alpha-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract.
作者： M.J. Kelley , L.L. David , N. Iwasaki , J. Wright , T.R. Shearer
DOI: 10.1016/S0021-9258(17)46704-4
关键词:
摘要: This study reports the first demonstration of a marked reduction in alpha-crystallin chaperone activity an experimental model cataract, and implicates activation cysteine protease calpain II (EC 3.4.22.17) as vivo responsible for decreased activity. Chaperone normal from lenses young rats was assayed by measuring attenuation heat-induced aggregation scattering beta L-crystallin. alpha-Crystallin nucleus with selenite cataract showed specific selective proteolysis, diminished. Proteolysis mimicked incubating II, this also resulted loss Two-dimensional gel electrophoresis peptide mapping were used to identify four partially degraded alpha A- B-crystallin polypeptides following incubation calpain. Similar A B found cataract. Previous experiments indicated that decreases because removal COOH terminus. Our support observation suggest proteolysis at terminus may result
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