductive system – structure and functions: ovary, oviduct, vagina.
15. Male reproductive system – structure and functions: testis, epididymis, deferent duct.
Tutorials:
1. Skin and accessory structures.
2. Digestive system (part 1).
3. Digestive system (part 2).
4. Glands of digestive system.
5. Respiratory system.
6. Endocrine system (part 1).
7. Endocrine system (part 2).
8. Urinary system.
9. Central nervous system.
10. Peripheral nervous system.
11. Sense organs.
12. Circulatory system.
13. Lymphatic system.
14. Female reproductive system.
15. Male reproductive system.
16. Final test; practical exam.
X.
Self-study topics:
----------XI.
Booklist:
Basic:
Junqueira LC, Carneiro J. Basic Histology: Text and Atlas. McGraw-Hill 2005; Eleventh Edition.
Mescher AL. Junqueira's Basic Histology: Text and Atlas. McGraw-Hill, 2009; Twelve Edition.
Additional:
Ross MH, Kaye GI, Pawlina W. Histology. A text and atlas with cell and molecular biology. Williams
&Wilkins 2003; Fourth Edition.
Sobotta/Hammersen. Histology, A Colour Atlas of Cytology, Histology and Microscopic Anatomy.
Urban & Schwarzenberg 1996.
XII.
Detailed list of required practical skills and confirmation of completing:
Name:
Year of study:
Group:
Academic year:
Date
Confirmation
of Notes
completing
Recognizing of normal human organs
on slides stained with different
histological techniques.
Rules and regulations
Obligatory textbook:
Junqueira LC, Carneiro J. Basic Histology: Text and Atlas. McGraw-Hill 2005; Eleventh Edition.
Mescher AL. Junqueira's Basic Histology: Text and Atlas. McGraw-Hill, 2009; Twelve Edition.
Additional textbooks:
Ross MH, Kaye GI, Pawlina W. Histology. A text and atlas with cell and molecular biology. Williams &Wilkins
2003; Fourth Edition.
Sobotta/Hammersen. Histology, A Colour Atlas of Cytology, Histology and Microscopic Anatomy. Urban &
Schwarzenberg 1996.
Requirements
1.
Students are obliged to prepare the part of material for each lab from the last topic.
2.
The labs are obligatory. In the case of the illness a sick leave has to be delivered. Other absences due
to important reason must be documented.
3.
Two unjustified and undocumented absences make it impossible to pass the semester and take the
Final test.
4.
Each Student is obliged to come for the labs on time. Delayed Students can enter the class only if the
time of delaying does not exceed 15 minutes from the moment a lab has been started.
5.
In the case of absence or delay (more than 15 minutes) the Student is obliged to pass the material
which was covered during the labs within 2 weeks.
6.
In the case of fail the entrance test the Student is obligated retake the test within 2 weeks.
7.
If Student does not pass the failed material during fixed time, he or she is obligated to retake the test
within the last 2 weeks of each semester.
8.
Students are obliged to bring pencils, color pencils and worksheets.
9.
Students are obligated to complete worksheets during each lab.
10. Students are obligated to clean up after themselves.
11. Any accidents, injuries and other emergencies must be immediately reported to the practice leader.
12. Eating, drinking, and using mobile phones during the labs are prohibited.
Point system
1.
Each lab (except the first labs in the first semester and second semester) will be entered with 10questioned test. For each correct answer Student will receive two points. Only students who will gain
at least 6 points pass the test.
2.
The labs in the first semester will be passed if all entrance tests and worksheets are passed.
3.
Practical recognizing of slides will be concerned with recognizing of histological preparations and
electronograms.
4.
Students can take the Final Exam on condition that they pass labs and the practical.
5.
Students are eligible to be exempt from Final Exam if all entrance tests and worksheets are passed
the first time (only if they hold a mark above 70% form each entrance test).
Final Exam
1.
The Final Exam consists of multiple choice questions (only one answer correct).
2.
Students who failed the Final Exam are obliged to retake the test.
3.
The final scores of the Final Exam are not changeable.
4.
The scores of the failed Final Exam and the retake will be confirmed by a signature in the Student
Book as two separated scores but not as the mean of these two.
5.
An excuse for absence should be submitted to the examiner the next day, or in justified
circumstances, within three days after the Final Exam.
6.
The Final Exam will be assessed according to given marks:
(Fail) – less than 60%
(3) – 60%
(3,5) – 65 %
(4) – 70%
(4,5) – 80 %
(5) – 90%
Embryology
The aim is to present the development of the human embryo from the fertilization of the ovum to the
fetus stage. This course helps student to understand the development, final form and relationships of
tissues and organs. Moreover, the course will provide students with the knowledge on the critical stages
of normal development and the effects of common teratogens, genetic mutations and environmental
hazards on it.
Teachers:
prof. dr hab. Alina Grzanka
Contact: kizhistol@cm.umk.pl
Syllabus
I.
Department of Histology and Embryology
II.
Head of the unit: Assoc. Prof. Alina Grzanka, Ph.D.
III.
Faculty of Medicine, Medical Program, 2nd year, 3rd semester (winter)
IV.
Course coordinator: Assoc. Prof. Alina Grzanka, Ph.D.
V.
Form of classes: lectures
VI.
Form of crediting/Assessment: Credit only, 2 ECTS points
VII.
Number of hours: 15 (lectures)
VIII.
Aim of the course:
Lectures
The aim is to present the development of the human embryo from the fertilization of the ovum to the
fetus stage. This course helps student to understand the development, final form and relationships of
tissues and organs. Moreover, the course will provide students with the knowledge on the critical stages
of normal development and the effects of common teratogens, genetic mutations and environmental
hazards on it.
IX.
Topics of lectures:
Lectures:
1.
Introduction to embryology. Historical perspectives.
2.
Gametogenesis and oogenesis, spermatogenesis. Abnormal gametes.
3.
Transport of gametes and fertilization.
4.
Cleavage and implantation. Ectopic pregnancy.
5.
Gastrulation.
6.
Basic embryonic body plan. Development of ectodermal, mesodermal and endodermal germ
layers.
7.
Fetal membranes – structure and significance.
8.
Umbilical cord – structure and function. Development of placenta.
9.
The mature placenta. Placental circulation and physiology.
10.
Development of the cardiovascular and digestive systems. Clinical correlations.
11.
Development of the respiratory, urogenital and nervous systems. Clinical correlations.
12.
Development of the endocrine system and body cavities. Clinical correlations.
13.
Development of the integumentary system. Clinical correlations.
14.
Multiple pregnancies. In vitro fertilization and cloning.
15.
Human birth defects. Types of abnormalities.
X.
Self-study topics:
----------XI.
Booklist:
Basic:
Carlson BM. Human embryology and developmental biology. Mosby 2004; Third Edition.
Additional:
Moore KL, Persaud TVN. The developing human. Clinically oriented embryology. Saunders 2003; Seventh
Edition.
XII.
Detailed list of required practical skills and confirmation of completing:
-----------
Rules and regulations
Credit form of coursework:
13. The coursework consist of lectures from embryology.
14. The coursework is ended with the Final Test.
Credit form of tutorials:
No concern
Credit form of colloquium:
No concern
Form of exam:
The coursework will be passed according to scores of the Final Test.
Rules of make-up the unjustified classes missed:
No concern
Deadline to deliver elaboration, raports or different forms required in the unit:
No concern
General and detailed Management of Health and Safety at Work Regulations required during teaching
programme in the unit:
Student are obligated to comply with general Management of Health and Safety at Work Regulations
Physiology with elements of clinical physiology
Physiology with elements of clinical physiology course is designed to provide students with understanding
of physiological mechanisms of human body functions, at the cellular and organ level as well as integrative
functioning of the human body. Course content will include neural and hormonal homeostatic control
mechanisms, study of the musculoskeletal, circulatory, respiratory, digestive, urinary, reproductive,
endocrine organ systems and the physiology of blood, kidney, principles of acid- base balance and
metabolism. Principles of exercise physiology will be emphasized throughout the course.
Teachers:
1.
2.
3.
4.
5.
6.
7.
8.
9.
Prof. dr hab. Małgorzata Tafil-Klawe
dr hab. Dariusz Soszyński, prof. UMK
dr Piotr Złomańczuk
dr Katarzyna Dmitruk
dr Wieńczysława Adamczyk
dr Daria Pracka
dr Tadeusz Pracki
dr Blanka Milczarek
mgr Małgorzata Gałązka
Contact: b.milczarek@cm.umk.pl, malgorzata.galazka@cm.umk.pl
Syllabus
I.
Department of Physiology
II.
Head of the Unit: prof. db. Małgorzata Tafil-Klawe
III.
Faculty of Medicine, Medical Program, II year
IV.
Course coordinator: prof. dr hab. Małgorzata Tafil-Klawe
V.
Form of the classes: lecture, classes
VI.
Assessment criteria: exam, ECTS 16 pts
VII.
Number of hours: 60 hours of classes, 120 hours of classes
VIII.
Course aims:
Physiology with elements of clinical physiology course is designed to provide students with
understanding of physiological mechanisms of human body functions, at the cellular and organ level
as well as integrative functioning of the human body. Course content will include neural and hormonal
homeostatic control mechanisms, study of the musculoskeletal, circulatory, respiratory, digestive,
urinary, reproductive, endocrine organ systems and the physiology of blood, kidney, principles of
acid- base balance and metabolism. Principles of exercise physiology will be emphasized throughout
the course.
IX.
Lecture topics:
1. The fundamentals of neurophysiology: neuron structure, types of neurons.
2. Synaptic conductivity, ionic currents and channels, ion- and metabotropic receptors and
neurotansmitters.
3. Higher functions of central nervous system.
4. Biological clocks -their formal properties and neurophysiological basis.
5. Normal anatomy of the heart. Phenomenon of electrical, mechanical and acoustic work-related
myocardial infarction.
6. Cardiac hemodynamics.
7. Mechanisms regulating cardiac function.
8. Normal anatomy of the circulatory system. Vasculature.
9. Cardiovascular regulation. The mechanisms regulating blood pressure.
10. Lung structure and function - lung ventilation.
11. The exchange of gases in the lungs. Transport of gases by blood. Diffusion of gases in the tissues.
12. Control of breathing. Neural and chemical control of breathing.
13. The fundamentals of clinical neurophysiology: EEG physiology,
14. Emotional responses
15. Adaptive significance of emotional states,
16. Lateralization of cerebral hemispheres," male brain" and "female brain".
17. Physical activity and human health.
18. Adaptation mechanisms: the influence of high mountain environment on human body.
19. Adaptation mechanisms: the influence of high pressure on human body.
20. Adaptation mechanisms: the influence of temperature pressure on human body.
21. Circadian rhythms.
22. Energy balance.
23. Homeostasis.
24. The role of hepcidine in iron level regulation in plasma.
25. Primary and secondary haemostasis.
26. Haemostasis system balance.
27. The autoregulatory mechanisms in kidneys.
28. RAA system and its functions.
29. The influence of endocrine system in the regulation of blood volume and pressure.
30. Psychoneuroimmunology- is it better to be an optimist or pessimist.
X.
Classes topics:
1. The structure of membranes. Membrane channels. Membrane transport.
2. Resting and action potential in nervous cell.
3. Synaptic condutivity. Types of synapses.
4. The physiology of the skeletal and smooth muscle.
5. Autonomic nervous system.
6. Reflex action of the central nervous system. Movement and posture control.
7. The physiology of senses. Sensation and perception.
8. Brain and immunity - anatomical and functional basis for interaction of the neuroendocrine system
with immune system.
9. Termoregulation and thermal states of the body according to set-point theory. Pathogenesis and
significance of fever.
10. Biological clocks - their formal properties and neurophysiological basis. Physiology of the EEG.
11. The role of autonomic and limbic system in hormonal regulation. The role of the hypothalamus in
endocrinology. Neural control of the pituitary gland. Control of the pituitary gland glandular part.
Pituitary hormones - mechanism of interaction. Feedback loops.
12. Pancreatic endocrine function. Adrenal steroids - regulation of the synthesis, secretion and the
mechanisms of interaction. Stress and adrenal function. The role of adrenal androgens and
estrogen. Hypothalamus - pituitary – gonads axis.
13. The mechanisms of interaction between ovarian and testicular hormones. Pregnancy, childbirth,
lactation – the endocrine specificity.
14. Hormons as the modulators of brain ontogeny. The mediators of cyclical changes. Mediators
induced by environmental changes. Mediators of brain development and sex differentiation of the
brain.
15. Blood. Composition of blood. Blood group. Morphology and physiology of erythrocytes, leukocytes
and thrombocytes. ESR. Cross - matching blood test. Immunological mechanisms. Haemostasis.
Hemostatic balance.
16. Functional anatomy of kidneys. Structure of nephron. Mechanisms of filtration, tubular resorption
and secretion. Autoregulation mechanisms in kidney.Urinary excretion. The effect of physical
exercise on urinary excretion.
17. Heart -electrical, mechanical and acoustic phenomenon.
18. Cardiac hemodynamics.
19. The mechanisms of regulation of the heart. Receptors.
20. Electrocardiogram- recording and results interpretation.
21. The effect of physical exercise on the cardiovascular system. Effort tests.
22. Blood pressure regulating mechanisms. Blood flow. Regulation of blood circulation in the brain,
lungs, skeletal muscle, kidney, liver. Heart and circulatory system before birth.
23. Structure and function of the respiratory system. The ventilation of the lungs.
24. Spirometry- recording and results interpretation.
25. Nervous and chemical regulation of breathing.
26. Mechanism of respiratory adaptation- the man at high altitude, high-pressure environment and
during physical activity.
27. Physiology of the digestive system.
28. Endocrine activity of digestive system
29. Acid-base balance.
30. Metabolism. The energy balance of the body. Overweight, obesity, "homo sedentarius” disease of
civilization.
XI.
The scope of the material for self-development:
1. Membrane channels and their functions.
2. Practical application of membrane channels.
3. News in the world of hormones.
4. Adaptive mechanisms of the human body.
5. Circadian rhythms, elements of chronomedicine and chronobiology.
6. Invasive and noninvasive diagnosis of the circulatory system.
7. Respiratory diagnostic methods.
8. Adaptive mechanisms of the human body.
XII.
Learning outcomes:
After completion the course, student:
1. explains the mechanisms of the human body function,
2. understands integration processes and interactions between different systems,
3. performs basic ECG examinations its interpretation,
4. performs effort test, lists and explains the indications and contraindications to effort tests.
5. is able to plan physical training and choose the appropriate physical activity to age, health
conditions and lifestyle to improve overall physical fitness .
XIII.
Required textbooks:
1. Raff H, Levitzky M, Medical Physiology: A Systems Approach, 1st edition, Lange McGraw-Hill, 2011
2. Guyton AC, Hall JE, The Textbook of Medical Physiology, 11th edition, Elsevier Saunders, 2006;
3. Seeley RR, Stephens TD, Tate P, Anatomy and Physiology, 6th edition, McGraw- Hill, 2006;
4. Purves D. et. al., Neuroscience, 3rd edition, Sinauer, 2004
Rules and regulations
Head of the Unit: Prof. dr. hab. med. Małgorzata Tafil-Klawe
Subject: Physiology with elements of clinical physiology
Faculty of Medicine
1. Physiology course consists of lectures and laboratories/seminars.
2. Both lecture and laboratory/seminar attendance is mandatory.
1. A formal excuse (see NCU policy) is required for each absence. The written excuse has to be
delivered to the TA as soon as possible after the absentee return.
2. All absentees are required to obtain the credit for unattended classes. The time and terms of credit
acquisition are decided by a respective TA.
3. At the beginning of the academic year, it is a duty of every student to familiarize her / him-self
with both electronic and paper information distribution systems utilized within the Department of
Physiology.
4. Students are expected to be familiar with all the current ordinances and information from
electronic and paper information systems.
5. Each student attending laboratory/seminar has to fulfill the following entry requirements:
a. arrive to the place of class meeting on time;
b. dress according to the safety code requirements;
c. be aware of the safety code requirements;
d. fulfill the knowledge requirements for the current class.
6. During a class student may be asked to leave the room and acquire the credit for the class in the
alternative time in the following circumstances:
a. student does not fulfill requirements described in pt. 5;
b. student behavior interferes with work of other student and/or TA’s work;
c. student is not actively participating in the current lab/seminar;
d. student does not follow the safety code guidelines.
7. The terms of lab/seminar credit acquisition are presented by the TA at the beginning of each
subject block.
8. Student is allowed to take mid-term tests only after acquiring credits for all labs/seminars in a
respective subject block.
9. Mid-term tests are administered at the end of each subject block. The detailed timing of the test
is decided and announced by a respective TA.
10. The subject matter covered by a given mid-term test includes:
a. knowledge presented during labs/seminars;
b. relevant knowledge presented during lectures;
c. information contained in the written/electronic resources indicated by a TA.
11. Student may retake a mid-term test twice. However, it is within a TA’s discretion to allow for the
retakes.
12. The lack of formal justification for an absence during a test eliminates the student’s right to take
the test.
13. The justified absence during a test does not alter the student’s eligibility to take a test.
14. In order to pass the Physiology Course in a given semester all lab/seminar credits have to be
acquired and all relevant tests have to be passed.
15. A failure to meet the requirements described in pt. 14 results in necessity to verify student’s
knowledge by the departmental commission.
16. Members of the departmental commission are nominated by the Department of Physiology
Chairwoman.
17. Labs/seminars are scored by graded or pass/fail systems.
18. The time and form of final exam are decided and announced by the Department of Physiology
Chairwoman.
The Department of Physiology Student Code of Conduct is based on § 24 of NCU Code of Conduct.
History and propedeutics of medicine
Weekly lectures. Prerequisite: second-year medical student. Students become acquainted with the
evolution of the concept of medicine as a science throughout the ages. Various socio-medical traditions
and the evolution of patient – physician interactions are also presented. Milestones in the development
of medicine, as well as the major historical figures and concepts are discussed.
Teacher:
1. dr Jakub Szmytkowski
Contact: dr Jakub Szmytkowski jakubszmytkowski@gmail.com
Syllabus
I.
Department of History of Medicine and Nursing
II.
Head of the unit: dr hab. Walentyna Korpalska
III.
Faculty of Medicine, Medical Program, year 2
IV.
Course Coordinator: Jakub Szmytkowski MD PhD
V.
Form of classes: lectures
VI.
Form of crediting: Exam, 2 ECTS points
VII.
Number of hours: 30 h
VIII.
Aim of the course:
To convey basic knowledge about: medicine as a science, the socio-medical traditions, the evolution of the
concept of human health and disease throughout history, the reactions to disease, therapy, physicians and
nurses. To explain the terms: science, medicine, health, disease, ethical norm. To help students develop
the ability to understand cause-and-effect relationships in the development of populations. To teach the
students to fully utilize modern and historical medical literature and perform critical analyses of historical
information.
IX.
Topics of lectures:
1.
Ludwik Rydygier – the patron of the Collegium Medicum
2.
History of medicine as a science, its scope and scientific tools. Historical sources. Introduction to
the history of Polish medicine.
3.
Medicine in the first civilizations: Mesopotamia, Egypt, China , India
4.
Medicine in ancient Greece – clerics, philosophers, physicians. Hippocrates and his school of
thought.
5.
Post – Hippocratic medicine. The Alexandrian school.
6.
Medicine in ancient Rome. Galen – the great reformer of medicine and pharmacology.
7.
Medieval medicine. Arab medicine. Avicenna.
8.
Medicine in medieval Europe. Secular medical schools in Montpellier and Salerno.
9.
The beginnings of Polish university medicine. The medical faculty of the Cracow Academy.
10.
Major figures in medieval medicine.
11.
The Renaissance of medicine.
12.
The evolving concepts of health and disease.
13.
Historic aspects of public healthcare. The history of hospitals from temple and poorhouse to
modern scientific and therapeutic institutions.
14.
Paracelsus, Andreas Vesalius, William Harvey – the founding fathers of modern medicine.
15.
The separation of surgery from medicine. The development of surgery and medicine until the
18th century.
16.
The foundations of modern medicine. The development of preclinical and basic sciences.
17.
The development of clinical medicine. Old and new Vienna schools.
18.
Therapeutic nihilism and skepticism. The 19th century – the age of pathologists.
19.
Surgery in the 19th and early 20th centuries.
20.
The history of anesthesia, aseptics and antiseptics.
21.
The development of clinical laboratory diagnostics.
22.
Medical microbiology. Louis Pasteur, Robert Koch.
23.
Polish microbiologists – Odo Bujwid, Rudolf Weigl.
24.
Radiology – a new diagnostic and therapeutic tool. The reception of W.K. Roentgen’s discovery in
Poland.
25.
Maria Curie – Skłodowska.
26.
Early medications.
27.
Pharmacology and its impact on the development of therapy.
28.
Polish medicine of the 19th and 20th centuries.
29.
Natural and unconventional treatment methods – history and present day.
X.
Self-study topics:
----------XI.
Booklist:
Basic:
The Western Medical Tradition: 800 BC to AD 1800;.
Lawrence I. Conrad, Michael Neve, Vivian Nutton, Roy Porter, and Andrew Wear
The Western Medical Tradition: 1800 AD to 2000 AD
W. F. Bynum, Anne Hardy, Stephen Jacyna, Christopher Lawrence, E. M. Tansey
Cambridge University Press 2006
Additional reading:
Cambridge History of Medicine, edited by Roy Porter
Cambridge University Press 1996
XII.
Detailed list of required practical skills and confirmation of completing:
Students become acquainted with the evolution of the concept of medicine as a science throughout the
ages. Various socio-medical traditions and the evolution of patient – physician interactions are also
presented. Milestones in the development of medicine, as well as the major historical figures and
concepts are discussed.
Rules and regulations
1.Attendance during lectures is mandatory.
2.The students are kindly requested to switch off mobile phones and other electronic equipment before
entering the classroom.
3.Please be punctual – come on time or do not come at all.
4.The lecture presentations will be made available to the students – do remember, however, that they
constitute copyrighted material.
Medical statistics
The course is aimed at providing students with knowledge and practical skills concerning basic statistical
methods. After the course students should understand an be able to apply such tools as estimating
parameters of probability distribution of a stochastic variable: quantiles, expectation value, standard
deviation, asymmetry, kurtosis etc. from data for a statistical sample. They should be able as well to
estimate degree of correlation between two stochastic variables, to calculate parameters of the linear
regression and to test simplest statistical hypotheses.
Teachers:
1. dr hab. Przemysław Staszewski, prof. UMK
2. dr Anita Dąbrowska
Contact: kinfmed@cm.umk.pl
Syllabus
I.
Chair of Theoretical Foundations of Biomedical Sciences and Medical Computer Science
II.
Head of the unit: dr hab. Przemysław Staszewski, Prof. UMK
III.
Faculty of Medicine, Medical Program, 2nd year
IV.
Course coordinator: dr hab. Przemysław Staszewski, Prof. UMK
V.
Form of classes: lectures, tutorials
VI.
Form of crediting/Assessment: Credit with grade, 2 ECTS points
VII.
Number of hours: 15 (lectures), 20 (tutorials)
VIII.
Aim of the course:
Lectures:
Basic notions of probability theory: random events and their properties, probability and its properties,
combinatorial formulae, conditional probability, independent events, Bernoulli experiment and Bernoulli
scheme.
Random variables: One-dimensional random variables: discrete and continuous. Examples of important
distribution functions of random variables:
binomial distribution, Poisson distribution, normal
distribution.
Parameters of distribution functions of random variables: mean (expectation) value, variance, moments
and central moments of order n, median.
Statistical inference for probabilistic experiments of two possible outcomes:
de Moivre-Laplace theorem. A statistical hypothesis, significance level and significance test, statistical
hypothesis testing, test functions. Verifying statistical hypotheses of p  p 0 and p  p 0 . The power of a
statistical test. Estimation of the parameter p. A confidence level and confidence interval.
Two-dimensional random variables. Populations and samples of two-dimensional random variables.
Examples of significance tests and their applications: A chi-square test for fit of a distribution, A chi-square
test for independence, Student’s t-test.
Pearson’s linear correlation coefficient.
Computer laboratory classes:
Solving simple problems of probability theory using combinatorics.
Determination and analysis of the distribution parameters of a sample.
Verification of statistical hypotheses given in the lectures.
Determination of the coefficient of linear correlation to verify the dependence of random variables.
IX.
Self-study topics:
-----------
X.
Booklist:
Medical Statistics at a Glance, Aviva Petrie & Caroline Sabin, Blackwell, 2005.
Essentials of Statistics In Heath Information Technology, Carol E. Osborn, Jones & Bartlett, 2007.
XI.
Detailed list of required practical skills and confirmation of completing
List of acquirements: Applcation of Bayes theorem, law of total probability and conditional probability in
solving medical problems; Determining the shape and estimation of the parameters of distribution
function of random variable; Standardizing the random variable and using the tables of distributions of
random variables; Interval estimation of distribution parameters, confidence interval; Putting and
verification of hypotheses, the choice of parametric and nonparametric tests of significance, checking
assumptions of the tests; Application of computer programs to medical statistics calculations.
Teaching method: lecture and computer laboratory classes.
Crediting conditions: classes credit.
Computer science
The course is aimed at providing students with practical skills in using the MS Office suite with particular
stress on advanced functions of the MS Word, MS Excel, and MS PowerPoint desktop applications. After
the course students should be able to write and format a document with inserted figures or graphs, tables
etc.; they should be able to apply MS Excel for elementary data processing, basic statistical and
mathematical analysis, plot production etc.; finally, they should be able to prepare MS PowerPoint
presentations with imported elements such as figures, plots, formulae etc.
Teachers:
1. mgr Artur Jasionowski
2. dr n. med. Magdalena Wietlicka-Piszcz
Contact: kinfmed@cm.umk.pl
Syllabus
I.
Chair of Theoretical Foundations of Biomedical Sciences and Medical Computer Science
II.
Head of the unit: Dr hab. Krzysztof Stefański, prof. UMK
III.
Faculty of Medicine, Medical Program, II year
IV.
Course coordinator: Dr hab. Krzysztof Stefański, prof. UMK
V.
Form of classes: tutorials at computer laboratory
VI.
Form of crediting: credit with a grade, 3 ECTS points
VII.
Number of hours: 45
VIII.
Aim of the course:
Instructing students how to apply MS Office and efficiently use Internet.
IX.
Topics of tutorials:
Application of word processor MS Word for creating and formatting documents
Formatting symbols and paragraphs. Spell-checking. Formatting documents with styles. Using equation
editor. Symbol inserting. Mail merge.
Application of spreadsheet program MS Excel for generating lists of data, data analysis and creating charts
Inserting data and formulae into the spreadsheet cells, formatting and addressing, formatting numbers,
date and time. Creating data series.
Functions – an overview of elementary functions . Nesting of functions. Logical functions, Date and time
functions, searching and addressing functions. Solving tasks using logical functions and date and time
functions.
Data visualisation: creating text diagrams, conditional formatting of data. Creating bar charts, line charts ,
pie charts and formatting their elements.
Array functions and creating their plots. Single-argument functions. Double-argument functions. Creating
surface charts.
Datebases with Excel: creating and processing databases. Importing data from Access.
Application of statistical functions with Analysis ToolPak: creating histograms, testing statistical
hypotheses, determining linear and nonlinear regressions.
Generating databases with MS Access
Defining tables, data types. Editing table data. Browsing and editing data. Data filtration. Query creating.
Sheet creating. Using report kreator.
Introduction to creating web pages with HTML
HTML file structure, references, lists, tables, graphics, etc.
X.
Self-study topics: individual work with computer.
XI.
Booklist:
1. Steve Lambert, M. Dow Lambert III, and Joan Preppernau, Microsoft® Office Access 2007 Step by Step,
Microsoft Press 2007
2. Curtis D. Frye, Microsoft® Office Excel 2007 Step by Step, Microsoft Press 2007
3. Joyce Cox and Joan Preppernau, Microsoft® Office Word 2007 Step by Step, Microsoft Press 2007
4. Steven M. Schafer , Html, Xhtml, And Css Bible, John Wiley & Sons 2010.
XII. Detailed list of required practical skills and confirmation of completing:
Full name of the student:
Course, group:
School year:
Practical skill
Creatin and formatting documents with MS Word:
formattting paragraphs, usage of styles; inserting of
tabe of contents, footnotes, formulae, and symbols;
checking of correctness.
Creating tables of data and their analysis with MS
Excel: dressing cells, formatting numbers, dates and
text; creating data series, using selected functions.. .
Visualizing data with MS Excel – creating plots,
Using statistical functions: tools of descriptive
statistics, creating histograms, creating pivot tables,
testing statistical hypotheses, application of simple
linear regressions.
Databases in MS Excel: creating simple databases,
adding data, sorting and filtering data, importing data
from other files.
Databases with MS Access: defining tables and
relations between them; editing data, adding and
removing of records, searching and filtering data,
querry creating, using simple criteria. Creating
formularies and reports..
date
signature of
of crediting
the authorized teacher
remarks
Creating WWW pages with HTML: inserting blocks of
text, lists, tables and graphic elements..
Computer science
The course is aimed at providing students with practical skills in using the MS Office suite with particular
stress on advanced functions of the MS Word, MS Excel, and MS PowerPoint desktop applications. After
the course students should be able to write and format a document with inserted figures or graphs, tables
etc.; they should be able to apply MS Excel for elementary data processing, basic statistical and
mathematical analysis, plot production etc.; finally, they should be able to prepare MS PowerPoint
presentations with imported elements such as figures, plots, formulae etc.
Teachers:
3. mgr Artur Jasionowski
4. dr n. med. Magdalena Wietlicka-Piszcz
Contact: kinfmed@cm.umk.pl
Syllabus
XII.
Chair of Theoretical Foundations of Biomedical Sciences and Medical Computer Science
XIII.
Head of the unit: Dr hab. Krzysztof Stefański, prof. UMK
XIV.
Faculty of Medicine, Medical Program, II year
XV.
Course coordinator: Dr hab. Krzysztof Stefański, prof. UMK
XVI.
Form of classes: tutorials at computer laboratory
XVII.
Form of crediting: credit with a grade, 3 ECTS points
XVIII.
Number of hours: 45
XIX.
Aim of the course:
Instructing students how to apply MS Office and efficiently use Internet.
XX.
Topics of tutorials:
Application of word processor MS Word for creating and formatting documents
Formatting symbols and paragraphs. Spell-checking. Formatting documents with styles. Using equation
editor. Symbol inserting. Mail merge.
Application of spreadsheet program MS Excel for generating lists of data, data analysis and creating charts
Inserting data and formulae into the spreadsheet cells, formatting and addressing, formatting numbers,
date and time. Creating data series.
Functions – an overview of elementary functions . Nesting of functions. Logical functions, Date and time
functions, searching and addressing functions. Solving tasks using logical functions and date and time
functions.
Data visualisation: creating text diagrams, conditional formatting of data. Creating bar charts, line charts ,
pie charts and formatting their elements.
Array functions and creating their plots. Single-argument functions. Double-argument functions. Creating
surface charts.
Datebases with Excel: creating and processing databases. Importing data from Access.
Application of statistical functions with Analysis ToolPak: creating histograms, testing statistical
hypotheses, determining linear and nonlinear regressions.
Generating databases with MS Access
Defining tables, data types. Editing table data. Browsing and editing data. Data filtration. Query creating.
Sheet creating. Using report kreator.
Introduction to creating web pages with HTML
HTML file structure, references, lists, tables, graphics, etc.
XXI.
Self-study topics: individual work with computer.
XXII.
Booklist:
1. Steve Lambert, M. Dow Lambert III, and Joan Preppernau, Microsoft® Office Access 2007 Step by Step,
Microsoft Press 2007
2. Curtis D. Frye, Microsoft® Office Excel 2007 Step by Step, Microsoft Press 2007
3. Joyce Cox and Joan Preppernau, Microsoft® Office Word 2007 Step by Step, Microsoft Press 2007
4. Steven M. Schafer , Html, Xhtml, And Css Bible, John Wiley & Sons 2010.
XII. Detailed list of required practical skills and confirmation of completing:
Full name of the student:
Course, group:
School year:
Practical skill
Creatin and formatting documents with MS Word:
formattting paragraphs, usage of styles; inserting of
tabe of contents, footnotes, formulae, and symbols;
checking of correctness.
Creating tables of data and their analysis with MS
Excel: dressing cells, formatting numbers, dates and
text; creating data series, using selected functions.. .
Visualizing data with MS Excel – creating plots,
Using statistical functions: tools of descriptive
statistics, creating histograms, creating pivot tables,
testing statistical hypotheses, application of simple
linear regressions.
Databases in MS Excel: creating simple databases,
adding data, sorting and filtering data, importing data
from other files.
Databases with MS Access: defining tables and
relations between them; editing data, adding and
date
signature of
of crediting
the authorized teacher
remarks
removing of records, searching and filtering data,
querry creating, using simple criteria. Creating
formularies and reports..
Creating WWW pages with HTML: inserting blocks of
text, lists, tables and graphic elements..
Clinical immunology
The course includes laboratory exercises focused on the presentation and individual preparation of the
selected immunological techniques most commonly used for the evaluation of phenotypical and
functional characteristics of innate and adaptive immune systems. The main topics will include:
peripheral blood lymphocyte isolation and cultures, flow cytometry and FACS analysis, monocyte and
lymphocyte subsets isolation using antibody-coated magnetic beads, identification of functional subsets
of T cells by staining for cytokines, stimulation of lymphocyte proliferation by treatment with polyclonal
mitogens or specific bacterial antigen, measurements of apoptosis, ELISA tests for cytokines
identification, phagocytosis evaluation techniques.
Teachers:
dr Lidia Gackowska
dr Anna Helmin-Basa
dr Andrzej Eljaszkiewicz
mgr Izabela Kubiszewska
mgr Milena Januszewska
Contact: kizimmun@cm.umk.pl, hermmina@gmail.com
Syllabus
I.
Name of the unit offering the course: Clinical Immunology
II.
Head of the unit: dr hab. Jacek Michałkiewicz Prof. UKM
III.
Faculty of Medicine, Medical Program, 2nd year
IV.
Course coordinator: dr hab. Jacek Michałkiewicz Prof. UKM
V.
Form of classes: lectures, tutorials
VI.
Form of crediting: Credit with grade, 5 ECTS points
VII.
Number of hours: 30 (lectures), 30 (tutorials)
VIII.
Aim of the course:
The immunology course for the group of the foreign medical students studying at Faculty of Medicine
second year will involve the basic subjects concerning the structures and functions of the immune
system and their significance in health and disease.
The course includes laboratory exercises (starting Feb, 16th 2011) focused on the presentation
and individual preparation of the selected immunological techniques most commonly used for the
evaluation of phenotypical and functional characteristics of innate and adaptive immune systems. The
main topics will include: peripheral blood lymphocyte isolation and cultures, flow cytometry and FACS
analysis, monocyte and lymphocyte subsets isolation using antibody-coated magnetic beads,
identification of functional subsets of T cells by staining for cytokines, stimulation of lymphocyte
proliferation by treatment with polyclonal mitogens or specific bacterial antigen, measurements of
apoptosis, ELISA tests for cytokines identification, phagocytosis evaluation techniques.
The second part of the course will include lectures on clinical immunology (starting next year).
The main topics will involve the introduction to immunology, basic features of innate and adaptive
immune systems, the immune system failures in the course of infection, allergy, hypersensitivity,
autoimmunity and transplantation.
IX.
Topics of lectures / tutorials:
The main topics concerning innate immunity – the introduction to the laboratory exercises:
General mechanisms of innate immune system action
Phagocytosis-types of cells involved, effector mechanisms, regulations
Pathogen recognition receptors (Toll and NOD systems)
Complement system main characteristics
Leucocyte rolling, adhesion, leucocyte extravasation
The main topics concerning adaptive immunity- the introduction to the laboratory exercises:
Lymphocyte receptors generation
Mechanisms of antigen recognition by lymphocytes
Antigen presenting cells (professional and non-professional)
Co-stimulation as a second and third signal of T cells induction
Exercise 1. 15-16.02.2011
Topic: Innate immunity – the introduction to the laboratory exercises:
dr hab. Jacek Michałkiewicz, Prof. UMK
Exercise 2. 22-23.02.2011
Topic: Cells of the Immune System and Antigen Recognition
Izabela Kubiszewska, MSc
Exercise 3. 01-02.03.2011
Topic: Mechanisms of cytotoxicity
Milena Urbańska, MSc
Exercise 4. 08-09.03.2011
Topic: Components of the innate immune system – the evaluation of the function of phagocytic cells.
Izabela Kubiszewska, MSc
Exercise 5. 15-16.03.2011
Topic: Adaptive immunity –the introduction to the laboratory exercises:
dr hab. Jacek Michałkiewicz, Prof. UMK
Exercise 6.22-23.03.2011
Topic: Flow cytometric measurement of intracellular proteins
Andrzej Eljaszewicz, MSc
Exercise 7.29-30.03.2011
Topic: Cell isolation and culture procedures in immunology.
Izabela Kubiszewska, MSc
X.
Self-study topics:
----------XI.
Booklist:
Basic literature
1.
Kenneth M. Murphy, Paul Travers, Mark Walpor
2.
Janeway’s Immunobiology, Garland Science available online at:
3.
http://www.ncbi.nlm.nih.gov/books/NBK10757/ (free)
4.
http://www.ncbi.nlm.nih.gov/sites/entrez?db=books (free)
5.
David Male, Ivan Roitt, Johathan Brostoff Immunology, Mosby.
6.
Abbas, Lichtman: Basic Immunology, Sauders.
7.
Helen Chapel, Mansel Haeney, Siraj Misbah, Neil Snowden Essentials of Clinical Immunology,
Blackwell.
8.
W. Luttmann, K. Bratke, M. Kupper, D. Myrtek Immunology Elsevier Science & Technology
Additional literature:
1.
Manjula Reddy, et al; “Comparative analysis of lymphocyte activation marker expression and
cytokine secretion profile in stimulated human peripheral blood mononuclear cell culture: an in vitro
model to monitor cellular immune function” Journal of Immunological Methods 2004. 293:127-142
2.
Marzio R. et al.; „CD69 and regulation of the immune function“; Immunopharmacology and
immunotoxicology 1999. 21:565-582
3.
Claman Prussin, Dean D. Metcalfe; “Detection in intracytoplasmic cytokine using flow cytometry
and directly conjugated anti-cytokine antibodies”; Journal of Immunological Methods 1995. 188:117-128
4.
Sewell W.A., et al.;”Determination of intracellular cytokines by flow-cytometry following wholeblood culture”; Journal of Immunological Methods 1997. 209:67-74
5.
Beate Mascher; et al.; “Expression and kinetic of cytokines determinated by intracellular staining
using flow cytometry”; Journal of Immunological Methods 1999. 223:115-121
6.
V Hemalatha, P Srikanth, M Mallika; SUPERANTIGENS – CONCEPTS, CLINICAL DISEASE AND
THERAPY; Indian Journal of Medical; (2004) 22 (4):204-211;
7.
Ulrich Sack, Atilla Tarnock, Gregor Rothe
8.
Cellular Diagnostic - basic principles, methods and applications of flow cytometry, ifcc.
Rules and regulations
1. The clinical immunology course includes lectures (30hours) and tutorials (30 hours)
2. Attendance is obligatory at each lecture and tutorial.
3. Each change between the groups must be approved by the teacher.
4. Students are expected to be punctual.
5. In case of absence students must present a sick leave.
6. Students should have the basic knowledge of the tutorial topics as well as have to actively participate
in the classes in order to accomplish the course.
7. Each tutorial includes a 10-point quiz, which is a form of evaluation of students’ knowledge,
8. Students who did not take the test because of the absence need to pass it individually no later than
two weeks after return from the sick leave.
9. To pass tutorials students need to collect 60% of total points
10. Students who receive less that 60% must take a test from knowledge presented in all tutorials.
11. The clinical immunology course ends with a credit-grade assigned for lectures and 60% of tutorials.