GAPDH: biological properties and diversity
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Dordrecht [u.a.]
Springer
2013
|
| Schriftenreihe: | Advances in experimental medicine and biology
985 |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XIV, 295 S. Ill., graph. Darst. |
| ISBN: | 9789400747159 9789400747166 |
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Datensatz im Suchindex
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|---|---|
| adam_text | Titel: GAPDH
Autor: Seidler, Norbert W
Jahr: 2013
Contents
Basic Biology of GAPDH............................................. 1
1.1 The GAPDH Gene.............................................. 2
1.1.1 Coding Region............................................ 4
1.1.2 Promoter Sequence......................................... 6
1.1.2.1 Hypoxia-Responsive Elements......................... 7
1.1.2.2 Basal Level Expression............................... 11
1.1.2.3 Glutamine-Responsive Elements........................ 11
1.1.3 Testes-Specific Isoform..................................... 12
1.1.4 GAPDH Pseudogenes....................................... 14
1.2 Regulation of GAPDH Expression................................... 15
1.2.1 Tissue Specificity.......................................... 15
1.2.2 Tracking GAPDH Information Electronically...................... 16
1.2.3 Cancer.................................................. 17
1.3 Cellular Levels of GAPDH........................................ 19
1.4 Oxidoreductase Activity of GAPDH.................................. 21
1.4.1 Mechanism of Catalysis..................................... 24
1.4.2 Kinetic Parameters......................................... 25
1.5 Architecture of the GAPDH Protein.................................. 27
1.5.1 Asymmetric Homotetramer................................... 28
1.5.2 Dinucleotide Binding Domain................................. 29
1.5.3 Catalytic Domain.......................................... 30
References........................................................ 32
GAPDH and Intermediary Metabolism.................................. 37
2.1 GAPDH, the Glycolytic Lynch-Pin.................................. 38
2.1.1 Metabolic Switch.......................................... 40
2.1.2 Glycolytic Tissues......................................... 41
2.1.3 Anaerobic Glycolysis....................................... 42
2.2 Determining GAPDH Activity...................................... 43
2.2.1 Chemical Inhibitors........................................ 43
2.2.2 Measurement of Glycolytic Flux............................... 44
2.2.3 Oxidoreductase Activity of GAPDH............................ 45
2.2.3.1 Conditions of Assay................................. 46
2.2.3.2 Assay Protocol..................................... 48
vi Contents
2.3 Role of GAPDH Metabolites....................................... 49
2.3.1 Counter-Catalytic Activity................................... 50
2.3.2 Controlling NADH Levels................................... 51
2.3.3 Phosphocreatine, as a Competitive Inhibitor....................... 52
2.3.4 Metabolic Parameters in the Brain.............................. 52
2.4 Comparative Analysis............................................ 53
2.4.1 Structure-Function of NAD+-Binding........................... 54
2.4.2 Sequence Homology........................................ 55
References........................................................ 56
3 Compartmentation of GAPDH........................................ 61
3.1 Compartmentation of Glycolytic Energy............................... 62
3.1.1 Microzones of Cellular ATP.................................. 62
3.1.2 Focal Regulation of NAD+/NADH Ratios........................ 65
3.1.3 Channeling of Metabolites................................... 65
3.1.4 Non-glycolytic Compartmentation.............................. 67
3.2 Binding to the Plasma Membrane.................................... 67
3.2.1 SLC4 Anion Exchanger..................................... 69
3.2.1.1 Band 3 in Erythrocytes............................... 70
3.2.1.2 Kidney AE1 Isoform................................. 72
3.2.2 Na+/K+-ATPase........................................... 73
3.2.3 ATP-Sensitive K+-Channel................................... 74
3.2.4 GLUT Transporters........................................ 75
3.2.4.1 GLUTI Transporter in Erythrocytes..................... 76
3.2.4.2 GLUT4 Transporter................................. 77
3.2.5 GABA (Type A) Receptor................................... 78
3.2.6 GAPDH, as a Lactoferrin Receptor............................. 78
3.3 Translocation to the Nucleus....................................... 79
3.4 Other Non-cytosolic Destinations.................................... 83
3.4.1 Clathrin-Coated Vesicles.................................... 83
3.4.2 Golgi Apparatus and Endoplasmic Reticulum..................... 84
3.4.3 Sarcoplasmic Reticulum..................................... 85
3.4.4 Mitochondria............................................. 87
3.5 Dendrites, Axons and Synapses..................................... 88
3.5.1 Synaptic Vesicles.......................................... 89
3.5.2 Post-synaptic Density....................................... 90
3.6 Specialized Compartment for Spermatogenic GAPDH..................... 91
References........................................................ 94
4 Functional Diversity................................................ 103
4.1 Classical Example of Protein Moonlighting ........................... 104
4.1.1 Evolutionary Considerations.................................. 104
4.1.2 Molecular Mechanisms...................................... 105
4.2 Structural Organization of the Cell................................... 107
4.2.1 Cytoskeletal Components.................................... 107
4.2.1.1 Actin Filaments.................................... 107
4.2.1.2 Microtubules...................................... Ill
4.2.2 Organelle Biogenesis....................................... 118
4.2.2.1 Triadic Junction.................................... 118
4.2.2.2 Nuclear Envelope................................... 118
Contents
4.2.2.3 Vesicle Recycling/Membrane Fusion..................... 120
4.2.2.4 Cell Polarization.................................... 121
4.2.2.5 Golgi and Endoplasmic Reticulum....................... 122
4.2.3 Autophagy............................................... 123
4.3 Transmission of Genetic Information................................. 124
4.3.1 RNA................................................... 125
4.3.1.1 mRNA........................................... 126
4.3.1.2 Polyribosomes..................................... 129
4.3.1.3 tRNA............................................ 130
4.3.1.4 RNA Viruses...................................... 130
4.3.2 Gene Expression.......................................... 131
4.3.3 DNA Repair.............................................. 134
4.4 Signal Transduction Networks...................................... 134
4.4.1 Nitric Oxide.............................................. 135
4.4.2 Unfolded Protein Response................................... 138
4.4.3 Peroxide Stress............................................ 138
4.4.4 PI3K/Akt/mTOR Signaling................................... 139
4.4.5 Light and Dark Events...................................... 140
References........................................................ 141
GAPDH, as a Virulence Factor........................................ 149
5.1 Surface-Localized GAPDH in Pathogenic Organisms..................... 150
5.1.1 Streptococcal Microorganisms................................ 150
5.1.1.1 Group A Streptococcus............................... 151
5.1.1.2 Other ß-Hemolytic Streptococci........................ 153
5.1.1.3 a-Hemolytic Streptococci............................. 154
5.1.2 Mycoplasmas............................................. 155
5.1.3 Candida albicans.......................................... 157
5.2 GAPDH: A Pathogenic Secretory Protein.............................. 159
5.3 Mining the Antigenic Properties of GAPDH............................ 161
5.3.1 In Search of a Vaccine for Mycoplasma bovis..................... 161
5.3.2 Tracking the Course of Candidiasis............................. 162
5.4 Pathogenic Mechanisms of Action................................... 163
5.4.1 Molecular Mimicry and Immune Modulation...................... 164
5.4.2 Virulence Maintenance...................................... 166
5.4.3 Phagocytic Strategy........................................ 166
5.4.4 Pathogenic Receptor for Host Plasminogen....................... 169
5.4.5 Adhesive Functions in Pathogen-Host Interaction................... 173
5.4.6 Viral Mechanisms......................................... 173
References........................................................ 175
Target for Diverse Chemical Modifications............................... 179
6.1 Post-Translational Protein Modification............................... 180
6.1.1 GAPDH Isozymes......................................... 180
6.1.1.1 Early Investigations................................. 180
6.1.2 Current Observations....................................... 181
6.1.2.1 Organisms with GAPDH Isozymes...................... 183
6.1.3 Auto-Catalytic Processes.................................... 183
6.1.4 Enzymatic Modifications of GAPDH............................ 184
Contents
6.2 Susceptibility to Stochastic Chemical Modification....................... 187
6.2.1 Oxidation of Active Site Cysteine.............................. 188
6.2.1.1 Disulfide Bond Formation............................. 188
6.2.1.2 Sulfhydryl to Sulfenic Acid............................ 190
6.2.2 Succination of Active Site Cysteine............................. 190
6.2.3 Nitration................................................ 191
6.2.4 Glycation................................................ 192
6.2.5 Lipid Peroxidative Byproducts................................ 194
6.2.6 S-Sulfhydration........................................... 195
6.3 Proposed Models for Cellular Decline................................ 196
6.3.1 Blocking Cellular Chaperonins................................ 197
6.3.2 Dehydration Model........................................ 198
6.4 Proposed Models for Cell Survival................................... 199
6.4.1 New and Old Perspectives................................... 199
6.4.1.1 Continuity in Cell Function............................ 199
6.4.1.2 Linkage to Energy Metabolism......................... 199
6.4.1.3 Sensor of Chemical Stressors.......................... 200
6.4.2 S-Thiolation of GAPDH..................................... 200
6.4.3 ISGylation............................................... 201
References........................................................ 203
Dynamic Oligomeric Properties........................................ 207
7.1 Factors Affecting Stability......................................... 208
7.1.1 Cooperativity............................................. 209
7.1.2 Temperature.............................................. 215
7.1.2.1 Testing Anti-Aggregation Agents....................... 217
7.1.2.2 Folding Accessory Proteins............................ 219
7.1.3 Chemical Dénaturants....................................... 221
7.2 Factors Affecting Oligomerization................................... 225
7.2.1 Storage (In Vitro Aging)..................................... 226
7.2.2 Chemical Modification...................................... 227
7.2.2.1 Maleylation....................................... 228
7.2.2.2 Acetylation....................................... 228
7.2.2.3 Pyridoxal Phosphate................................. 229
7.2.2.4 Carbamylation..................................... 229
7.2.2.5 Succinic Anhydride................................. 229
7.2.2.6 Cross-Linking Agents................................ 230
7.2.3 Substrates and Coenzymes................................... 231
7.2.4 Chloride Ions............................................. 232
7.2.5 Adenine Nucleotides....................................... 234
7.3 Comparative Analysis............................................ 237
7.3.1 Tetrameric Hybrids........................................ 238
7.3.2 Adenosine Binding Site..................................... 238
7.4 Domain Exchange............................................... 239
7.4.1 Human Serum Albumin as a Model............................. 239
7.4.2 Other Model Proteins....................................... 240
7.4.3 Proposed Oligomeric Dynamics of GAPDH....................... 240
References........................................................ 242
Contents x
8 Multiple Binding Partners............................................ 249
8.1 The Interactome................................................ 250
8.1.1 Emerging Mechanisms...................................... 252
8.1.2 Role of Acidic Dipeptide Sequences............................ 253
8.1.3 Criteria for Interactive Partner................................. 253
8.1.4 Glycolytic Interactome...................................... 254
8.2 Proteins Associated with Neurodegenerative Diseases...................• ¦ 256
8.2.1 Alzheimers Disease: Amyloid-ß Peptide and Tau................... 257
8.2.2 Parkinsons Disease: a-Synuclein............................... 258
8.2.3 Proteins with Tracts of Polyglutamine Repeats..................... 259
8.2.4 Cataracts................................................ 260
8.3 Multiple Catalytic Functions....................................... 261
8.3.1 Peroxidase Activity........................................ 261
8.3.2 S-Nitrosylase Activity...................................... 262
8.3.3 Kinase Activity........................................... 262
8.3.4 ADP-Ribosylase Activity.................................... 263
References........................................................ 264
9 GAPDH in Anesthesia............................................... 269
9.1 Is Anesthesia Mediated by GAPDH?................................. 269
9.1.1 GABAA Receptor.......................................... 271
9.1.2 GAPDH Regulates GABAA Receptor........................... 272
9.1.3 Proposed Mechanism of Action of Inhaled Anesthetics............... 276
9.2 Binding of Inhaled Anesthetics..................................... 277
9.2.1 Anesthetic Binding Site..................................... 278
9.2.2 Human Serum Albumin as a Model Protein....................... 279
9.2.3 Other Model Proteins....................................... 280
9.2.4 Adenine Metabolites........................................ 280
9.3 GAPDH and Isoflurane Preconditioning............................... 282
9.3.1 The Phenomenon of Anesthetic Preconditioning.................... 283
9.3.2 Dehydration-Induced Protein Misfolding......................... 285
References........................................................ 287
Index............................................................... 293
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| spelling | Seidler, Norbert W. Verfasser aut GAPDH biological properties and diversity Norbert W. Seidler Dordrecht [u.a.] Springer 2013 XIV, 295 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Advances in experimental medicine and biology 985 Advances in experimental medicine and biology 985 (DE-604)BV000003102 985 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025270608&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Seidler, Norbert W. GAPDH biological properties and diversity Advances in experimental medicine and biology |
| title | GAPDH biological properties and diversity |
| title_auth | GAPDH biological properties and diversity |
| title_exact_search | GAPDH biological properties and diversity |
| title_full | GAPDH biological properties and diversity Norbert W. Seidler |
| title_fullStr | GAPDH biological properties and diversity Norbert W. Seidler |
| title_full_unstemmed | GAPDH biological properties and diversity Norbert W. Seidler |
| title_short | GAPDH |
| title_sort | gapdh biological properties and diversity |
| title_sub | biological properties and diversity |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025270608&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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