Oxalomalate, a competitive inhibitor of NADP + -dependent isocitrate dehydrogenase, enhances lipid peroxidation-mediated oxidative damage in U937 cells
Archives of Biochemistry and Biophysics, ISSN: 0003-9861, Vol: 416, Issue: 1, Page: 31-37
2003
- 15Citations
- 23Captures
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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.
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Metrics Details
- Citations15
- Citation Indexes15
- 15
- CrossRef14
- Captures23
- Readers23
- 23
Article Description
Membrane lipid peroxidation processes yield products that may react with DNA and proteins to cause oxidative modifications. Cytosolic NADP + -dependent isocitrate dehydrogenase (ICDH) in U937 cells produces NADPH, an essential reducing equivalent for the antioxidant system. The protective role of ICDH against lipid peroxidation-mediated oxidative damage in U937 cells was investigated in control cells pre-treated with oxalomalate, a competitive inhibitor of ICDH. Upon exposure to 2,2 ′ -azobis(2-amidinopropane) hydrochloride (AAPH) to U937 cells, which induces lipid peroxidation in membranes, the viability was lower and the protein oxidation, lipid peroxidation, and oxidative DNA damage, reflected by an increase in 8-hydroxy-2 ′ -deoxyguanosine, were higher in oxalomalate-treated cells as compared to control cells. We also observed the significant increase in the endogenous production of reactive oxygen species, as measured by the oxidation of 2 ′,7 ′ -dichlorodihydrofluorescin, as well as the significant decrease in the intracellular GSH level in oxalomalate-treated U937 cells upon exposure to AAPH. These results suggest that ICDH plays an important role as an antioxidant enzyme in cellular defense against lipid peroxidation-mediated oxidative damage through the removal of reactive oxygen species.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0003986103002911; http://dx.doi.org/10.1016/s0003-9861(03)00291-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037676172&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12859979; http://linkinghub.elsevier.com/retrieve/pii/S0003986103002911; http://api.elsevier.com/content/article/PII:S0003986103002911?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0003986103002911?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0003986103002911; http://dx.doi.org/10.1016/s0003-9861%2803%2900291-1; https://dx.doi.org/10.1016/s0003-9861%2803%2900291-1
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