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

Mitsuyoshi Azuma, Eri Inoue, Takayuki Oka, Thomas (Tom) Shearer

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

To confirm the effect of a new aldose reductase inhibitor (ARI), rat lenses were cultured with xylose. ARI prevented opacities and reduced lens hydration caused by xylose. Next, cataract was produced by feeding a diet containing 50% galactose. ARI was tested for amelioration of cataract. On day 19 after feeding of galactose, nuclear cataracts were visible in 75% of the animals receiving only galactose, while nuclear cataracts were not observed in animals treated with ARI. In galactose cataract, lens hydration and calcium were significantly increased. Calpain in soluble and insoluble fractions was decreased, αand βcrystallins were proteolyzed. These changes were inhibited by administration of ARI. These results suggested that proteolysis by calpain is an underlying mechanism in formation of sugar cataract in rat lens.

Original languageEnglish (US)
Pages (from-to)27-34
Number of pages8
JournalCurrent Eye Research
Volume14
Issue number1
DOIs
StatePublished - 1995

Fingerprint

Calpain
Cataract
Lenses
Proteolysis
Aldehyde Reductase
Galactose
Xylose
Crystallins
Diet
Calcium

Keywords

  • Aldose reductase inhibitor
  • Calcium
  • Calpain
  • Proteolysis
  • Rat
  • Sugar cataract

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

Cite this

Proteolysis by calpain is an underlying mechanism for formation of sugar cataract in rat Lens. / Azuma, Mitsuyoshi; Inoue, Eri; Oka, Takayuki; Shearer, Thomas (Tom).

In: Current Eye Research, Vol. 14, No. 1, 1995, p. 27-34.

Research output: Contribution to journalArticle

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