TEMPERATURE-DEPENDENT CHAPERONE-LIKE ACTIVITY OF ALPHA-CRYSTALLIN

被引:150
作者
RAMAN, B [1 ]
RAMAKRISHNA, T [1 ]
RAO, CM [1 ]
机构
[1] CTR CELLULAR & MOLEC BIOL,HYDERABAD 500007,ANDHRA PRADESH,INDIA
关键词
CHAPERONE; AGGREGATION; INSULIN; ALPHA-CRYSTALLIN; ZETA-CRYSTALLIN;
D O I
10.1016/0014-5793(95)00440-K
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Alpha-crystallin, a multimeric protein present in the eye lens, is known to have chaperone-like activity in preventing the aggregation of enzymes and other crystallins. We have studied the chaperone-like activity of this protein towards the aggregation of insulin B chain, induced by reducing the interchain disulphide bond with dithiothreitol. At room temperature, there is no detectable protection (at a 1:1 (w/w) ratio of insulin: alpha-crystallin) against the aggregation of insulin B chain by alpha-crystallin, whereas it completely prevents this aggregation at 40 degrees C, We have monitored the temperature dependence of the protection of aggregation by alpha-crystallin; the protection increases sharply above 30 degrees C and reaches almost 100% by 41 degrees C, Probing the hydrophobic surfaces of alpha-crystallin with the hydrophobic fluorphore 8-anilino-1 naphthalene sulfonate suggests that the hydrophobic surfaces of alpha-crystallin are exposed to a greater extent above 30 degrees C, A complete prevention of the aggregation is achieved at 27.6 degrees C by increasing the concentration of alpha-crystallin by more than 8 fold, Similar temperature dependent chaperone-like activity of alpha-crystallin is observed towards the aggregation of zeta-crystallin, an enzyme crystallin from guinea pig, We have earlier shown that alpha-crystallin exposes hydrophobic surface(s) at temperatures above 30 degrees C, These results support our earlier hypothesis [Raman, B. and Rao, Ch.M. (1994) J. Biol, Chem, 269, 27264-27268] that the chaperone-like activity of alpha-crystallin is more pronounced in its structurally perturbed state.
引用
收藏
页码:133 / 136
页数:4
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