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首页> 外文期刊>Biochemistry >Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin
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Binding of γ-Crystallin Substrate Prevents the Binding of Copper and Zinc Ions to the Molecular Chaperone α-Crystallin

机译:γ-晶体素基质的结合可防止铜和锌离子的结合到分子伴侣α-晶体中

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摘要

α-Crystallin is a small heat shock protein and molecular chaperone. Binding of Cu~(2+) and Zn~(2+) ions to Rcrystallin leads to enhanced chaperone function. Sequestration of Cu~(2+) by R-crystallin prevents metal-ion mediated oxidation. Here we show that binding of human γD-crystallin (HGD, a natural substrate) to human RA-crystallin (HAA) is inversely related to the binding of Cu~(2+)/Zn~(2+) ions: The higher the amount of bound HGD, the lower the amount of bound metal ions. Thus, in the aging lens, depletion of free HAA will not only lower chaperone capacity but also lower Cu~(2+) sequestration, thereby promoting oxidation and cataract.
机译:α-结晶是小型热休克蛋白和分子伴侣。 Cu〜(2+)和Zn〜(2+)离子与rcrystallin的结合导致增强的伴侣官能团。 R-结晶素Cu〜(2+)的螯合防止金属离子介导的氧化。 在这里,我们表明,人γD-结晶素(HGD,天然基质)与人Ra-结晶(HAA)的结合与Cu〜(2 +)/ Zn〜(2+)离子的结合与:越高 结合HGD的量,结合金属离子的量越低。 因此,在老化晶状体中,游离HAA的耗竭不仅将降低伴侣容量,而且降低Cu〜(2+)螯合,从而促进氧化和白内障。

著录项

  • 来源
    《Biochemistry》 |2011年第16期|共3页
  • 作者单位

    Department of Chemistry Life Sciences Research Building University at Albany State University of New York Albany New York 12222 United States;

    Department of Chemistry Life Sciences Research Building University at Albany State University of New York Albany New York 12222 United States;

    Department of Chemistry Life Sciences Research Building University at Albany State University of New York Albany New York 12222 United States;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

    γ-Crystallin; Substrate; Ions;

    机译:γ-晶体;衬底;离子;

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