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Am J Physiol Cell Physiol 287: C246-C256, 2004; doi:10.1152/ajpcell.00516.2003
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INVITED REVIEW

Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers

Henry Jay Forman,1 Jon M. Fukuto,2 and Martine Torres3,4

1School of Natural Sciences, University of California, Merced 95344; 2Department of Pharmacology, University of California, Los Angeles 90095; 3The Saban Research Institute of Childrens Hospital Los Angeles and 4Department of Pediatrics, Keck School of Medicine, University of Southern California, Los Angeles, California 90027

Submitted 19 November 2003 ; accepted in final form 13 January 2004

Except for the role of NO in the activation of guanylate cyclase, which is well established, the involvement of reactive oxygen species (ROS) and reactive nitrogen species (RNS) in signal transduction remains controversial, despite a large body of evidence suggestive of their participation in a variety of signaling pathways. Several problems have limited their acceptance as signaling molecules, with the major one being the difficulty in identifying the specific targets for each pathway and the chemical reactions supporting reversible oxidation of these signaling components, consistent with a second messenger role for ROS and RNS. Nevertheless, it has become clear that cysteine residues in the thiolate (i.e., ionized) form that are found in some proteins can be specific targets for reaction with H2O2 and RNS. This review focuses on the chemistry of the reversible oxidation of those thiolates, with a particular emphasis on the critical thiolate found in protein tyrosine phosphatases as an example.

hydrogen peroxide; thiolate; nitrosothiol; nitric oxide; signal transduction


Address for reprint requests and other correspondence: H. J. Forman, School of Natural Sciences, Univ. of California, Merced, PO Box 2039, Merced, CA 95344 (E-mail: hforman{at}ucmerced.edu).




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