An SOD mimic protects NADP+-dependent isocitrate dehydrogenase against oxidative inactivation.

Published

Journal Article

The isocitrate dehydrogenases (ICDs) catalyse the oxidative decarboxylation of isocitrate to alpha-ketoglutarate and can use either NAD(+) or NADP(+) as a cofactor. Recent studies demonstrate that the NADP(+)-dependent isocitrate dehydrogenase, as a source of electrons for cellular antioxidants, is important for protection against oxidative damage. ICD, however, is susceptible to oxidative inactivation, which in turn compromises cellular antioxidant defense. This study investigates the effect of a superoxide dismutase (SOD) mimic, MnTM-2-PyP(5+), on the inactivation of NADP(+)-dependent ICD in SOD-deficient Escherichia coli and in diabetic rats. The findings show that E. coli ICD is inactivated by superoxide, but the inactivated enzyme is replaced by de novo protein synthesis. Statistically significant decrease of ICD activity was found in the hearts of diabetic rats. MnTM-2-PyP(5+) protected ICD in both models.

Full Text

Duke Authors

Cited Authors

  • Batinic-Haberle, I; Benov, LT

Published Date

  • July 2008

Published In

Volume / Issue

  • 42 / 7

Start / End Page

  • 618 - 624

PubMed ID

  • 18608518

Pubmed Central ID

  • 18608518

Electronic International Standard Serial Number (EISSN)

  • 1029-2470

Digital Object Identifier (DOI)

  • 10.1080/10715760802209639

Language

  • eng

Conference Location

  • England