Monday, August 24, 2009

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WELCOME


_______________________

UNIVERSITY OF GUADALAJARA

CURRENT COURSE SCHEDULE FOR 2008 CALENDAR SUBJECT TO NAME



CELL BIOLOGY

SUBJECT CODE
101 CELL AND MOLECULAR BIOLOGY DEPARTMENT CODE DEPARTMENT
BC
Cinci UNIVERSITY OF AGRICULTURAL BIOLOGICAL AND LOAD TIME 93 Hours
THEORY, PRACTICE
12 hours Total 105 10 CREDITS

VOCATIONAL TRAINING LEVEL PREREQUISITES BS Biochemistry
GOAL




study the cell as the fundamental unit COMPOSITION, STRUCTURE AND FUNCTION OF LIVING FOR ESTABLISHING THE BASIS FOR THE UNDERSTANDING OF THE PHYSIOLOGY OF BIOLOGICAL SYSTEMS



SPECIFIC OBJECTIVES 1. Identify the purpose of studying cell biology and its features, its scope and relationship to other areas of knowledge.

2. Knowing how prebiotic and processes that have led to levels of cellular organization now known, differentiating cells of prokaryotes eukaryotic cells both plant and animal.

3. Study the principles that govern the formation and function of biological membranes from its components, as well as transport mechanisms through membranes.

4. Studying the structure of intracellular organelles, integrating biochemical knowledge of metabolism with the function and structure of them.

5. Understanding the mechanisms that allow inter-and intracellular communication.

6. Understanding the mechanisms by which preserves and transmits the biological information.


THEMATIC CONTENT SYNTHETIC

conceptual units

1. INTRODUCTION TO THE STUDY OF THE CELL. hours: 4 Hrs.

1.1. DEFINITION AND SCOPE OF CELL BIOLOGY
(and its relation to other areas)
1.2 Levels of biological organization
1.3 Characteristics of living matter and cellular theory
1.4 Features of prokaryotes and eukaryotes
1.5 TECHNIQUES USED IN CELL BIOLOGY

2. ORIGIN AND EVOLUTION OF THE CELL. hours: 6 Hrs.

2.1 Historical background (Various theories)
2.2 STAGES OF THE ORIGIN OF LIFE

2.2.1 Abiotic Stage (Theory of Evolution Chemical Oparin and Haldane)

2.2.1.1 Origin and formation of the universe.
2.2.1.2 Origin and formation of the earth. Training
air and primeval soup
Synthesis of monomers and polymers (Miller, Urey, Wachterhauser and others)

Stage 2.2.2 Prebiotic Evolution (protobiological)

2.2.2.1 pre-RNA world (metabolic systems vs. self-replicating systems) 2.2.2.2
RNA World (autocatalytic systems, self-replicating and inheritable) Models 2.2.2.3
prebiotics (protobiont, sulfobios, microspherules protein and coacervates)

Stage 2.2.3 Biological Evolution (biological)

2.2.3.1 In prokaryotes to eukaryotes: compartmentalization and endosymbiosis. Food
: heterotrophs vs. autotrophs.
Metabolism: Aerobic vs. Anaerobic
Power: Photosynthetic
Chemosynthetic
vs 3. Cell membranes. hours: 20 Hrs

3.1. STRUCTURE, COMPOSITION AND FUNCTIONS OF THE PLASMA MEMBRANE

3.1.1 Structure and chemical composition (membrane structure models)

3.1.1.1 Properties: semipermeable Asymmetry, fluidity, elasticity and resistance to stress.

3.1.2 Functions of the membrane. 3.1.3 Specializations


membrane junctions
3.1.3.1 (strong, adherent and communicating)
3.1.3.2 Receivers (plasma membrane and intracellular)
3.1.4 Extracellular matrix and cell wall

3.2. Membrane transport mechanism

3.2.1 Through Membrane Transport

3.2.1.1 Passive Diffusion

simple
Σ Σ Osmosis: hypotonic, isotonic, hypertonic. Σ
Facilitated diffusion: permeases, ion channels

3.2.1.2 Active Transport
Σ
by Co-transporters Unidirectional

Exchange Σ Σ Bi ion pumps

3.2.2 By

3.2.2.1 Endocytosis Vesicles


Σ Σ Pinocytosis Receptor-mediated endocytosis Phagocytosis


Σ 3.2.2.3 Exocytosis

4. INTRACELLULAR ORGANIZATION. hours: 32 Hrs. 4.1

endomembrane system and intracellular organelles



Core 4.1.1 Structural Components (nuclear envelope, nuclear matrix, chromatin) and complex
supramacromolecular
Nucleosome

functions (replication and transcription)



4.1.2 Smooth endoplasmic reticulum: Rugged
lipid synthesis, protein synthesis and complex
supramacromolecular
Ribosome 4.1.3


Golgi complex protein modification
Vesicle formation

vesicles System 4.1.4 Lysosomes


microbodies (peroxisomes, glyoxysomes, glycosomes, hydrogenosomes)

storage vesicles Vesicles secretion granules




4.1.6 4.1.5 Mitochondria Chloroplasts

4.2. CYTOSKELETON AND MATRIX Cytoplasmic

4.2.1 4.2.2 Microtubule System

microtrabecular microtubule organizing center and complex
supramacromoleculares Centrioles and Basal Bodies and Flagella Cilia
of prokaryotes and eukaryotes. 4.2.3

Microfilaments actin and myosin

nonmuscle cells
sarcomere structure and muscle contraction

4.2.4 Intermediate Filaments


5. CELL COMMUNICATION. hours: 16 Hrs.

5.1 BASICS OF CELLULAR COMMUNICATION
Issuer, Message, Medium, Receiver and Response
INTERCELLULAR
5.2 Communication



5.2.1 Characteristics 5.2.2 Examples: Communication

endocrine, autocrine, paracrine
neuron-neuron communication, neuron-muscle cell, neuron-cell secretory intracellular communication


5.3

5.3.1 System Components 5.3.2
Examples: Via cAMP; Way of DAG and IP3, and others.

6. CELL CYCLE . Hours: 15 hrs .



6.1 Concept 6.2 STAGES OF CELL

Phases 6.2.1: M, G1, S, G2, G0.

6.2.2 Cell division (M phase) 6.2.2.1
Eukaryotes: Mitosis, Meiosis.

6.2.2.2 Prokaryotes: binary fission, sporulation

6.3
cell cycle regulation
inducers and repressors Factors 6.3.1.


LABORATORY PRACTICE

1. Formation of coacervates.
2. Cell differentiation prokaryotes and eukaryotes (animal and plant)
3. Transport through membrane (osmosis).
4. Isolation of chloroplasts.
5. Mitosis. BASIC BIBLIOGRAPHY



1) Molecular Biology of the Cell. Alberts. 3a. ed. 2002. Garland
2) Cell Biology. Wood, Smith. 1a. ed. 2006. Addison Wesley
3) Cell Biology Avers, Ch 2a. ed. 2002. Grupo Editorial Iberoamericano.
4) Cellular Physiology. Giese, AE 4a. ed. 1999. American.
5) Cell and Molecular Biology. Robertis and Robertis. 10a. ed. 1999. El Ateneo.
6) Cell Biology. Junqueira, et al. 1a. 5a. Reprinted 1990. Mexican Medical Press.
7) Cellular Biology. Gerald Karp. American / McGraw Hill. 1999
8) The Cell, A Molecular Approach, Cooper GM "2nd Ed 2000. ADM PRESS
9) Molecular Cell Biology. Lodish, H. ET. AL. 2000. Freeman.



SUPPLEMENTARY BIBLIOGRAPHY 1. The Origin Life. Lazcano-Araujo, A. Ed. Trillas, 1990.
2. Molecular Biology of the Gen. Watson, J. 4a. ed. 1987. The Benjamin / Cummings Publishing Co, Inc.
3. The living cell. De Duve, A. 1992. Scientific American Library. Scientific Press.
4. Biochemistry. Leningher, A. 2a. ed. 1980. Omega.
5. Biology. Solomon, Ville, et al. 2a. ed. 1992. McGraw Hill-Interamericana.
6. Histology. Weiss, L. & Greep. 4a. ed. 1977. McGraw Hill.
TEACHING-LEARNING


In a theoretical-practical, such as this, the transmission of subject content is the responsibility of the teacher, student and reference literature and materials properly programmed and method transfer of matter to the laboratory or field work.

One idea is to unify the classroom, laboratory and field, creating a course designed teaching aids "on purpose" under the scheme: Reading - research presentation - discussion, demonstration - Exercises - practice - testing, evaluation - measurement - Accreditation - promotion. This model seeks flexible learning mode to carry out a continuous upward development of school learning.

FEATURES OF THE IMPLEMENTATION OF THE SUBJECT BUSINESS

common basic matter, relevant for students of Biology, Agronomy, and Veterinary Medicine, which sets the stage for understanding the functioning of biological systems.

KNOWLEDGE, SKILLS, VALUES, ETC.

With the development of the course, it is intended that students acquire skills and abilities allowing him to identify the importance of the cell as the fundamental unit of living things



Evaluation methods Evaluation of Teacher (ordinary and extraordinary course) Reviews
theoretical partial participation and attendance

presentations
analysis and discussion of reading questions and answers


Product Practices
terminal Departmental Review (Value 10% of final grade)

PARTICIPATION IN CLASS 10%
exams
40% 10% departmental review

PRACTICES 10% 30% TASKS


White Lump On Roof Of Mouth Symptoms

CELLULAR BIOLOGY PROGRAM Semester 2009 B





Model proposed by Singer and Nicolson


Cell Membrane

Functionally the cell membrane behaves as a semipermeable barrier: Some water-soluble and fat-soluble substances of low molecular weight readily cross cell membranes, while electrically charged molecules or large (protein) do not. Transmembrane movement of drugs are influenced by the composition and structure of the cell membrane. This is thin (70 - 100 Armstrong) and composed of phospholipids and carbohydrates as well as scattered groups of proteins comprehensive act as receptors, channels, pumps, enzymes or simply structural. The theory of the lipid bilayer or membrane unit proposed by Davson and Danielly (1952), considers that the cell membrane is composed of two layers of phospholipids between two layers of proteins, with the "heads" hydrophilic phospholipids oriented outside while the "tails" are aligned towards the hydrophobic interior. This theory explains the observation that lipid-soluble drugs tend to more easily penetrate the membrane polar substances. However, this model does not take into account the diffusion of water, the passage of low molecular weight molecules (urea) and certain ions.

fluid mosaic model proposed by Singer and Nicolson (1972), explains the transcellular diffusion of polar molecules. According to this model represented in the graph, the membrane globular protein is embedded in a fluid dynamics in a matrix of a lipid bilayer. These proteins provide a route for the selective transfer of ions and polar molecules through the lipid barrier and pore forming two types: The first about 10 nanometers and the other between 50-70 nm. The first act as channels for the diffusion of water or ions (Na +, K +, Cl-, etc).

taken from: http://www.virtual.unal.edu.co/cursos/ciencias/12161/lecciones/02_01_01.htm

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The Fluid Mosaic Model of the Cell Membrane - The Mosaic



Module by: Laura Martin


Although the bilayer nature of the cell membrane was described in the mid-1920's, it was not until 1972 that the currently accepted model of the plasma membrane, the fluid mosaic model, was formally outlined by S. J. Singer and Garth L. Nicolson in the journal Science.


Singer’s work on membrane structure originated in the 1950’s when he, along with other protein chemists, demonstrated that many water-soluble proteins like those found in cytoplasm could unexpectedly dissolve in nonaqueous, non-polar solvents. Furthermore, the shape a protein assumed differed in hydrophobic and hydrophilic environments (Singer, 1992).

From an historical perspective these results are significant because they led Singer to wonder about the structure of the proteins revealed to be closely associated with lipid-rich, and therefore nonaqueous, cell membranes in the 1930’s (Eichman, 2007). As he later wrote,

Although we had not experimented with membrane proteins and knew very little about membranes at the time, as almost an aside we speculated [in a 1962 publication] that because “the cellular environment of many proteins contains high concentrations of lipid components in a wide variety of cellular membranes, the gross conformations of these proteins in situ may be determined by this association with a nonaqueous environment.” This notion set off a train of ideas and experiments that eventually led us to the fluid mosaic model. (Singer, 1992, p.3)

At the time Singer's train set off, the standard model for membrane structure, the Davson-Danielli-Roberston (DDR) model, was a bilayer of lipids sequestered between two monolayers of unfolded protein (Figure 1). Each protein layer faced an aqueous environment, cytoplasm or interstitial fluid, depending upon whether the membrane enclosed an organelle or the cell itself (Figure 1; Singer, 1992).


Figure 1: Original figure from Singer (1992) illustrating the Davson-Danielli-Robertson model of the plasma membrane. Notice that the lipid bilayer is isolated from the surrounding aqueous environment by two layers of unfolded membrane protein (p). Each membrane forming lipid is composed of a polar head group (h) and fatty acyl tail (f). Text added.

When Singer and colleagues applied their understanding of the influence of solvent environment on protein conformation specifically to the problem of membrane proteins, they realized the DDR model was energetically untenable. As he and Nicolson (1972) later wrote,

The latter [DDR] model is thermodynamically unstable because not only are the
non-polar amino acid residues of the membrane proteins in this model perforce [by circumstance] largely exposed to water but the ionic and polar groups of the lipid are sequestered by a layer of protein from contact with water. Therefore, neither hydrophobic nor hydrophilic interactions are maximized in the classical [DDR] model. (Singer and Nicolson, 1972, p.721)

That is, the DDR model was energetically unfeasible because the constitutive molecules could not stably persist in aqueous cytoplasm in the physical conformation proposed. Just as oil and water will spontaneously separate when left to stand after shaking, the hydrophilic and hydrophobic components of a single polypeptide or an entire cell will spontaneously organize so that hydrophilic elements are in contact with the aqueous environment and the hydrophobic elements are sequestered, isolated from contact with polar components.

Thus, they reasoned that membrane proteins in a cell will assume globular (folded) conformations, due to hydrophobic and hydrophilic amino acid residues interacting with each other and the solvent environment, not the unfolded structures suggested by the DDR model. Similarly, membrane proteins will not be positioned to prevent contact between the polar head groups of membrane lipids and the aqueous cytoplasm.

So, if membrane proteins are globular and not layered on top of the membrane, where are they? How are they associated with the membrane?

The mosaic element of Singer and Nicolson's (1972) fluid mosaic model answered these questions. According to this model, membrane proteins come in two forms: peripheral proteins, which are dissolved in the cytoplasm and relatively loosely associated with the surface of the membrane, and integral proteins, which are integrated into the lipid matrix itself, to create a protein-phospholipid mosaic (Figure 2; Singer and Nicolson, 1972).



Figure 2: Original figure from Singer and Nicolson (1972) depicting membrane cross section with integral proteins in the phospholipid bilayer mosaic. Phospholipids are depicted as spheres with tails, proteins as embedded shaded, globular objects. Peripheral proteins, which would be situated at, not in, the membrane surface, are not shown. Recall that both surfaces of this membrane intercept an aqueous environment either the cytoplasm and/or the interstitial fluid. Transmembrane protein spanning entire membrane on left.Figure 2 (Fluid mosaic diagram Singer and Nicholson resized.jpg)

Singer and Nicolson (1972) supported these categories of proteins and their physical arrangement with both physical and biochemical evidence. For example, researchers had successfully separated the bilayers of frozen plasma membranes from a variety of sources including vacuoles, nuclei, chloroplasts, mitochondria and bacteria to reveal proteins embedded within (Singer and Nicolson, 1972). Similarly, evidence had also emerged to support the existence of transmembrane proteins, proteins that traversed the entire plasma membrane and extended into the aqueous environment on either side of the membrane (Figure 2).

Clear data supporting the predicted biochemical structure of integral proteins was harder to gain, however, and would only follow many years after the publication of the model. What was the biochemical structure of these proteins predicted to be?

Consider the energetic principles and molecular interactions on which Singer and Nicolson's model is based. Use your understanding of how these principles influence the structure and organization of individual polypeptides and the structural components of cells to answer the following questions.

1. Examine Figure 2. Predict biochemical properties (for example the hydrophobic or hydrophilic regions) of an integral protein versus those of a peripheral protein. Please be sure to explain your reasoning.

2. How do your predictions of the biochemical nature of integral proteins compare to Singer and Nicolson's predictions (Figure 3) adapted from a figure published by Lenard and Singer in 1966? If your predictions differ, please be sure to explain how and why they do.



Figure 3: Original figure from Singer and Nicolson (1972) depicting membrane cross section with integral proteins in the phospholipid bilayer. The ionic and polar portions of the proteins, as indicated by the +/- signs, contact the aqueous solutions (cytoplasm and/or interstitial fluid) surrounding the lipid bilayer. The membrane spanning or inserted region of the protein is non-polar/hydrophobic and therefore lacks charge as indicated by the absence of +/- symbols.Figure 3 (Amphipathic protein diagram Singer and Nicholson resized.jpg)
Works Cited

* Eichman, P. 2007. http://www1.umn.edu/ships/9-2/membrane.htm. SHiPS Resource Center for Sociology, History and Philosophy in Science Teaching
* Lenard, J. and S.J. Singer. 1966. Protein conformation in cell membrane preparations as studied by optical rotatory dispersion and circular dichroism. Proceedings of the National Academy of Sciences. 56:1828-1835.
* Singer, S.J. and G. L. Nicolson. 1972. The fluid mosaic model of the structure of cell membranes. Science. 175: 720-731.
* Singer, S.J. 1992. The structure and function of membranes - a personal memoir. Journal of Membrane Biology. 129:3-12.


E-mail the author of the module, The Fluid Mosaic Model of the Cell Membrane - The Mosaic

http://cnx.org/content/m15255/latest/

Sunday, August 23, 2009

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