Chapter 18. Compartmentation of Redox Signaling and Control: Discrimination of Oxidative Stress in Mitochondria, Cytoplasm, Nuclei, and Endoplasmic Reticulum

  1. James A. Dykens6,
  2. Yvonne Will7
  1. Patrick J. Halvey1,2,
  2. Jason M. Hansen3,
  3. Lawrence H. Lash4,
  4. Dean P. Jones5

Published Online: 22 JAN 2008

DOI: 10.1002/9780470372531.ch18

Book Title

Drug-Induced Mitochondrial Dysfunction

Drug-Induced Mitochondrial Dysfunction

Additional Information

How to Cite

Halvey, P. J., Hansen, J. M., Lash, L. H. and Jones, D. P. (2008) Compartmentation of Redox Signaling and Control: Discrimination of Oxidative Stress in Mitochondria, Cytoplasm, Nuclei, and Endoplasmic Reticulum, in Drug-Induced Mitochondrial Dysfunction (eds J. A. Dykens and Y. Will), John Wiley & Sons, Inc., Hoboken, NJ, USA. doi: 10.1002/9780470372531.ch18

Editor Information

  1. 6

    Pfizer, Inc., Sandwich, UK

  2. 7

    Pfizer, Inc., Groton, Connecticut, USA

Author Information

  1. 1

    Department of Pediatrics, and Division of Pulmonary, Allergy and Critical Care Medicine, Department of Medicine, Emory University, Atlanta, Georgia

  2. 2

    Department of Biochemistry and National Centre for Biomedical Engineering Science, National University of Ireland, Galway, Ireland

  3. 3

    Department of Pediatrics, Emory University, Atlanta, Georgia

  4. 4

    Department of Pharmacology, Wayne State University School of Medicine, Detroit, Michigan, USA

  5. 5

    Division of Pulmonary, Allergy and Critical Care Medicine, Department of Medicine, Emory University, Atlanta, Georgia

Publication History

  1. Published Online: 22 JAN 2008
  2. Published Print: 14 SEP 2008

ISBN Information

Print ISBN: 9780470111314

Online ISBN: 9780470372531

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Keywords:

  • redox signaling and control compartmentation;
  • mitochondrial thioredoxin and peroxiredoxin systems;
  • redox signaling processes and GSH/GSSG, Trx, Prx

Summary

This chapter contains sections titled:

  • Introduction

  • Mitochondrial oxidative stress and protective thiol–disulfide systems

  • Sources of ROS in the mitochondria

  • Mitochondrial GSH and GSH-dependent systems

  • Mitochondrial thioredoxin and peroxiredoxin systems

  • Non-thiol-based mitochondrial antioxidants

  • Proteomic techniques for identification of oxidatively modified proteins

  • Fluorescent probes for detection of mitochondrial ROS

  • Compartmentation in redox signaling and control in the nucleus and cytoplasm

  • Oxidative protein folding and redox signaling events in the endoplasmic reticulum

  • Conclusions and future perspectives

  • References

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