Advanced glycation end products in human senile and diabetic cataractous lenses.
Advanced glycation end products in human senile and diabetic cataractous lenses.
复制标题
人类老年和糖尿病白内障晶状体中的高级糖基化终产物。
DOI：
10.1023/a:1007015416572
复制
发表时间：
2000
影响因子：
4.3
通讯作者：
Abraham,EC
中科院分区：
文献类型：
--
作者：
Zarina,S;Zhao,HR;Abraham,EC
作者从人类老年性、糖尿病性白内障晶状体和年龄匹配的透明晶状体中制备了晶状体蛋白的水溶性（WSF）、脲溶（USF）、碱溶（ASF）、超声溶（SF）、超声不溶（SIF）和膜溶（MF）组分。通过非竞争性和竞争性酶联免疫吸附试验（ELISA）测定糖基化终末产物（AGEs）的水平，包括糖基化产物羧甲基赖氨酸（CML）。通过SDS-PAGE和Western blotting确定AGEs在各蛋白组分中的分布。与老年性白内障晶状体和透明晶状体相比，糖尿病性白内障晶状体中AGEs水平总体上有所增加。ASF和SF均来源于尿素不溶性部分，其AGEs含量最高。然而，CML水平在透明晶状体和老年性和糖尿病性白内障晶状体中没有明显的差异。在所有馏分中，AGEs主要分布在高分子团聚体中。这些数据表明，AGEs有助于蛋白质聚集和随后的不溶化。
The authors prepared water-soluble (WSF), urea-soluble (USF), alkali-soluble (ASF), sonicated (SF), sonicated insoluble (SIF) and membrane (MF) fractions of lens proteins from human senile and diabetic cataractous lenses and age-matched clear lenses. Levels of advanced glycation end products (AGEs) including carboxymethyl lysine (CML), a glycoxidation product, were determined by both non-competitive and competitive enzyme-linked immunosorbent assay (ELISA). Distribution of AGEs in the various protein fractions was ascertained by SDS-PAGE and Western blotting. An overall increase in the levels of AGEs in diabetic cataractous lenses as compared to senile cataractous lenses and clear lenses has been observed. ASF and SF , both of which originated from the urea-insoluble fraction, showed the highest levels of AGEs. However, no clear-cut differences in CML levels were seen among clear lenses and senile and diabetic cataractous lenses. AGEs were found to be distributed mostly in the high molecular aggregates in all the fractions. These data suggest that AGEs contribute to protein aggregation and subsequent insolubilization.