β-Crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β-crystallins insolubilized during cataract

Larry L. David, Thomas R. Shearer

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

Incubation of soluble proteins from rat lens with the protease calpain II caused the precipitation of β-crystallin polypeptides. Two-dimensional electrophoresis and sequence analysis identified β-crystallin polypeptides both before and after their precipitation by calpain II. β-crystallin polypeptides precipitated by calpain were cleaved at their NH2-terminal extensions. These cleavage sites were similar to cleavage sites occurring in β-crystallin polypeptides precipitated during formation of experimental cataract induced by an overdose of selenite. These data suggested that calpain II caused β-crystallin insolubilization during cataract formation, and indicated that the process can be mimicked in vitro.

Original languageEnglish (US)
Pages (from-to)265-270
Number of pages6
JournalFEBS Letters
Volume324
Issue number3
DOIs
StatePublished - Jun 21 1993

Keywords

  • Calpain
  • Cataract
  • Crystallin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'β-Crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β-crystallins insolubilized during cataract'. Together they form a unique fingerprint.

  • Cite this