Clark J I, Huang Q L
University of Washington, Seattle 98195-7420, USA.
Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15185-9. doi: 10.1073/pnas.93.26.15185.
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.
评估了泛硫乙胺、谷胱甘肽和选定化学试剂对α-晶状体蛋白抗聚集活性的影响。通过变性β-L-晶状体蛋白或乙醇脱氢酶（ADH）溶液的光散射监测蛋白质聚集。调整β-L-晶状体蛋白/α-晶状体蛋白和ADH/α-晶状体蛋白的比例，以便分别在60℃或37℃观察到蛋白质聚集的部分抑制，并且可以用选定的内源性代谢物轻松评估α-晶状体蛋白伴侣作用的调节。在β-L-晶状体蛋白测定中，泛硫乙胺增强抗聚集活性的作用最强，它似乎与α-晶状体蛋白相互作用。在ADH测定中，谷胱甘肽增强抗聚集活性的作用最强，它似乎与ADH相互作用。结果表明，常见代谢途径的产物可以调节α-晶状体蛋白对蛋白质聚集的伴侣样作用。
