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Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH)
The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease
Provides key insights into GAPDH from a world-expert with detailed exposition on post-translational modification
Michael A. Sirover (Author)
9780128098523
Paperback, published 25 May 2017
324 pages
22.9 x 15.1 x 2.1 cm, 0.52 kg
Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease examines the biochemical protein interactions of the multi-dimensional protein GAPDH, further considering the regulatory mechanisms through which cells control their functional diversity. This protein’s diverse activities range from nuclear tRNA export and the maintenance of genomic integrity, to cytoplasmic post-transcriptional control of gene expression and receptor mediated cell signaling, to membrane facilitation of iron metabolism, trafficking and fusion. This book will be of great interest to basic scientists, clinicians and students, including molecular and cell biologists, immunologists, pathologists and clinical researchers who are interested in the biochemistry of GAPDH in health and disease.
Section I. Moonlighting GAPDH in Normal Cell Function1. Transcriptional Expression2. Post-translational mRNA Regulation3. Iron Metabolism4. Membrane Trafficking5. Maintenance of DNA Integrity6. GAPDH and Neural Transmission7. GAPDH and Cell Proliferation Section II. Physiological Stress and GAPDH Functional Diversity1. GAPDH and Oxidative Stress: Nitric Oxide, apoptosis and heme metabolism2. GAPDH and Hypoxia3. GAPDH and Ischemia. Ischemia may be defined as a restriction in blood supply to tissues resulting in oxygen deprivation. Recent studies indicate that moonlighting GAPDH may be specifically regulated as a function of ischemic stress. This includes its role in receptor mediated glutamate exocytosis and its intracellular interaction with the p53 protein. The former regulates AMPAR action while the latter involves the formation of a GAPDH:p53 protein-protein complex as well as post-translational modification of the p53 protein. Section III. The Pathology of GAPDH Functional Diversity1. GAPDH and Age-Related Neurodegenerative Disease2. Moonlighting GAPDH and Cancer Development3. Functional Diversity of GAPDH in Infection and Immunity Section IV. The Pharmacology of Moonlighting GAPDH Section V. Discussion
Subject Areas: Biochemistry [PSB]
