The effect of glutathione upon chaperone activity of alpha-crystallin is probably mediated through target modulation.

We studied the effect of the presence of glutathione, both reduced (GSH) and oxidized (GSSG), on the chaperone activity of alpha-crystallin towards thermal aggregation of gamma 2-crystallin. Results showed that while GSH enhanced the chaperone activity of alpha-crystallin, GSSG appeared to diminish it to some extent. When, however, the effect of the presence of glutathione was studied in the absence of alpha-crystallin, the nature of their action was found to be almost similar to that observed in its presence. These results suggest that glutathiones probably modulate the target protein which ultimately influences the chaperone activity of alpha-crystallin.