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Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats
PURPOSE: To determine putative alterations in the major lenticular proteins in Wistar rats of different ages and to compare these alterations with those occurring in rats with selenite-induced cataract. METHODS: Lenticular transparency was determined by morphological examination using slit-lamp biom...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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Molecular Vision
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838741/ https://www.ncbi.nlm.nih.gov/pubmed/20300567 |
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author | Sakthivel, Muniyan Elanchezhian, Rajan Thomas, Philip A. Geraldine, Pitchairaj |
author_facet | Sakthivel, Muniyan Elanchezhian, Rajan Thomas, Philip A. Geraldine, Pitchairaj |
author_sort | Sakthivel, Muniyan |
collection | PubMed |
description | PURPOSE: To determine putative alterations in the major lenticular proteins in Wistar rats of different ages and to compare these alterations with those occurring in rats with selenite-induced cataract. METHODS: Lenticular transparency was determined by morphological examination using slit-lamp biomicroscopy. Alterations in lenticular protein were determined by sodium dodecyl sulfate-PAGE (SDS–PAGE) and confirmed immunologically by western blot. RESULTS: Morphological examination did not reveal observable opacities in the lenses of the rats of different age groups; however, dense nuclear opacities were noted in lenses of rats in the selenite-cataract group. Western blot assays revealed age-related changes in soluble and urea-soluble lenticular proteins. Decreased αA- and βB1-crystallins in the soluble fraction and aggregation of αA-crystallin, in addition to the degraded fragment of βB1-crystallin, in the urea-soluble fraction appeared to occur in relation to increasing age of the rats from which the lenses were taken; similarly, cytoskeletal proteins appeared to decline with increasing age. The lenses from rats in the selenite-cataract group exhibited similar changes, except that there was also high molecular weight aggregation of αA-crystallin. CONCLUSIONS: The results of this study suggest that there is loss, as well as aggregation, of αA-crystallin in the aging rat lens, although there is no accompanying loss of lenticular transparency. |
format | Text |
id | pubmed-2838741 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Vision |
record_format | MEDLINE/PubMed |
spelling | pubmed-28387412010-03-17 Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats Sakthivel, Muniyan Elanchezhian, Rajan Thomas, Philip A. Geraldine, Pitchairaj Mol Vis Research Article PURPOSE: To determine putative alterations in the major lenticular proteins in Wistar rats of different ages and to compare these alterations with those occurring in rats with selenite-induced cataract. METHODS: Lenticular transparency was determined by morphological examination using slit-lamp biomicroscopy. Alterations in lenticular protein were determined by sodium dodecyl sulfate-PAGE (SDS–PAGE) and confirmed immunologically by western blot. RESULTS: Morphological examination did not reveal observable opacities in the lenses of the rats of different age groups; however, dense nuclear opacities were noted in lenses of rats in the selenite-cataract group. Western blot assays revealed age-related changes in soluble and urea-soluble lenticular proteins. Decreased αA- and βB1-crystallins in the soluble fraction and aggregation of αA-crystallin, in addition to the degraded fragment of βB1-crystallin, in the urea-soluble fraction appeared to occur in relation to increasing age of the rats from which the lenses were taken; similarly, cytoskeletal proteins appeared to decline with increasing age. The lenses from rats in the selenite-cataract group exhibited similar changes, except that there was also high molecular weight aggregation of αA-crystallin. CONCLUSIONS: The results of this study suggest that there is loss, as well as aggregation, of αA-crystallin in the aging rat lens, although there is no accompanying loss of lenticular transparency. Molecular Vision 2010-03-16 /pmc/articles/PMC2838741/ /pubmed/20300567 Text en |
spellingShingle | Research Article Sakthivel, Muniyan Elanchezhian, Rajan Thomas, Philip A. Geraldine, Pitchairaj Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats |
title | Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats |
title_full | Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats |
title_fullStr | Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats |
title_full_unstemmed | Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats |
title_short | Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats |
title_sort | alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in wistar rats |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838741/ https://www.ncbi.nlm.nih.gov/pubmed/20300567 |
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