Reversible S-glutathionylation of proteins is a focal point of redox signaling and cellular
defense against oxidative stress. This post-translational modification alters protein function,
and its reversal (deglutathionylation) is catalyzed specifically and efficiently by glutaredoxin
(GRx, thioltransferase), a thioldisulfide oxidoreductase. We hypothesized that changes in
glutaredoxin might be important in the development of diabetic retinopathy, a condition
characterized by oxidative stress. Indeed, GRx protein and activity were increased in retinal …