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

Thomas (Tom) Shearer, D. B. Throneburg, M. Shih

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 numberSUPPL. 2
StatePublished - Aug 1996

Fingerprint

Crystallins
Calpain
Lenses
Calcium
Messenger RNA
In Vitro Techniques
Cysteine Proteases
Reverse Transcriptase Polymerase Chain Reaction
Cataract
Rodentia
Hydrolysis

Keywords

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

ASJC Scopus subject areas

  • Ophthalmology

Cite this

In vitro precipitation of rat lens crystallins by calpain I - A calpain requiring low amounts of calcium for activation. / Shearer, Thomas (Tom); Throneburg, D. B.; Shih, M.

In: Ophthalmic Research, Vol. 28, No. SUPPL. 2, 08.1996, p. 109-114.

Research output: Contribution to journalArticle

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