In vitro precipitation of rat lens crystalline by calpain I – A calpain requiring low amounts of calcium for activation

T. R. Shearer, D. B. Throneburg, M. Shih

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

The overall goal of this study was to provide data on the function and physiologic significance of lens calpain I, a cysteine protease requiring low amounts of calcium for activation. Reverse-transcriptase polymerase chain reaction was used to detect mRNAs for calpains I and II in young rat lenses. An in vitro model of crystallin precipitation was used to assess the ability of calpain I to induce hydrolysis and precipitation of crystallins. We found that incubation of crystallins with purified calpain I was indeed a powerful inducer of crystallin precipitation. However, mRNA levels for calpain I in whole lens appeared to be lower compared to calpain-II mRNA. Participation of calpain I in crystallin precipitation during normal maturation of rodent lenses or cataract formation is thus theoretically possible, but unlikely, because of the low level of expression of calpain I.

Original languageEnglish (US)
Pages (from-to)109-114
Number of pages6
JournalOphthalmic Research
Volume28
Issue number2
DOIs
StatePublished - Jan 1 1997

Keywords

  • Calpain I
  • Crystallins
  • Lens
  • Precipitation
  • Rat
  • mRNA

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

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