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

Mitsuyoshi Azuma; Eri Inoue; Takayuki Oka; Thomas R. Shearer

doi:10.3109/02713689508999911

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

Mitsuyoshi Azuma, Eri Inoue, Takayuki Oka, Thomas R. Shearer

Integrative Biosciences

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

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 language	English (US)
Pages (from-to)	27-34
Number of pages	8
Journal	Current Eye Research
Volume	14
Issue number	1
DOIs	https://doi.org/10.3109/02713689508999911
State	Published - 1995

Keywords

Aldose reductase inhibitor
Calcium
Calpain
Proteolysis
Rat
Sugar cataract

ASJC Scopus subject areas

Ophthalmology
Sensory Systems
Cellular and Molecular Neuroscience

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10.3109/02713689508999911

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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.",

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AU - Azuma, Mitsuyoshi

AU - Inoue, Eri

AU - Oka, Takayuki

AU - Shearer, Thomas R.

PY - 1995

Y1 - 1995

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AB - 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.

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KW - Proteolysis

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KW - Sugar cataract

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

Abstract

Keywords

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