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Current Eye Research Volume 14, 1995 - Issue 1
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Original Article

Proteolysis by calpain is an underlying mechanism for formation of sugar cataract in rat lens

Mitsuyoshi Azuma Department of Oral Molecular Biology, Oregon Health Sciences University, Portland, OR, 97201, USA; Research Laboratories, Senju Pharmaceutical Co. Ltd, Kobe, Japan
,
Eri Inoue Research Laboratories, Senju Pharmaceutical Co. Ltd, Kobe, Japan
,
Takayuki Oka Research Laboratories, Senju Pharmaceutical Co. Ltd, Kobe, Japan
&
Thomas R. Shearer Department of Oral Molecular Biology, Oregon Health Sciences University, Portland, OR, 97201, USA
Pages 27-34 | Received 21 Apr 1994, Accepted 29 Sep 1994, Published online: 02 Jul 2009

References

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  • David L. L., Wright J. W., Shearer T. R. Calpain II induced insolubilization of lens β-crystallin polypeptides may induce cataract. Biochim. Biophys. Acta 1992; 1139: 210–216
  • David L. L., Shearer T. R. β-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β-crystallins insolubilized during cataract. FEBS Lett 1993; 324: 265–270
  • Shearer T. R., David L. L., Anderson R. S., Azuma M. Review of selenite cataract. Curr. Eye Res. 1992; 11: 357–369
  • Kelley M. J., David L. L., Iwasaki N., Wright J., Shearer T. R. α-crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J. Biol. Chem. 1993; 268: 18844–18849
  • Azuma M., David L. L., Shearer T. R. Proteolysis of β-crystallins during normal aging in human lens. Invest. Ophthalmol. Vis. Sci. 1994; 35(Suppl.): 4427

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