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Research Progress on the Classification and Function of Aldehyde Dehydrogenase as Corneal Crystallin |
Muchen Ren, Yuxi He, Shurong Wang, Yan Zhang |
Department of Ophthalmology, the Second Hospital of Jilin University, Changchun 130041, China |
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Abstract Aldehyde dehydrogenase exists in cornea. As a metabolic enzyme that contains a high proportion of corneal water-soluble proteins, it belongs to the most abundant protein in the cornea—corneal crystallins. Aldehyde dehydrogenase is a multifunctional protein, which not only maintains lens transparency but also has enzyme activity. It greatly improves the transparency and refractive power of corneal tissue. Simultaneously, aldehyde dehydrogenase also has effects on inhibiting the proliferation of corneal epithelial cells and corneal fbroblasts, extending the cell cycle, and regulating the scale-shaped differentiation of corneal epithelial cells. In addition, aldehyde dehydrogenase has the properties of anti-oxidative stress. It plays an important role in metabolizing endogenous and exogenous aldehydes in the body, avoiding the accumulation of toxic aldehydes, and resisting the body's oxidative stress response. Aldehyde dehydrogenase can reduce the irreversible damage to the cornea caused by free radicals and hundreds of toxic aldehydes produced by lipid peroxidation, which is of great signifcance in corneal homeostasis. This article will briefy describe the origin and classifcation of aldehyde dehydrogenase as corneal crystallin and focus on the research progress of its function in cornea.
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Received: 08 May 2021
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Fund:International Science and Technology Cooperation Project of Jilin Provincial Science and Technology Department (20200801016GH); Science and Technology Research Project of Jilin Provincial Education Department (JJKH20201103KJ) |
Corresponding Authors:
Yan Zhang, Department of Ophthalmology, the Second Hospital of Jilin University, Changchun 130041, China (Email: zhangy66@jlu.edu.cn)
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[1] |
. [J]. Chinese Journal of Optometry Ophthalmology and Visual science, 2023, 25(8): 0-. |
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