Emerging mechanisms of glutathione-dependent chemistry in biology and disease.

Y.M. Janssen-Heininger, J.D. Nolin, S.M. Hoffman, A.L.J. van der Velden, J. E. Tully, K.G. Lahue, S.T. Abdalla, D.G. Chapman, N.L. Reynaert, A. van der Vliet, V. Anathy

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease. J. Cell. Biochem. 114: 1962-1968, 2013. 

Original languageEnglish
Pages (from-to)1962-1968
Number of pages7
JournalJournal of Cellular Biochemistry
Volume114
Issue number9
DOIs
Publication statusPublished - Sep 2013

Keywords

  • GLUTAREDOXIN-1
  • PROTEIN S-GLUTATHIONYLATION
  • REDOX
  • BIOTIN SWITCH
  • DISULFIDE BOND FORMATION
  • REDOX-BASED REGULATION
  • ENDOPLASMIC-RETICULUM
  • SIGNAL-TRANSDUCTION
  • CYSTEINE DERIVATIZATION
  • MOLECULAR-MECHANISMS
  • PEROXIREDOXIN
  • APOPTOSIS

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