Lens aging: effects of crystallins.
Lens aging: effects of crystallins.
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DOI：
10.1016/j.bbagen.2009.05.008
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发表时间：
2009-10
期刊：
影响因子：
--
通讯作者：
Santhoshkumar P
中科院分区：
文献类型：
--
作者：
Sharma KK;Santhoshkumar P
眼睛透镜的主要功能是把光线聚焦在视网膜上。晶状体中的主要蛋白质-a、B和g-晶状体蛋白-不断经历与年龄相关的变化，例如氧化、脱酰胺、截短、糖化和甲基化。这种与年龄相关的修饰是累积的，并影响晶体蛋白的结构和功能。随着时间的推移，修饰的晶状体蛋白聚集，导致透镜在视网膜上越来越多地散射光，而不是将光聚焦在其上，并导致透镜逐渐失去其透明度并变得不透明。晶状体相关的透镜混浊或白内障是全世界失明的主要原因。我们回顾了老化过程中晶状体中发生的脱酰胺和糖化作用，并牢记这些修饰在蛋白质中带来的结构和功能变化。此外，我们回顾蛋白水解和讨论最近的观察如何晶体蛋白片段在体内产生的，通过其抗分子伴侣活性可能会导致晶体蛋白聚集在老化的镜头。我们还回顾了高压氧治疗诱导的豚鼠和“人源化”抗坏血酸转运小鼠模型，作为研究透镜蛋白年龄相关变化的合适选择。
The primary function of the eye lens is to focus light on the retina. The major proteins in the lens—a, b, and g-crystallins—are constantly subjected to age-related changes such as oxidation, deamidation, truncation, glycation, and methylation. Such age-related modifications are cumulative and affect crystallin structure and function. With time, the modified crystallins aggregate, causing the lens to increasingly scatter light on the retina instead of focusing light on it and causing the lens to lose its transparency gradually and become opaque. Age-related lens opacity, or cataract, is the major cause of blindness worldwide. We review deamidation, and glycation that occur in the lenses during aging keeping in mind the structural and functional changes that these modifications bring about in the proteins. In addition, we review proteolysis and discuss recent observations on how crystallin fragments generated in vivo, through their anti-chaperone activity may cause crystallin aggregation in aging lenses. We also review hyperbaric oxygen treatment induced guinea pig and ‘humanized’ ascorbate transporting mouse models as suitable options for studies on age-related changes in lens proteins.
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影响因子：
5.6
作者：
Ahmad, Md. Falz;Raman, Bakthisaran;Rao, Ch. Mohan
通讯作者：
Rao, Ch. Mohan
DOI：
10.1006/bbrc.2000.3461
发表时间：
2000-09-16
影响因子：
3.1
作者：
Aquilina, JA;Truscott, RJW
通讯作者：
Truscott, RJW
DOI：
10.1006/bbrc.2001.5288
发表时间：
2001-08-03
影响因子：
3.1
作者：
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通讯作者：
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影响因子：
4.8
作者：
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影响因子：
4.1
作者：
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通讯作者：
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