老化过程中α-晶体蛋白分子伴侣活性的变化  

Change of α-Crystallin Acting as Molecular Chaperone Activity with Ageing

作　　者：严宏[1] 惠延年[2] 范建国[3] 王为农[1] 

机构地区：[1]第四军医大学唐都医院眼科,西安710038 [2]第四军医大学西京医院眼科,西安710032 [3]北京军区总医院眼科,北京100700

出　　处：《Eye Science》2003年第4期239-243,共5页眼科学报（英文版）

基　　金：中国人民解放军总后勤部留学回国人员基金(No:97H26)

摘　　要：目的:研究老化过程中α-晶体蛋白的分子伴侣功能。 方法:使用Sephacryl S-300HR分离幼年、中年和老年兔晶状体皮质和核α-晶体蛋白。测定α-晶体蛋白对加热(60℃)诱导过氧化氢酶(catalase,CAT)和β_L-晶体蛋白凝聚,果糖(37℃)和加热(60℃)诱导CAT失活的保护作用。 结果:四种评估伴侣功能的方法有类似的结果。不同年龄兔晶状体皮质α-晶体蛋白的保护作用较核强,α_H-晶体蛋白的伴侣功能均较α_L-晶体蛋白降低;随着老化晶状体皮质α_H-和α_L-晶体蛋白的伴侣功能无显著性降低,但核α_L-晶体蛋白伴侣功能的降低具有显著性。 结论:晶状体核α-晶体蛋白年龄依赖性伴侣功能的降低,可以参与老年性白内障的形成。眼科学报 2003;19:239-243。Purpose :To evaluate the molecular chaperone function of α-crystallin with ageing. Mehods:α-Crystallin of newborn,adult and old rabbits lenses in both of cortex and nucleus were separated by chromatography on Sephacryl S-300HR.The protection of α- crystallin against thermal aggregation of catalase and β_L-crystallin (60℃),inactivation of catalase by fructose(37℃)and heat stress(60℃)were measured spectrophotometrically. Results:Protection of α-crystallin against aggregation and inactivation using four methods showed a similar pattern.The protective ability in cortex was greatly higher than in nucleus of different-aged lenses,and α_H-crystallin was less than α_L-crystallin in both cortex and nucleus.There was no statistically decrease with age of chaperone function of both α_H-crystallin and α_L-crystallin in the cortex,whereas α_L-crystallin in the nucleus was compromised. Conclusion:α-Crystallin in the nucleus shows age-related decrease in chaperone function,which may be responsible for cataract formation. Eye Science 2003;19:239-243.

关 键 词：Α-晶体蛋白 分子伴侣 老化 过氧化氢酶 老年性白内障 

分 类 号：R776[医药卫生—眼科]