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Ferricyanide reductase activity in cataractous human lens
S Matsukura1, M Bando, H Obazawa
1Department of Ophthalmology, Tokai University School of Medicine, Kanagawa, Japan.
Ophthalmic Research
|January 1, 1996
Summary
Ferricyanide reductase activity decreases in human lenses with cataracts, correlating with protein aggregation and cataract development. This suggests a link between reductase function and lens opacity.
Area of Science:
- Ophthalmology
- Biochemistry
- Cell Biology
Background:
- Cataracts involve lens protein aggregation and opacity.
- NADH-dependent diaphorase activities are crucial in cellular metabolism.
- Lens structure changes significantly during cataract formation.
Purpose of the Study:
- To investigate ferricyanide reductase activity in different human cataractous lens fractions.
- To correlate reductase activity with lens protein aggregation and cataract type.
- To explore the role of reductase activity in the insoluble fraction.
Main Methods:
- Assaying ferricyanide reductase activity in soluble and insoluble lens fractions.
- Analyzing activity in cortex, nucleus periphery, and nucleus center.
- Measuring specific activity per mg of insoluble protein.
Main Results:
- Ferricyanide reductase activity decreased from cortex to nucleus center in both soluble and insoluble fractions.
- Reduced reductase activity correlated with increased lens protein aggregation.
- Insoluble fraction showed high specific activity in the cortex, decreasing with higher insoluble protein levels.
Conclusions:
- Decreased ferricyanide reductase activity is linked to lens protein aggregation and cataract development.
- The insoluble fraction's reductase activity may relate to plasma membrane metabolic activity.
- These findings offer insights into cataract pathogenesis and potential therapeutic targets.