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      In vitro UV-B Effect on Lens Protein Solutions

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          Abstract

          To investigate the effects of UV-B exposure on the protein solutions of different lens parts, rabbit lenses were separated into the equator (Eq), anterior cortex (Ac), nucleus (Nu) and posterior cortex (Pc). After homogenization, the water-soluble protein from each part was irradiated with UV-B at 0 to 0.225 J/cm<sup>2</sup>. Alterations in the content of protein SH, carbonyl groups, light scattering intensity and SDS-PAGE pattern were measured to compare the effect of UV-B on the protein solutions of various lens parts with or without additional GSH to test its preventive effect. The results showed that after UV-B irradiation, the protein sulfhydryl groups are gradually reduced. The nonprotein thiol (GSH added to the protein solution) was lost more rapidly than the protein sulfhydryl. The high molecular bands on the SDS-PAGE pattern mainly aggregated with disulfide. UV-B damage also increased the content of carbonyl groups and light scattering, irrespective of the lens parts. Lens proteins from the equator suffered the least damage while those of the nucleus were most strongly affected by UV-B exposure. This study suggests that the lens proteins from various lens parts have different responses to UV-B exposure; the sensitivity was in the following order: Eq < Ac ≤ Pc < Nu.

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          Author and article information

          Journal
          ORE
          Ophthalmic Res
          10.1159/issn.0030-3747
          Ophthalmic Research
          S. Karger AG
          0030-3747
          1423-0259
          1997
          1997
          11 December 2009
          : 29
          : 2
          : 75-82
          Affiliations
          Department of Ophthalmology, Kanazawa Medical University, Uchinada, Japan
          Article
          268000 Ophthalmic Res 1997;29:75–82
          10.1159/000268000
          9154533
          © 1997 S. Karger AG, Basel

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          Page count
          Pages: 8
          Categories
          Original Paper

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