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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:40 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 2:36 p.m.) |
Indexed | 1 month, 3 weeks ago (July 2, 2025, 1:51 p.m.) |
Issued | 28 years, 8 months ago (Dec. 24, 1996) |
Published | 28 years, 8 months ago (Dec. 24, 1996) |
Published Online | 28 years, 8 months ago (Dec. 24, 1996) |
Published Print | 28 years, 8 months ago (Dec. 24, 1996) |
@article{Clark_1996, title={Modulation of the chaperone-like activity of bovine α-crystallin}, volume={93}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.93.26.15185}, DOI={10.1073/pnas.93.26.15185}, number={26}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Clark, John I. and Huang, Qing-ling}, year={1996}, month=dec, pages={15185–15189} }