Integrated course: anatomy, physiology and BiochemistryModule Biochemistry
Academic Year 2023/2024 - Teacher: Gabriella LUPOExpected Learning Outcomes
After completing this module the student will learn the general knowledge on the molecular basis of life, the fundamental chemical properties of the substances, the structure and function of macromolecules involved in staying alive, both at the cellular and extracellular levels, and the metabolic transformations of biomolecules
Course Structure
Traditional lectures.
Should teaching be carried out in mixed mode or remotely, it may be necessary to introduce changes with respect to previous statements, in line with the programme planned and outlined in the syllabus.
Learning assessment may also be carried out on line, should the conditions require it.
Detailed Course Content
1) Amino acids: structure, function, physical and chemical characteristics and their classification.
2) Peptides: Characteristics of the peptide bond; examples of peptides of significant biological interest. Levels of structural organization and supramolecular protein. Levels of structural organization and supermolecular of nucleic acids. Chromoproteins transporter of oxygen: myoglobin and hemoglobin; structural and functional differences; factors that affect the binding of hemoglobin to oxygen; behavior allosterismo hemoglobin; role of hemoglobin in the transport of carbon dioxide; buffering action of hemoglobin; physiological and pathological forms of hemoglobin variants.
3) General properties and characteristics of enzymes; Classification and nomenclature of enzymes, isoenzymes, complex multi-enzyme; enzyme kinetics, affinity and activity: the Michaelis-Menten constant, maximum speed and their implications; graph of the double reciprocal for the calculation of KM; enzyme inhibitors (reversible and irreversible, competitive, non-competitive and incompetivi; methods to recognize the type of inhibition). Regulation of enzyme activity; Allosteric enzymes;
4) Vitamins, coenzymes and their role in metabolism (cAMP, cGMP, IP3, DAG, Ca++) and their synthesis, action and degradation.
5) The mitochondrial respiratory chain and its regulation, inhibitors and uncoupling; Energy-rich compounds.
6) Structural and functional characteristics of the different types of receptors for hormones and growth factors receptors (7-transmembrane helices, with the tyrosine kinase activity, receptors for steroid hormones, thyroid hormone receptors); signal transduction pathways (protein Gs, Gi and Gq; intracellular second messengers (cAMP, cGMP, IP3, DAG, Ca ++) and their mode of synthesis, action and degradation.
7) Metabolism: catabolism and anabolism. Respiratory chain and oxidative phosphorylation.
8) Glucose metabolism: glucose transporters; glycolysis and gluconeogenesis; citric acid cycle.
9) Lipid metabolism: lipogenesis and lipolysis; ketogenesis; plasma lipoproteins.
10) Metabolism of amino acids: transamination and deamination; urea synthesis.
11) Control of blood glucose: hormones (insulin, glucagon and epinephrine).
12) Muscle metabolism during physical exercise: the protein composition of muscle cell. Energetic mechanisms in physical exercise: oxidative catabolism, anaerobic glycolysis, high-energy phosphates. The Phosphocreatine. The myokinase and the role of the AMP. Biochemical characteristics of muscle fibers. Prolonged aerobic exercise of mild to moderate intensity. Exercise of short duration high intensity. Metabolism of lactate: lactate transporters, aerobic oxidation of lactate, Cori cycle. Cardiac metabolism and exercise.
Textbook Information
- Introduzione alla Biochimica di Lehninger – D.L. Nelson, M.M. Cox – ZANICHELLI
- Biochimica medica – Siliprandi, Tettamanti – PICCIN
Course Planning
| Subjects | Text References | |
|---|---|---|
| 1 | LE PROTEINE. La struttura degli aminoacidi. Il legame peptidico. Organizzazione strutturale delle proteine. collagene, elastina, cheratina. Le immunoglobuline e le lipoproteine plasmatiche. | Testo 1: cap. 4; Testo 2: capp. 3 e 4. |
| 2 | CROMOPROTEINE TRASPORTATRICI DI OSSIGENO. La struttura dell’Eme. Mioglobina ed Emoglobina. Il trasporto dell’ossigeno e del biossido di carbonio. L’effetto Bohr. Il 2,3-bisfosfoglicerato e suo ruolo fisiologico. Funzione tampone dell’emoglobina. Patologie | Testo 1: cap. 5 ; Testo 2: cap. 5. |
| 3 | Le proteine plasmatiche. L’albumina e le sue funzioni principali. Le principali proteine plasmatiche: gamma-globuline (funzione e cenni sulla struttura); le lipoproteine plasmatiche, metabolismo e ruolo fisiologico. Cenni sulla cascata di coagulazione. | Testo 2: cap. 25. |
| 4 | L’energia di attivazione e ruolo degli enzimi nell’abbassamento del suo valore. Lo stato di transizione nelle razioni. Curve di saturazione. Effetto della concentrazione del substrato. La curva e l’equazione di Michaelis-Menten. | Testo 1: cap. 6; Testo 2: cap. 7. |
| 5 | IL METABOLISMO GLUCIDICO: glicolisi, gluconeogenesi, il ciclo di Krebs. Le fermentazioni e LDH. Ciclo di Cori e dell'alanina. Il destino metabolico del piruvato | Testo 1: capp. 7, 12, 14 , 15, 16, 19 (parti curate a lezione); Testo 2: cap. 7, 19 (I) |
| 6 | IL METABOLISMO LIPIDICO. Ossidazione e Sintesi degli acidi grassi e regolazioni reciproche. I corpi chetonici e la loro utilizzazione energetica, in particolare nel miocardio. | Testo 1: capp. 10, 17 , 21 (solo 21.1) ; Testo 2: cap. 2, 12 |
| 7 | IL METABOLISMO DEGLI AMINOACIDI. Digestione e assorbimento degli aminoacidi e dei peptidi. Il catabolismo degli aa: reazioni di transaminazione, deaminazione e decarbossilazione. La Glutammato deidrogenasi. La Glutaminasi renale. Ciclo dell'Urea. | Testo 1: cap. 18 Testo 2: cap. 13 (parti curate a lezione) |
| 8 | LE VITAMINE e le loro implicazioni metaboliche e nella patologia. | Testo 2: cap. 8 |