Antioxidant Defenses in the Human Eye: A Focus on Metallothioneins.

Antioxidant Defenses in the Human Eye: A Focus on Metallothioneins.
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DOI:
10.3390/antiox10010089
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发表时间:
2021-01-11
期刊:
Antioxidants (Basel, Switzerland)
影响因子:
--
通讯作者:
González-Iglesias H
González-Iglesias H
中科院分区:
其他
文献类型:
--
作者:
Álvarez-Barrios A;Álvarez L;García M;Artime E;Pereiro R;González-Iglesias H

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人眼是高度专门化的视觉器官,受内源性和外源性氧化剂的影响很大。氧化应激影响人眼的所有结构,特别是眼表、透镜、视网膜及其视网膜色素上皮,它们被认为是抗氧化剂保护的天然屏障,有助于眼部疾病的发作和/或进展。这些眼部结构包含复杂的抗氧化防御系统,根据细胞组织的不同,沿眼睛沿着略有不同。除了广泛研究的酶促抗氧化剂,包括超氧化物歧化酶、谷胱甘肽过氧化物酶、过氧化氢酶、过氧化物氧还蛋白和硒蛋白之外,金属硫蛋白(MT)被认为是具有进一步细胞介导功能的越来越受关注的抗氧化蛋白。这个富含半胱氨酸的低分子量蛋白质家族在涉及锌结合和释放的氧化还原依赖性机制中捕获和中和自由基。本文综述了MTs的分类、主要功能、作为抗氧化防御系统的Zn-MT氧化还原循环以及Zn-MTs在眼表、透镜、视网膜及其色素上皮中的抗氧化活性,并对Zn-MTs的抗氧化活性与锌结合位点的关系进行了综述。
The human eye, the highly specialized organ of vision, is greatly influenced by oxidants of endogenous and exogenous origin. Oxidative stress affects all structures of the human eye with special emphasis on the ocular surface, the lens, the retina and its retinal pigment epithelium, which are considered natural barriers of antioxidant protection, contributing to the onset and/or progression of eye diseases. These ocular structures contain a complex antioxidant defense system slightly different along the eye depending on cell tissue. In addition to widely studied enzymatic antioxidants, including superoxide dismutase, glutathione peroxidase, catalase, peroxiredoxins and selenoproteins, inter alia, metallothioneins (MTs) are considered antioxidant proteins of growing interest with further cell-mediated functions. This family of cysteine rich and low molecular mass proteins captures and neutralizes free radicals in a redox-dependent mechanism involving zinc binding and release. The state of the art of MTs, including the isoforms classification, the main functions described to date, the Zn-MT redox cycle as antioxidant defense system, and the antioxidant activity of Zn-MTs in the ocular surface, lens, retina and its retinal pigment epithelium, dependent on the number of occupied zinc-binding sites, will be comprehensively reviewed.
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