Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry
Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry
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DOI：
10.1006/exer.1998.0481
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发表时间：
1998-07-01
影响因子：
3.4
通讯作者：
David, LL
中科院分区：
文献类型：
--
作者：
Lampi, KJ;Ma, ZX;David, LL
本研究的目的是鉴定成人晶状体中的主要蛋白质组分，并利用双向电泳法、Edman测序法，结合随附的手稿中的数据-质谱仪，分析这些蛋白质随年龄的具体变化。晶状体蛋白双向电泳谱的变化大多发生在17岁以前，包括迁移到βB1、βB3、βA3、伽马C和伽马D原始位置的蛋白质减少，以及在双向凝胶上出现许多新的物种，其表观分子量类似于βB2和伽马S，但具有更酸性的PI S。这些蛋白质被鉴定为βB1和βA3/A1的去酰胺化形式，缺失其N末端延伸的部分。除αB外，在所有晶状体蛋白中都检测到了脱酰胺作用。这些数据表明，成人晶状体中的大部分水溶性蛋白由截短的βB1和βA3/A1晶状体蛋白组成，几乎所有的人晶状体蛋白，包括β晶状体蛋白，都容易发生脱酰胺。这些结果还提供了迄今为止成人晶状体双向电泳胶上蛋白质种类鉴定的最详细图谱。(C)1998年学术出版社。
The purpose of this study was to identify the major protein components in adult human lenses and to analyse the specific age-related changes in these proteins using two-dimensional electrophoresis, Edman sequencing, and in conjunction with the data in the accompanying manuscript, mass spectrometry. The majority of changes in the two-dimensional electrophoretic pattern of lens proteins occurred prior to 17 years of age, and included a decrease in proteins migrating to the original positions of beta B1, beta B3, beta A3, gamma C and gamma D, and the appearance of many new species with apparent molecular weights on two-dimensional electrophoretic gels similar to beta B2 and gamma S, but having more acidic pIs. These proteins were identified as deamidated forms of beta B1 and beta A3/A1 missing portions of their N-terminal extensions. With the exception of alpha B, deamidation was detected in all crystallin species. These data indicated that a major fraction of the water-soluble protein of the adult human lens is composed of truncated beta B1 and beta A3/A1 crystallins, and that nearly all human crystallins, including the beta-crystallins, are susceptible to deamidation. The results also provided the most detailed map to date of the identities of protein species on two-dimensional electrophoresis gels of adult human lenses. (C) 1998 Academic Press.