Syllabus query



Academic Year/course: 2017/18

26703 - Human biochemistry


Syllabus Information

Academic Year:
2017/18
Subject:
26703 - Human biochemistry
Faculty / School:
104 - Facultad de Medicina
229 - Facultad de Ciencias de la Salud y del Deporte
Degree:
304 - Degree in Medicine
305 - Degree in Medicine
ECTS:
6.0
Year:
1
Semester:
First semester
Subject Type:
Basic Education
Module:
---

5.1. Methodological overview

The learning process designed for this subject is based on the following:

The activities programmed for the course are the same in the different groups at the School of Medicine in Zaragoza and the School for Health and Sport Sciences in Huesca.

The course is composed of 40 one-hour lectures, 10 hours of laboratory sessions, and 10 hours of seminars. Students will also have to carry out and present 4 tutored reports.

With regard to the lectures, the materials for each chapter will be available at the Photocopying Service at least one week before the beginning of that chapter lectures, so that students can peruse it in advance. These materials will also be available through the webpage dedicated to this subject in the ADD (University’s teaching website).

Seminars will be organized around 2 hour sessions and will be used to discuss the functional-structural properties of biomolecules.

Laboratory sessions of two hours are taught in small groups of 15 students each. Student performance will be assessed through specific questions included in the final text exam.

Tutored reports will be carried out individually and their themes will be related to the main contents of the subject. This activity also aims to develop the transversal learning competence of using Internet based communication and knowledge resources.

5.2. Learning tasks

The program is designed to help the students reach their learning goals, and includes the following activities:

1. Lectures

2. Seminars

3. Laboratory sessions: students will be informed about the risks and hazards they may become exposed to in the laboratories, and about actions to be taken in case of accident. Students will be asked to sign a consenting form binding them to follow security rules before they can take part in the laboratory sessions. Students can request more information from the Unit for Prevention of Labor Risks at http/uprl.unizar.es/estudiantes.html

4. Tutored reports

5. Clinical cases

6. Tutorial sessions with professors of the subject.

7. Evaluation

5.3. Syllabus

CHAPTER I: AMINO ACIDS AND PROTEINS

 

Lecture 1. Amino acids, Structure, properties and classification of proteinogenic amino acids. Stereochemistry. Acid-base properties of amino acids.

 

Lecture 2. Proteins. Composition of proteins. Classification. Functional diversity of proteins. Primary structure. Peptide bond. Acid-Base properties of peptides. Peptides of biological interest.

 

Lecture 3. Spatial conformation of proteins. Regular conformations of polypeptide chain: a-helix and b-sheet  secondary structures. Collagen helix. Non covalent forces determining and stabilizing secondary structure.

 

Lecture 4. Conformation of globular proteins: tertiary and quaternary structures. Myoglobin: structure. Heme group binding to protein and oxygen. Quaternary structure: hemoglobin. Types of hemoglobin. Tertiary structure of globins. Oxygen saturation curves for myoglobin and hemoglobin. Regulation of hemoglobin oxygenation. Bohr effect. Fetal and S hemoglobin. Thalassemias.

 

Lecture 5. Enzymes. General properties of enzymes. Specificity. Classification and nomenclature. Distribution of enzymes. Isoenzymes. Enzymes in clinical diagnostics. Enzyme quantification.

 

Lecture 6. Enzyme kinetics. Catalysis and enzyme mechanism of action. Enzyme kinetics: Michaelis-Menten equation and its transformations. Effects of pH, temperature and enzyme concentration in enzymatic reaction speed. Enzyme inhibitors.

 

Lecture 7. Regulation of enzyme activity. Metabolic regulation. Induction, repression and derepression. Proenzymes. Antienzymes. Feedback and covalent modification.

 

Lecture 8. Vitamins. Hydrophilic vitamins and their roles as coenzymes. Structure and function. Lipophilic vitamins. Structure and function.

 

Laboratory sessions:

Session 1: Serum protein electrophoresis in cellulose acetate strips.

Session 2: Clinical case I: Clinical Enzymology.

Session 3: Clinical case II: Vitamin B12 deficit and vitamin D toxicity.

 

Learning activities:

Lectures: 10 hours

Laboratory sessions: 5 hours

Student autonomous work: 18.5 hours.

 

 

CHAPTER II: STORAGE AND USE OF GENETIC INFORMATION

 

Lecture 9. Nucleic acids. Structure and properties of nucleosides and nucleotides. DNA structure: double helix. DNA supercoiling. Topoisomerases. Chromatin structure. RNA: structure and types. Degradation of nucleic acids.

 

Lecture 10. DNA replication. General characteristics of replication: semiconservative, bidirectional. Mechanisms for DNA replication in prokaryotes. Primosome and replisome. DNA reparation. Replication origin.

 

Lecture 11. DNA transcription: RNA synthesis. Prokaryote transcription. Post-transcriptional modifications of rRNAs and tRNAs. Ribozymes.

 

Lecture 12. Translation of genetic message: protein biosynthesis. The genetic code. Translation machinery: involved molecules. Activation and binding of amino acids to tRNA: aminoacil tRNA synthetases. Prokaryote protein synthesis. Post-translational modifications. Differential characteristics os eukaryote protein synthesis. Inhibitors of protein synthesis.

 

Lecture 13. Mitochondrial genetic system. Gene organization. Replication and transcription of mammal DNA. RNAs processing. Regulation of expression.

 

Laboratory Session:

Session 4: Nucleic acids: Isolation and purification of DNA.

 

Learning activities:

Lectures: 6 hours

Laboratory sessions: 2 hours

Student autonomous work: 10 hours.

 

CHAPTER III: INTRODUCTION TO INTERMEDIARY METABOLISM

 

Lecture 14. Intermediary metabolism. Concept. Catabolic, anabolic and amphibolic routes. Bioenergetics: exergonic and endergonic processes. Energetic coupling. Energy rich compounds: chemical characteristics. Transferred chemical groups. Types of energy rich bounds. Enzymes and coenzymes involved in biological oxydoreduction processes.

 

Learning activities:

Lectures: 3 hours

Student autonomous work: 4.5 hours.

 

 

CHAPTER IV: METABOLISM OF CARBOHYDRATES

 

Lecture 15. Glycolysis. Glucose uptake by tissues. Stages of glycolysis. Pyruvate metabolic fates. Metabolic and hormonal regulation of glycolysis. Stoichiometry and energy balance. Cori's cycle. Other hexoses incorporation of glycolytic pathway. Pyruvate oxidation to acetyl-CoA.

 

Lecture 16. Cytric acid cycle. Cycle's role within intermediary metabolism. Cellular localization. Metabolic reactions and their regulation. Cycle's energy balance. Anaplerotic reactions.

 

Lecture 17. Biological oxidation and respiratory chain. Components of respiratory chain. Sequence of respiratory chain components. Oxidative phosphorylation. Structure and function of ATP synthetase. Chemiosmotic hypothesis. Specific transport systems in the mitochondria's inner membrane: translocases. System of mitochondrial shuttles. ATP balance in glucose total oxidation. Reactive oxygen species, antioxidant defenses and human disease.

 

Lecture 18. Gluconeogenesis. Specific reactions. Metabolic and hormonal reactions. Stoichiometry and energy balance. Enzymatic differences between glycolysis and gluconeogenesis. Alterations in gluconeogenesis in humans.

 

Lecture 19. Glycogen metabolism and its regulation. Glycogen stores and their physiological role. Glycogenolysis. Synthesis of Glycogen. Hormonal regulation of glycogen metabolism in muscle and liver. Glycogen phosphorylase system. Glycogen synthetase system. Dephosphorylation of enzymes: phosphatases. Glycogenosis.

 

Lecture 20. Pentose phosphate pathway. Reactions of oxidative phase. Reactions of non oxidative phase. Regulatory mechanisms. Enzymatic defects. Glucuronic acid pathway.

 

Lecture 21. Heteroside metabolism. General properties. Biosynthesis of glycoproteins: N-glycans and O-glycans. Control of glycoprotein biosynthesis. Glycoprotein catabolism. Biosynthesis and degradation of proteoglycans. Mucopolysaccharides.

 

Laboratory sessions

Session 5: Carbohydrates: Starch hydrolysis and determination of reducing sugars.

 

Learning activities:

Lectures: 9 hours

Laboratory sessions: 2 hours

Student autonomous work: 12 hours.

 

 

CHAPTER V: LIPID METABOLISM

 

Lecture 22. Lipoprotein metabolism. Exogenous and endogenous lipid transport. Reverse cholesterol transport.

 

Lecture 23. Adipose tissue metabolism and fat mobilization. Lipolysis. Hormonal regulation of lipolysis. Lipolysis products fate: liver metabolic reactions. Fat liver degeneration.

 

Lecture 24. Fatty actid oxidation. Fatty acid activation in cytosol and transport inside mitochondria. Carnitine as shuttling molecule. Mitochondrial beta-oxidation of even-and odd-chain saturated fatty acids. Energy balance.

 

Lecture 25. Ketonic bodies metabolism. Ketogenesis. Use of ketonic bodies by extrahepatic tissues: cetolysis. Regulation of fatty acid beta-oxidation and ketogenesis.

 

Lecture 26. Biosynthesis of fatty acids: lipogenesis. Biosynthesis of even-and odd-chain saturated fatty acids. Sources of acetyl-CoA and NADPH for lipogenesis. Malonil-CoA formation. Enzymatic and co-enzymatic components of fatty acid synthase. Metabolic reactions. Regulation of synthesis of fatty acid. Fatty acid chain elongation. Biosynthesis of mono-and polyunsaturated fatty acids.

 

Lecture 27. Eicosanoid biosynthesis. Eicosanoid precursors. Metabolism of araquidonic acid. Biosynthesis of eicosanoids: cyclooxigenase pathway and lipoxigenase pathway. Catabolism of eicosanoids. Mechanism of action of eicosanoids and its clinical significance.

 

Lecture 28. Metabolism of complex lipids. Biosynthesis of triacylglicerides. Biosynthesis of phosphoacylglycerides: de novo pathway and saving pathway. Phosphoacylglycerides degradation. Biosynthesis and degradation of sphingolipids.

 

Lecture 29. Metabolism of cholesterol. Whole body cholesterol balance. Biosynthesis of cholesterol. Mevalonate formation. Mevalonate transformation into squalene. Squalene transformation into cholesterol. Control of cholesterol synthesis.: HMG-CoA reductase. Cholesterol transport. Diseased caused by alterations in cholesterol metabolism.

 

Lecture 30. Cholesterol derivatives with physiological significance in human body. Biliary acids. Biosynthesis of primary and secondary biliary acids. Regulation of biliary acid synthesis. Enterohepatic circulation. Cholesterol excretion. Steroid hormones from adrenal cortex and gonads: biosynthesis and degradation. Biosynthesis of 1,25-dihydroxycholecalciferol.

 

Laboratory Session:

Session 6: Metabolism Clinical cases.

 

Learning activities:

Lectures: 7 hours

Laboratory sessions: 1 hours

Student autonomous work: 11 hours.

 

 

CHAPTER VI: METABOLISM OF NITROGEN COMPOUNDS

 

Lecture 31. General reaction in amino acid catabolism. Transamination reactions. Oxidative deamination. Decarboxylation. Ammonia fate. Glutamine formation and ammonium excretion. Urea cycle and its regulation. Enzymatic defects in urea cycle.

 

Lecture 32. Fate of carbon skeleton from amino acids. Routes for amino acid carbon skeleton incorporation into different metabolic intermediates. Glycogenic and ketogenic amino acids.

 

Lecture 33. Conversion of amino acids into specialized products. Creatine and creatinin formation. Creatinine excretion rate as muscle mass index. Triptophane: serotonin precursor. Malignant carcinoid syndrome (argentaffin cell tumors). Metabolism of g-aminobutyrate.

 

Lecture 34. Metabolism of purines and pyrimidines.

 

Lecture 35. Metabolism of Hemoglobin. Biosynthesis and regulation of porphyrins and heme group. Porphyrias: definition and classification. Biosynthesis of hemoglobin. Catabolism of hemoglobin: metabolism of bilirubin, and biliary pigment formation. Jaundice.

 

Learning activities:

Lectures: 6 hours

Student autonomous work: 9 hours.

5.4. Course planning and calendar

Schedule for face-to-face activities and Tutored reports deadlines.

 

Summary of learning-teaching activities schedule.

 

ACTIVITY

ON-SITE HOURS

FACTOR

AUTONOMOUS EFFORT/OFF-SITE HOURS

TOTAL

Lectures

40

1.5

60

100

Seminars

10

1.5

15

25

Laboratories

10

0.5

5

15

Tutored Reports

 

 

6

6

Exams

 

 

4

4

Total

60

 

90

150

 

 

Activities and Calendar

 

The provisional schedule for this subject is shown below. This provisional planning is subject to modifications by the School.

 

Week

Lecture

Laboratory

Seminars/Tests

Off-site activities/Tutored Reports

1

Chapter I (3h)

Distribution of activities

 

Distribution of Tutored Reports

2

Chapter I (3h)

Seminar on proteins

 

 

3

Chapter I (3h)

Seminar on carbohydrates

 

 

4

Chapter I (1h)

Chapter II (2h)

Seminar on carbohydrates

 

 

5

Chapter II (3h)

Seminar on lipids

 

 

6

Chapter II (1h)

Chapter III (2h)

Seminar on lipids

Partial Evaluation

 

7

Chapter III (1h)

Chapter IV (2h)

Laboratory sessions

 

 

8

Chapter IV (3h)

Laboratory sessions

 

 

9

Chapter IV (3h)

Laboratory sessions

 

 

10

Chapter IV (1h)

Chapter V (2h)

Laboratory sessions

 

 

11

Chapter V (3h)

Laboratory sessions

 

 

12

Chapter V (2h)

Chapter VI (1h)

Laboratory sessions

 

 

13

Chapter VI (3h)

Laboratory sessions

 

Correction of Tutored Reports

14

Chapter VI (1h)

Laboratory sessions

Final Evaluation

 

5.5. Bibliography and recommended resources

Zaragoza:

 
BB Baynes, John W.. Bioquímica médica / John W. Baynes y Marek H. Dominiczak ; [revisión científica, María Josefa Sabriá Pau] . - 4ª ed. Ámsterdam ; Barcelona ; Madrid [etc.] : Elsevier, cop. 2015
BB Bioquímica / Christopher K. Mathews ... [et al.] ; revisión técnica José Manuel González de Buitrago . - 4ª ed. Madrid [etc.] : Pearson Education, 2013
BB McKee, Trudy. Bioquímica : las bases moleculares de la vida / Trudy McKee, James R. McKee ; traducción, Martha Elena Araiza Martínez, Anahí Hurtado Chong . - 5ª ed. Madrid [etc.] : McGraw-Hill Interamericana, cop. 2014
BB Nelson, David L. : Principios de bioquímica / David L. Nelson, Michael M. Cox ; coordinador de la traducción, Claudi M. Cuchillo. - 6ª ed. Barcelona : Omega, D.L. 2014
BB Stryer, Lubert. Bioquímica : con aplicaciones clínicas / Lubert Stryer, Jeremy M. Berg, John L. Tymoczko ; con la colaboración de Gregory J. Gatto, Jr. . - 7ª ed., imp. digital Barcelona [etc.] : Reverté, D.L. 2015
BC Bioquímica : libro de texto con aplicaciones clínicas / coordinada por Thomas M. Devlin. . - 4ª ed., reimp. Barcelona [etc.] : Reverté, D.L. 2008
BC Bioquímica ilustrada / Rodwell, Victor W... [et al.] ; traductor, Bernardo Rivera Muñoz. 30ª ed. México ; Madrid [etc.] : McGraw-Hill Interamericana, cop. 2016
BC Tymoczko, John L. : Bioquímica : curso básico / John L. Tymoczko, Jeremy M. Berg, Lubert Stryer ; [versión española traducida por Juan Manuel González Mañas] Barcelona [etc.] : Reverté, D.L. 2014
BC Voet, Donald : Fundamentos de bioquímica : la vida a nivel molecular / Donald Voet, Judith G. Voet, Charlote W. Pratt . - 4ª ed. Ciudad de México : Ed. Médica Panamericana, 2016


Huesca:

 
BB Baynes, John W.. Bioquímica médica / John W. Baynes y Marek H. Dominiczak ; [revisión científica, María Josefa Sabriá Pau] . - 4ª ed. Ámsterdam ; Barcelona ; Madrid [etc.] : Elsevier, cop. 2015
BB Berg, Jeremy M.. Bioquímica / Jeremy M. Berg, John L. Tymoczko, Lubert Stryer ; [versión española por José Mª Macarulla] . 6ª ed. Barcelona [etc.] : Reverté, D.L. 2007, cop. 2008
BB Bioquímica : libro de texto con aplicaciones clínicas / coordinada por Thomas M. Devlin. . 4ª ed., reimp. Barcelona [etc.] : Reverté, D.L. 2008
BB Mathews, Christopher K.. Bioquímica / Christopher K. Mathews, K. E. Van Holde, Kevin G. Ahern ; traducción José Manuel González de Buitrago. . 3̇ ed., reimp. Madrid [etc.] : Pearson, D.L. 2005.
BB McKee, Trudy. Bioquímica : la base molecular de la vida / Trudy McKee, James R. McKee ; [traducción, José Manuel González de Buitrago] . 1ª ed. [reimp.] en español, traducción de la 3ª ed. en inglés Madrid [etc.] : McGraw-Hill Interamericana, D.L. 2005
BB Nelson, David L. : Principios de bioquímica / David L. Nelson, Michael M. Cox ; coordinador de la traducción, Claudi M. Cuchillo. - 6ª ed. Barcelona : Omega, D.L. 2014
BB Principios de bioquímica / H. Robert Horton ... [et al.] ; traducción, Virgilo González y Pozo ; revisión técnica, Leticia Bucio Ortiz, Verónica Souza Arroyo, Luis Enrique Gómez Quiroz . - 4̇ª ed. Naucalpan de Juárez (México) [etc.] : Pearson Educación, 2008
BB Voet, Donald. Fundamentos de bioquímica : la vida a nivel molecular / Donald Voet, Judith G. Voet, Charlote W. Pratt ; [traducción de : María Inés Gismondi... (et al.)] . 2ª ed. Buenos Aires [et al.] : Ed. Médica Panamericana, D.L. 2007

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