GAPDH: Biological Properties and Diversity

2013
ISBN: 978-94-007-4715-9
Verlag: Springer Netherlands

Buch, Englisch, Band 985, 295 Seiten, HC runder Rücken kaschiert, Format (B × H): 183 mm x 260 mm, Gewicht: 787 g

Reihe: Advances in Experimental Medicine and Biology

The book represents a comprehensive review and synthesis of the biomedical literature that spans over a half-century on a single protein called glyceraldehyde 3-phosphate dehydrogenase (or, GAPDH). Due to the protein’s involvement in a vast array of cellular activities, GAPDH is of interest to the cell biologist, immunologist, virologist, biochemist etc. The protein has a significant role in fertility, cancer and neurodegeneration, suggesting that this book can be a vital resource for drug development. GAPDH function may provide insight into anesthesia. Furthermore, GAPDH is highly conserved meaning that the protein found in microorganisms, such as pathogens, remained relatively unchanged in evolution. Pathogens use GAPDH as a virulence factor, offering a unique challenge in developing anti-microbial agents that target this protein. To the evolutionary biologist, a book on the multi-functionality of GAPDH provides a focal point for a cogent discussion on the very origin of life.

Zielgruppe

Research

Autoren/Hrsg.

Seidler, Norbert W.

Fachgebiete

• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Medizin, Gesundheitswesen Biomedizin, Medizinische Forschung, Klinische Studien
• Naturwissenschaften Biowissenschaften Molekularbiologie
• Naturwissenschaften Biowissenschaften Kohlenhydrate
• Naturwissenschaften Biowissenschaften Lipidologie
• Naturwissenschaften Biowissenschaften Enzymologie
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Molekulare Medizin, Zellbiologie
• Naturwissenschaften Biowissenschaften Zellbiologie
• Naturwissenschaften Biowissenschaften Proteinforschung

Inhaltsverzeichnis

1. Basic Biology of GAPDH
1.1   The GAPDH Gene
   1.1.1   Coding Region
   1.1.2   Promoter Sequence
      1.1.2.1   Hypoxia-Responsive Elements
      1.1.2.2   Basal Level Expression
      1.1.2.3   Glutamine-Responsive Elements
   1.1.3   Testes-Specific Isoform
   1.1.4   Pseudogenes
1.2   Regulation of GAPDH Expression
   1.2.1   Tissue Specificity
   1.2.2   Electronic Databases
   1.2.3   Cancer
1.3   Cellular Levels of GAPDH
1.4   Oxidoreductase Activity of GAPDH
   1.4.1   Mechanism of Catalysis
   1.4.2   Kinetic Parameters
1.5   Protein Architecture of GAPDH 
   1.5.1   Asymmetric Homotetramer 
   1.5.2   Dinucleotide Binding Domain
   1.5.3   Catalytic Domain
2. GAPDH and Intermediary Metabolism
2.1   GAPDH, the Glycolytic Lynch-Pin
   2.1.1   Metabolic Switch
2.1.2          Glycolytic Tissues
   2.1.3   Anaerobic Glycolysis
2.2   Determining GAPDH Activity
   2.2.1   Chemical Inhibitors
   2.2.2   Measurement of Glycolytic Flux
   2.2.3   Oxidoreductase Activity of GAPDH
      2.2.3.1   Conditions of Assay
      2.2.3.2   Assay Protocol
2.3   Role of GAPDH Metabolites
   2.3.1   Counter-Catalytic Activity
   2.3.2   Controlling NADH levels
   2.3.3   Phosphocreatine, as a Competitive Inhibitor
   2.3.4   Metabolic Parameters in the Brain
2.4   Comparative Analysis
   2.4.1   Structure-Function of NAD+-Binding
   2.4.2   Sequence Homology
3. Compartmentation of GAPDH
3.1   Compartmentation of Glycolytic Energy
   3.1.1   Microzones of Cellular ATP
   3.1.2   Focal Regulation of NAD+/NADH Ratios   3.1.3   Channeling of Metabolites
   3.1.4   Non-Glycolytic Compartmentation
3.2   Binding to the Plasma Membrane
   3.2.1   SLC4 Anion Exchanger
      3.2.1.1   Band 3 in Erythrocytes
      3.2.1.2   Kidney AE1 Isoform
   3.2.2   Na+/K+-ATPase
   3.2.3   ATP-sensitive K+-Channel
   3.2.4   Glucose Transporters
      3.2.4.1   GLUT1 Transporter in Erythrocytes
      3.2.4.2   GLUT4 Transporter
   3.2.5   GABA (type A) Receptor
   3.2.6   GAPDH, as a Lactoferrin Receptor
3.3   Translocation to the Nucleus
3.4   Other Non-Cytosolic Destinations
   3.4.1   Clathrin-Coated Vesicles 
   3.4.2   Golgi Apparatus and Endoplasmic Reticulum 
   3.4.3   Sarcoplasmic Reticulum
   3.4.4   Mitochondria
3.5   Dendrites, Axons and Synapses
   3.5.1   Synaptic Vesicles
      3.5.1.1   Glutamate Uptake into Vesicles
   3.5.2   Post-Synaptic Density
3.6   Specialized Compartment for Spermatogenic GAPDH
4. Functional Diversity
4.1   Classical Example of Protein ‘Moonlighting’ 
   4.1.1   Evolutionary Considerations
   4.1.2   Molecular Mechanisms
4.2   Structural Organization of the Cell
   4.2.1   Cytoskeletal Components
      4.2.1.1   Actin Filaments
      4.2.1.2   Microtubules
   4.2.2   Organelle Biogenesis
      4.2.2.1   Triadic Junction
      4.2.2.2   Nuclear Envelope
      4.2.2.3   Vesicle Recycling/Membrane Fusion
      4.2.2.4   Cell Polarization
      4.2.2.5   Golgi and Endoplasmic Reticulum
   4.2.3   Autophagy
4.3   Transmission of Genetic Information
   4.3.1   RNA
      4.3.1.1   mRNA
      4.3.1.2   Polyribosomes      4.3.1.3   tRNA
      4.3.1.4   RNA viruses
   4.3.2   Gene Expression
   4.3.3   DNA Repair
 4.4   Signal Transduction Networks
   4.4.1   Nitric Oxide
   4.4.2   Unfolded Protein Response
   4.4.3   Peroxide Stress
   4.4.4   PI3K/Akt/mTOR Signaling
   4.4.5   Light and Dark Cycles
5. GAPDH, as a Virulence Factor
5.1   Surface-Localized GAPDH in Pathogenic Organisms
   5.1.1   Streptococcal Microorganisms
      5.1.1.1   Group A Streptococcus
      5.1.1.2   Other b-Hemolytic Streptococci
      5.1.1.3   a-Hemolytic Streptococci
   5.1.2   Mycoplasmas
   5.1.3   Candida albicans
5.2   GAPDH, as a Pathogenic Secretory Protein
5.3   Mining the Antigenic Properties of GAPDH
   5.3.1   In Search of a Vaccine for Mycoplasma bovis
   5.3.2   Tracking the Course of Candidiasis
5.4    Pathogenic Mechanisms o