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Originally published In Press as doi:10.1074/jbc.M111454200 on January 2, 2002

J. Biol. Chem., Vol. 277, Issue 12, 9806-9811, March 22, 2002
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Detection, Quantitation, Purification, and Identification of Cardiac Proteins S-Thiolated during Ischemia and Reperfusion*

Philip EatonDagger , Helen L. Byers§, Nicola Leeds§, Malcolm A. Ward§, and Michael J. Shattock

From the Centre for Cardiovascular Biology and Medicine, The Rayne Institute, St Thomas' Hospital, King's College London, SE1 7EH and § Proteome Sciences plc, South Wing Laboratory, Institute of Psychiatry, King's College London, Denmark Hill, SE5 8AF, United Kingdom

We have developed methods that allow detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. Cysteine was biotinylated and loaded into isolated rat hearts. During oxidative stress, biotin-cysteine forms a disulfide bond with reactive protein cysteines, and these can be detected by probing Western blots with streptavidin-horseradish peroxidase. S-Thiolated proteins were purified using streptavidin-agarose. Thus, we demonstrated that reperfusion and diamide treatment increased S-thiolation of a number of cardiac proteins by 3- and 10-fold, respectively. Dithiothreitol treatment of homogenates fully abolished the signals detected. Fractionation studies indicated that the modified proteins are located within the cytosol, membrane, and myofilament/cytoskeletal compartments of the cardiac cells. This shows that biotin-cysteine gains rapid and efficient intracellular access and acts as a probe for reactive protein cysteines in all cellular locations. Using Western blotting of affinity-purified proteins we identified actin, glyceraldehyde-3-phosphate dehydrogenase, HSP27, protein-tyrosine phosphatase 1B, protein kinase Calpha , and the small G-protein ras as substrates for S-thiolation during reperfusion of the ischemic rat heart. MALDI-TOF mass fingerprint analysis of tryptic peptides independently confirmed actin and glyceraldehyde-3-phosphate dehydrogenase S-thiolation during reperfusion. This approach has also shown that triosephosphate isomerase, aconitate hydratase, M-protein, nucleoside diphosphate kinase B, and myoglobin are S-thiolated during post-ischemic reperfusion.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 020-7928-9292 (ext. 2749); Fax: 020-7922-8139; E-mail: philip.eaton@kcl.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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