Regulation of voltage-dependent K+ channels by methionine oxidation: effect of nitric oxide and vitamin C

FEBS Lett. 1999 Jan 8;442(1):48-52. doi: 10.1016/s0014-5793(98)01616-0.

Abstract

Methionine oxidation is known to alter functional properties of a transient A-type potassium channel expressed in Xenopus oocytes. We show here that nitric oxide (NO) slows down the K+ channel inactivation time course by oxidizing a critical methionine residue in the inactivation ball domain of the channel protein. We also demonstrate that the channel protein is protected from methionine oxidation by the enzyme methionine sulfoxide reductase and the antioxidant vitamin C.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ascorbic Acid / pharmacology
  • Female
  • In Vitro Techniques
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Methionine / chemistry
  • Molecular Sequence Data
  • Nitric Oxide Donors / pharmacology
  • Nitric Oxide Synthase / metabolism
  • Oocytes / drug effects
  • Oocytes / metabolism
  • Oxidation-Reduction
  • Peptides / antagonists & inhibitors
  • Peptides / chemistry
  • Peptides / genetics
  • Peptides / metabolism
  • Potassium Channel Blockers
  • Potassium Channels / chemistry
  • Potassium Channels / metabolism*
  • Rats
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Shaker Superfamily of Potassium Channels
  • Xenopus

Substances

  • Intracellular Signaling Peptides and Proteins
  • Nitric Oxide Donors
  • Peptides
  • Potassium Channel Blockers
  • Potassium Channels
  • Recombinant Proteins
  • Shaker B potassium channel polypeptide
  • Shaker Superfamily of Potassium Channels
  • Shaker B inactivating peptide
  • Methionine
  • Nitric Oxide Synthase
  • Ascorbic Acid