頁籤選單縮合
題 名 | Physiological Role of the Association Complexes of α-Crystallin and Its Substrates on the Chaperone Activity |
---|---|
作 者 | Lee,Jiahn-shing; Samejima,Tatsuya; Liao,Jiahn-haur; Wu,Shih-hsiung; Chiou,Shyh-horng; | 書刊名 | 中央研究院生物化學研究所論文集 |
卷 期 | 24 1998[民87.] |
頁 次 | 頁83-88 |
分類號 | 361.19 |
關鍵詞 | α-crystallin; |
語 文 | 英文(English) |
英文摘要 | Previous reports on the chaperone activity of α-crystallin to prevent protein denaturation and thermal aggregation have suggested that partially denatured proteins can bind α -crystallin in its central region. Likewise, β - and γ -crystallin can also be localized to the central cavity of α-crystallin particle in vivo, which provides indirect evidence that α-crystallin can function as a chaperone in the intact lens. In this study, we have further demonstrated that the binding of the substrate proteins to α-crystallin by short-term preincubation may mimic the in vivo conditions of crystallin association. Preheating of a-crystallin with its substrate proteins at 60℃ for 20 min resulted in the formation of stable complexes between α-crystallin and its substrates (8.0% of insulin or 5.3% of γ -crystallin was involved in complex formation). Under such conditions, the chaperone activity of α -crystallin to inhibit dithiothreitol-, ultraviolet-, or oxidation-induced protein aggregation can be greatly enhanced. Since UVirradiation and oxidative stress are common insults to eye lenses under normal physiological conditions, the presence of (α / γ and α / β complex in vivo may play an important role to maintain the lens in a transparent State. |
本系統中英文摘要資訊取自各篇刊載內容。