Boyle D, Takemoto L
Division of Biology, Kansas State University, Manhattan 66506.
Exp Eye Res. 1994 Jan;58(1):9-15. doi: 10.1006/exer.1994.1190.
Previous studies have demonstrated that in vitro, alpha-crystallin can protect other lens proteins against extensive denaturation and aggregation. The mechanism of this protection involves preferential binding of the partially denatured protein to a central region of the native alpha-crystallin complex. To test whether a similar phenomenon might occur in vivo, a high molecular weight aggregate (HMWA) fraction was isolated from the aged bovine lens. Negative staining of this preparation revealed the presence of particles of 13-14 nm diameter, characteristic of alpha-crystallin. Immunolocalization of the same particles using antiserum specific for gamma- and beta-crystallins demonstrated preferential binding of these crystallins to the central region of the alpha-crystallin complex. Together, these results provide evidence that in the intact lens, the alpha-crystallins are functionally important molecular chaperones.
以往的研究表明，在体外，α-晶状体蛋白可以保护其他晶状体蛋白不发生广泛的变性和聚集。这种保护机制涉及部分变性的蛋白质与天然α-晶状体蛋白复合物的中心区域优先结合。为了测试体内是否可能发生类似现象，从老年牛晶状体中分离出高分子量聚集体（HMWA）组分。对该制剂进行负染色显示存在直径为13-14nm的颗粒，这是α-晶状体蛋白的特征。使用针对γ-和β-晶状体蛋白的抗血清对相同颗粒进行免疫定位，结果表明这些晶状体蛋白优先结合到α-晶状体蛋白复合物的中心区域。这些结果共同提供了证据，表明在完整的晶状体中，α-晶状体蛋白是功能重要的分子伴侣。
