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人眼醛脱氢酶同工酶:作为角膜和晶状体中主要可溶性蛋白质的分布及特性

Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens.

作者信息

King G, Holmes R

机构信息

Faculty of Science and Technology, Griffith University, Brisbane, Queensland, Australia.

出版信息

J Exp Zool. 1998;282(1-2):12-7.

PMID:9723161
Abstract

Human aldehyde dehydrogenase isozymes (ALDHs; EC 1.2.1.3) exhibit very high levels of activity in anterior eye tissues. Human corneal ALDH1 and ALDH3 isozymes are present as major soluble proteins (3% and 5%, respectively, of corneal soluble protein) and may play major roles in protecting the cornea against ultraviolet radiation (UVR)-induced tissue damage, as well as contributing directly to ultraviolet B (UV-B) photoreception. The human lens exhibits high levels of ALDH1 activity (1-2% of lens-soluble protein) and lower levels of ALDH3 activity. Kinetic analyses support a role for these enzymes in the metabolism of peroxidic aldehydes, which have been reported in ocular tissues.

摘要

人醛脱氢酶同工酶(ALDHs;EC 1.2.1.3)在前眼部组织中表现出非常高的活性水平。人角膜ALDH1和ALDH3同工酶作为主要的可溶性蛋白质存在(分别占角膜可溶性蛋白质的3%和5%),可能在保护角膜免受紫外线辐射(UVR)诱导的组织损伤方面发挥主要作用,以及直接参与紫外线B(UV-B)光感受。人晶状体表现出高水平的ALDH1活性(占晶状体可溶性蛋白质的1-2%)和较低水平的ALDH3活性。动力学分析支持这些酶在眼部组织中已报道的过氧化物醛代谢中的作用。

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