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      Oxidative Denaturation of Lens Protein: Prevention by Pyruvate

      ,

      Ophthalmic Research

      S. Karger AG

      Protein carbonyl, Pyruvate, Oxygen radicals, Peroxide, Lens

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          Abstract

          The denaturation of lens proteins as apparent by the generation of protein carbonyl in the presence of active oxygen and the prevention of such denaturation by pyruvate were studied. Active oxygen was generated by the action of xanthine oxidase on xanthine under aerobic conditions. Rat lens protein when incubated with xanthine and xanthine oxidase produced significant amounts of the carbonyl derivative. The formation of such carbonyl was substantially inhibited by pyruvate. In addition, the keto acid also was found to stimulate the utilization of glucose through HMP shunt, a mechanism known to transport reducing equivalents from glucose to peroxide. The results suggest that pyruvate exerts a beneficial effect in attenuating the age-related protein modifications and consequent physiological impairments. These studies are also considered useful from the therapeutic point of view.

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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
          1995
          1995
          11 December 2009
          : 27
          : 1
          : 18-22
          Affiliations
          Department of Ophthalmology, University of Maryland at Baltimore, Md., USA
          Article
          267562 Ophthalmic Res 1995;27:18–22
          10.1159/000267562
          7596555
          © 1995 S. Karger AG, Basel

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          Page count
          Pages: 5
          Categories
          Original Paper

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