α-晶状体蛋白可作为分子伴侣发挥作用。
Alpha-crystallin can function as a molecular chaperone.
作者信息
Horwitz J
机构信息
Jules Stein Eye Institute, University of California, Los Angeles School of Medicine 90024-7008.
出版信息
Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10449-53. doi: 10.1073/pnas.89.21.10449.
The alpha-crystallins (alpha A and alpha B) are major lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. In addition, crystallins (especially alpha B) are found in many cells and organs outside the lens, and alpha B is overexpressed in several neurological disorders and in cell lines under stress conditions. Here I show that alpha-crystallin can function as a molecular chaperone. Stoichiometric amounts of alpha A and alpha B suppress thermally induced aggregation of various enzymes. In particular, alpha-crystallin is very efficient in suppressing the thermally induced aggregation of beta- and gamma-crystallins, the two other major mammalian structural lens proteins. alpha-Crystallin was also effective in preventing aggregation and in refolding guanidine hydrochloride-denatured gamma-crystallin, as judged by circular dichroism spectroscopy. My results thus indicate that alpha-crystallin refracts light and protects proteins from aggregation in the transparent eye lens and that in nonlens cells alpha-crystallin may have other functions in addition to its capacity to suppress aggregation of proteins.
α-晶状体蛋白（αA和αB）是脊椎动物眼睛中主要的晶状体结构蛋白，与小分子热休克蛋白家族相关。此外，晶状体蛋白（尤其是αB）在晶状体以外的许多细胞和器官中也有发现，并且在几种神经疾病以及应激条件下的细胞系中αB会过度表达。在此我表明α-晶状体蛋白可以作为分子伴侣发挥作用。化学计量的αA和αB可抑制各种酶的热诱导聚集。特别地，α-晶状体蛋白在抑制β-和γ-晶状体蛋白（另外两种主要的哺乳动物晶状体结构蛋白）的热诱导聚集方面非常有效。通过圆二色光谱法判断，α-晶状体蛋白在防止聚集以及使盐酸胍变性的γ-晶状体蛋白复性方面也很有效。因此我的结果表明，α-晶状体蛋白在透明的晶状体中折射光线并保护蛋白质免于聚集，并且在非晶状体细胞中，α-晶状体蛋白除了具有抑制蛋白质聚集的能力外可能还有其他功能。
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