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In praise of H2O2, the versatile ROS, and its vanadium complexes

Ramasarma, T (2012) In praise of H2O2, the versatile ROS, and its vanadium complexes. In: Toxicology Mechanisms and Methods, 22 (5). pp. 336-346.

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Official URL: http://dx.doi.org/10.3109/15376516.2012.666649


Hydrogenperoxide (H2O2) is generated in mitochondria in aerobic cells as a minor product of electron transport, is inhibited selectively by phenolic acids (in animals) or salicylhydroxamate (in plants) and is regulated by hormones and environmental conditions. Failure to detect this activity is due to presence of H2O2-consuming reactions or inhibitors present in the reaction mixture. H2O2 has a role in metabolic regulation and signal transduction reactions. A number of enzymes and cellular activities are modified, mostly by oxidizing the protein-thiol groups, on adding H2O2 in mM concentrations. On complexing with vanadate, also occurring in traces, H2O2 forms diperoxovanadate (DPV), stable at physiological pH and resistant to degradation by catalase. DPV was found to substitute for H2O2 at concentrations orders of magnitude lower, and in presence of catalase, as a substrate for user reaction, horseradish peroxidase (HRP), and in inactivating glyceraldehyde-3-phosphate dehydrogenase. superoxide dismutase (SOD)-sensitive oxidation of NADH was found to operate as peroxovanadate cycle using traces of DPV and decameric vanadate (V-10) and reduces O-2 to peroxide (DPV in presence of free vanadate). This offers a model for respiratory burst. Diperoxovanadate reproduces several actions of H2O2 at low concentrations: enhances protein tyrosine phosphorylation, activates phospholipase D, produces smooth muscle contraction, and accelerates stress induced premature senescence (SIPS) and rounding in fibroblasts. Peroxovanadates can be useful tools in the studies on H2O2 in cellular activities and regulation.

Item Type: Journal Article
Publication: Toxicology Mechanisms and Methods
Publisher: Informa plc
Additional Information: Copyright of this article is belongs to Informa plc.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 23 Jul 2012 12:25
Last Modified: 23 Jul 2012 12:25
URI: http://eprints.iisc.ac.in/id/eprint/44649

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