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

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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

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Crystallins
Calpain
Cataract
Peptides
Selenious Acid
Electrophoresis
Rats
Lenses
Peptide Hydrolases
Sequence Analysis
In Vitro Techniques
Proteins

Keywords

  • Calpain
  • Cataract
  • Crystallin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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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.",
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AU - David, Larry

AU - Shearer, Thomas (Tom)

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N2 - 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.

AB - 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.

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KW - Cataract

KW - Crystallin

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