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Papers In Press, published online ahead of print January 2, 2002
The Centre for Cardiovascular Research and Medicine, Kings College London, London SE1 7EH
Corresponding Author: philip.eaton{at}kcl.ac.uk
We have developed methods that allowed 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, the biotin-cysteine forms a disulfide bond with reactive protein cysteines and these can be detected by probing Western blots with streptavidin-HRP. 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-fold and 10-fold respectively. DTT-treatment of homogenates fully abolished the signals detected. Fractionation studies showed the modified proteins are located within the cytosol, membrane and myofilament/cytoskeletal compartments of the cardiac cells. This shows the biotin-cysteine gains rapid and efficient intracellular access and acts a probe for reactive protein cysteines in all cellular locations. Using Western blotting of affinity purified proteins, we identified actin, GAPDH, HSP27, protein-tyrosine phosphatase 1B, protein kinase C
J. Biol. Chem, 10.1074/jbc.M111454200
Submitted on November 30, 2001
Revised on December 20, 2001
Accepted on January 2, 2002
Detection, quantitation, purification and identification of cardiac proteins S-thiolated during ischemia and reperfusion
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 GAPDH S-thiolation during reperfusion. This approach has also showed triosephosphate isomerase, aconitate hydratase, M-protein, nucleoside diphosphate kinase B and myoglobin are S-thiolated during post-ischemic reperfusion.
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