Oxidant-mediated proteolytic activation of Ca(+)-ATPase in microsomes of pulmonary smooth muscle

FEBS Lett. 1996 Jun 3;387(2-3):171-4. doi: 10.1016/0014-5793(96)00471-1.

Abstract

Treatment of bovine pulmonary artery smooth muscle tissue microsomes with H2O2 (1 mM) markedly stimulated protease activity tested with a synthetic substrate N-benzoyl-DL-arginine p-nitroanilide (BAPNA), and also enhanced Ca(2+)-ATPase activity. ATP-dependent Ca(2+) uptake was found to be stimulated upon treatment of the microsomes with H2O2. Pretreatment of the microsomes with vitamin E and aprotinin prevented the H2O2-induced stimulation of Ca(2+)-ATPase activity and also ATP-dependent Ca(2+) uptake. In contrast, H2O2-induced inhibition of Na(+)-dependent Ca(2+) uptake was reversed by vitamin E and aprotinin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5'-Nucleotidase / metabolism
  • Acid Phosphatase / metabolism
  • Animals
  • Aprotinin / pharmacology
  • Calcium / metabolism
  • Calcium-Transporting ATPases / drug effects
  • Calcium-Transporting ATPases / metabolism*
  • Cattle
  • Electron Transport Complex IV / metabolism
  • Enzyme Activation
  • Hydrogen Peroxide / pharmacology*
  • Microsomes / drug effects
  • Microsomes / enzymology*
  • Muscle, Smooth, Vascular / enzymology*
  • NADH, NADPH Oxidoreductases / metabolism
  • NADPH-Ferrihemoprotein Reductase
  • Oxidants / pharmacology*
  • Pulmonary Artery
  • Vitamin E / pharmacology

Substances

  • Oxidants
  • Vitamin E
  • Aprotinin
  • Hydrogen Peroxide
  • NADH, NADPH Oxidoreductases
  • NADPH-Ferrihemoprotein Reductase
  • Electron Transport Complex IV
  • Acid Phosphatase
  • 5'-Nucleotidase
  • Calcium-Transporting ATPases
  • Calcium