Modulation of the chaperone-like activity of bovine α-crystallin
- 24 December 1996
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (26) , 15185-15189
- https://doi.org/10.1073/pnas.93.26.15185
Abstract
The effects of pantethine, glutathione, and selected chemical reagents on the anti-aggregation activity of α-crystallin was evaluated. Protein aggregation was monitored by light scattering of solutions of denatured β L -crystallin or alcohol dehydrogenase (ADH). The ratios of β L -crystallin/α-crystallin and ADH/α-crystallin were adjusted so that partial inhibition of protein aggregation at 60°C or 37°C, respectively, was observed and modulation of the chaperone action of α-crystallin could be evaluated easily with selected endogenous metabolites. Enhancement of the anti-aggregation activity in the β L -crystallin assay was strongest with pantethine, which appeared to interact with α-crystallin. Enhancement of the anti-aggregation activity in the ADH assay was strongest with glutathione which appeared to interact with ADH. The results indicated that the products of common metabolic pathways can modulate the chaperone-like effects of α-crystallin on protein aggregation.Keywords
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