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Inactivation of mitochondrial NADP+-dependent isocitrate dehydrogenase by hypochlorous acid.
Free Radic Res. 2008 May; 42(5):467-73.FR

Abstract

Myeoloperoxidase catalyses the formation of hypochlorous acid (HOCl) via reaction of H(2)O(2) with Cl(-) ion. Although HOCl is known to play a major role in the human immune system by killing bacteria and other invading pathogens, excessive generation of this oxidant is known to cause damage to tissue. Recently, it was demonstrated that the control of mitochondrial redox balance and oxidative damage is one of the primary functions of mitochondrial NADP(+)-dependent isocitrate dehydrogenase (IDPm) to supply NADPH for antioxidant systems. This study investigated whether the IDPm would be a vulnerable target of HOCl as a purified enzyme and in intact cells. Loss of enzyme activity was observed and the inactivation of IDPm was reversed by thiols. Transfection of HeLa cells with an IDPm small interfering RNA (siRNA) markedly enhanced HOCl-induced oxidative damage to cells. The HOCl-mediated damage to IDPm may result in the perturbation of the cellular antioxidant defense mechanisms and subsequently lead to a pro-oxidant condition.

Authors+Show Affiliations

School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, Taegu, South Korea.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18484410

Citation

Park, Sin Young, et al. "Inactivation of Mitochondrial NADP+-dependent Isocitrate Dehydrogenase By Hypochlorous Acid." Free Radical Research, vol. 42, no. 5, 2008, pp. 467-73.
Park SY, Lee SM, Shin SW, et al. Inactivation of mitochondrial NADP+-dependent isocitrate dehydrogenase by hypochlorous acid. Free Radic Res. 2008;42(5):467-73.
Park, S. Y., Lee, S. M., Shin, S. W., & Park, J. W. (2008). Inactivation of mitochondrial NADP+-dependent isocitrate dehydrogenase by hypochlorous acid. Free Radical Research, 42(5), 467-73. https://doi.org/10.1080/10715760802098834
Park SY, et al. Inactivation of Mitochondrial NADP+-dependent Isocitrate Dehydrogenase By Hypochlorous Acid. Free Radic Res. 2008;42(5):467-73. PubMed PMID: 18484410.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inactivation of mitochondrial NADP+-dependent isocitrate dehydrogenase by hypochlorous acid. AU - Park,Sin Young, AU - Lee,Su-Min, AU - Shin,Seoung Woo, AU - Park,Jeen-Woo, PY - 2008/5/20/pubmed PY - 2008/8/22/medline PY - 2008/5/20/entrez SP - 467 EP - 73 JF - Free radical research JO - Free Radic Res VL - 42 IS - 5 N2 - Myeoloperoxidase catalyses the formation of hypochlorous acid (HOCl) via reaction of H(2)O(2) with Cl(-) ion. Although HOCl is known to play a major role in the human immune system by killing bacteria and other invading pathogens, excessive generation of this oxidant is known to cause damage to tissue. Recently, it was demonstrated that the control of mitochondrial redox balance and oxidative damage is one of the primary functions of mitochondrial NADP(+)-dependent isocitrate dehydrogenase (IDPm) to supply NADPH for antioxidant systems. This study investigated whether the IDPm would be a vulnerable target of HOCl as a purified enzyme and in intact cells. Loss of enzyme activity was observed and the inactivation of IDPm was reversed by thiols. Transfection of HeLa cells with an IDPm small interfering RNA (siRNA) markedly enhanced HOCl-induced oxidative damage to cells. The HOCl-mediated damage to IDPm may result in the perturbation of the cellular antioxidant defense mechanisms and subsequently lead to a pro-oxidant condition. SN - 1029-2470 UR - https://www.unboundmedicine.com/medline/citation/18484410/Inactivation_of_mitochondrial_NADP+_dependent_isocitrate_dehydrogenase_by_hypochlorous_acid_ DB - PRIME DP - Unbound Medicine ER -