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GAPDH: Biological Properties and Diversity

  • Norbert W. Seidler

Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 985)

Table of contents

  1. Front Matter
    Pages i-xiv
  2. Norbert W. Seidler
    Pages 1-36
  3. Norbert W. Seidler
    Pages 37-59
  4. Norbert W. Seidler
    Pages 61-101
  5. Norbert W. Seidler
    Pages 103-147
  6. Norbert W. Seidler
    Pages 149-178
  7. Norbert W. Seidler
    Pages 179-206
  8. Norbert W. Seidler
    Pages 207-247
  9. Norbert W. Seidler
    Pages 249-267
  10. Norbert W. Seidler
    Pages 269-291
  11. Back Matter
    Pages 293-295

About this book

Introduction

GAPDH (glyceraldehyde 3-phosphate dehydrogenase) is more than just a glycolytic enzyme. An unprecedented amount of literature demonstrates that GAPDH has an astounding multiplicity of function. This diversity is not simply due to cell compartmentation (i.e. redistributing glycolytic energy to where it is needed), although this feature is undoubtedly important and discussed in the book. GAPDH integrates glycolysis with other cellular processes. This concept of integration cannot be understated. But, there is more.

GAPDH actively participates in numerous non-glycolytic cellular events that fall into very broad categories including the cell infrastructure and the transmission of genetic information. Some of GAPDH’s biological properties are completely non-intuitive given the current undergraduate textbook understanding of this glycolytic enzyme. For example, GAPDH binds to select phospholipids and catalyzes organelle biogenesis. It has fusogenic properties, enabling it to be actively involved in nuclear envelop reassembly, autophagy and membrane trafficking. Human macrophages exhibit surface-localized GAPDH with receptor function. As scientists, we are trained to consider GAPDH as a soluble cytosolic dehydrogenase enzyme. The literature observations - as described in this book - tell us something quite different. Besides oxidoreductase activity, GAPDH exhibits peroxidase, uracil DNA glycosylase, nitrosylase, mono-ADP-ribosylase, esterase and phosphotransferase activity. GAPDH binds membrane transport proteins, G-proteins, poly-nucleotides, adenines, specific lipids, select carbohydrates, cytoskeletal proteins, nuclear import and export proteins, diverse ATPases, molecular chaperones and other molecules.

Keywords

apoptosis cancer glyceraldehyde 3-phosphate dehydrogenase inhaled anesthetics neurodegeneration

Authors and affiliations

  • Norbert W. Seidler
    • 1
  1. 1.and Biosciences, Department of BiochemistryKansas City University of MedicineKansas CityUSA

Bibliographic information

  • DOI https://doi.org/10.1007/978-94-007-4716-6
  • Copyright Information Springer Science+Business Media Dordrecht 2013
  • Publisher Name Springer, Dordrecht
  • eBook Packages Biomedical and Life Sciences
  • Print ISBN 978-94-007-4715-9
  • Online ISBN 978-94-007-4716-6
  • Series Print ISSN 0065-2598
  • Buy this book on publisher's site
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