Glyoxalase i activity and immunoreactivity in the aging human lens
Biogerontology, ISSN: 1389-5729, Vol: 10, Issue: 6, Page: 711-720
2009
- 23Citations
- 17Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations23
- Citation Indexes23
- 23
- CrossRef14
- Captures17
- Readers17
- 17
Article Description
Glyoxalase I (GLOI) is the first enzyme of the glyoxalase system that catalyzes the metabolism of reactive dicarbonyls, such as methylglyoxal (MGO). During aging and cataract development, human lens proteins are chemically modified by MGO, which is likely due to inadequate metabolism of MGO by the glyoxalase system. In this study, we have determined the effect of aging on GLOI activity and the immunoreactivity and morphological distribution of GLOI in the human lens. A monoclonal antibody was developed against human GLOI. GLOI immunoreactivity was strongest in the anterior epithelial cells and weaker in rest of the lens. Cultured human lens epithelial cells showed immunostaining throughout the cytoplasm. In the human lens, GLOI activity and immunoreactivity both decreased with age. We believe that this would lead to promotion of MGO-modification in aging lens proteins. © 2009 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=71349086842&origin=inward; http://dx.doi.org/10.1007/s10522-009-9218-2; http://www.ncbi.nlm.nih.gov/pubmed/19238574; http://link.springer.com/10.1007/s10522-009-9218-2; https://dx.doi.org/10.1007/s10522-009-9218-2; https://link.springer.com/article/10.1007/s10522-009-9218-2; http://www.springerlink.com/index/10.1007/s10522-009-9218-2; http://www.springerlink.com/index/pdf/10.1007/s10522-009-9218-2
Springer Science and Business Media LLC
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