Distribution and activity of glutathione-S-transferase in normal human lenses and in cataractous human epithelia
- 1 January 1993
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 12 (5) , 433-437
- https://doi.org/10.3109/02713689309024625
Abstract
The distribution of glutathione-S-transferase (GST) activity was determined in frozen normal human lenses. The highest activity of GST was found in the peripheral and equatorial regions, whereas the lowest activity was found in the nucleus. Western blot showed that both μ and χ isoenzymes of GST were present in human lenses. This result is similar to that found in rat lenses. In addition, GST activity was analyzed in 50 lens epithelia which were obtained during cataract surgery. Twenty-seven lens epithelia showed no activity. Statistically significant association was found between cortical and mixed cortical-nuclear cataract and loss of GST activity. No association was found between pure nuclear cataract and loss of epithelial GST activity.Keywords
This publication has 25 references indexed in Scilit:
- The human glutathione S-transferases: comparison of isoenzyme expression in normal and astrocytoma brainBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1992
- Pig lens glutathione S-transferase belongs to class Pi enzymeBiochemical and Biophysical Research Communications, 1991
- Glutathione S-transferases of bovine iris and ciliary body: characterization of isoenzymesCurrent Eye Research, 1989
- Glutathione Transferases—Structure and Catalytic ActivitCritical Reviews in Biochemistry, 1988
- Glutathione reductase in human lens epithelium: FAD-inducedin vitroactivationCurrent Eye Research, 1987
- Glutathione peroxidase, glutathione reductase and glutathione-S-transferase activities in the rhesus monkey lens as a function of ageCurrent Eye Research, 1986
- Glutathione metabolism in lenses of Emory and cataract-resistant mice: activity of five enzymesCurrent Eye Research, 1986
- Superoxide dismutase, catalase and glutathione peroxidase in the human cataractous lensExperimental Eye Research, 1983
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Glutathione Metabolic Pathway as a Scavenging System in the LensOphthalmic Research, 1979