Modulation of the chaperone-like activity of bovine alpha-crystallin.
The effects of pantethine, glutathione, and selected chemical reagents on the anti-aggregation activity of alpha-crystallin was evaluated. Protein aggregation was monitored by light scattering of solutions of denatured beta L-crystallin or alcohol dehydrogenase (ADH). The ratios of beta L-crystallin/alpha-crystallin and ADH/alpha-crystallin were adjusted so that partial inhibition of protein aggregation at 60 degrees C or 37 degrees C, respectively, was observed and modulation of the chaperone action of alpha-crystallin could be evaluated easily with selected endogenous metabolites. Enhancement of the anti-aggregation activity in the beta L-crystallin assay was strongest with pantethine, which appeared to interact with alpha-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 alpha-crystallin on protein aggregation.
Clark
J I
JI
University of Washington, Seattle 98195-7420, USA.
Huang
Q L
QL
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry* / Q000502:physiology*; D005978:Glutathione; D007700:Kinetics; D018832:Molecular Chaperones / Q000502:physiology*; D010204:Pantetheine / Q000031:analogs & derivatives; D011489:Protein Denaturation; D013997:Time Factors
D003459:Crystallins; D018832:Molecular Chaperones; D010204:Pantetheine; C005425:pantethine; D000426:Alcohol Dehydrogenase; D005978:Glutathione