Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide. Evidence for a dithiol-disulfide equilibrium and implications for redox regulation.

@article{Bogumil2000InactivationOC,
  title={Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide. Evidence for a dithiol-disulfide equilibrium and implications for redox regulation.},
  author={Ralf Bogumil and Dmitry Namgaladze and Dieter Schaarschmidt and T Schmachtel and S Hellstern and Rupert Mutzel and Volker Ullrich},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 5},
  pages={1407-15}
}
Calcineurin (CaN) is a Ca2+-and calmodulin (CaM)-dependent serine/threonine phosphatase containing a dinuclear Fe-Zn center in the active site. Recent studies have indicated that CaN is a possible candidate for redox regulation. The inactivation of bovine brain CaN and of the catalytic CaN A-subunit from Dictyostelium by the vicinal dithiol reagents phenylarsine oxide (PAO) and melarsen oxide (MEL) and by H2O2 was investigated. PAO and MEL inhibited CaN with an IC50 of 3-8 microM and the… CONTINUE READING

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