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Reversal Of Protein S-Glutathiolation By Glutaredoxin In The Retinal Pigment Epithelium., Yuh-Cherng Chai, George Hoppe, Jonathan Sears

Yuh-Cherng Chai

Protein cysteines can serve both sensory and activation roles in the regulation of protein function. The modulation of mixed disulfides with glutathione may promise to be a broad mechanism of redox signalling. Using both protein extract and intact RPE cells, we have generated covalent adduction of glutathione to protein cysteines and further show that glutaredoxin (Grx-1) is able to remove glutathione from protein S-glutathiolated substrates. Our data demonstrate that glutathione can modify a wide range of RPE proteins in intact cells, but that the reversal of this process–deglutathiolation and thiol bond restoration–may require a specific catalytic reaction with glutaredoxin. More …