Nitric oxide regulates exocytosis by S-nitrosylation of N-ethylmaleimide-sensitive factor

Cell. 2003 Oct 17;115(2):139-50. doi: 10.1016/s0092-8674(03)00803-1.

Abstract

Nitric oxide (NO) inhibits vascular inflammation, but the molecular basis for its anti-inflammatory properties is unknown. We show that NO inhibits exocytosis of Weibel-Palade bodies, endothelial granules that mediate vascular inflammation and thrombosis, by regulating the activity of N-ethylmaleimide-sensitive factor (NSF). NO inhibits NSF disassembly of soluble NSF attachment protein receptor (SNARE) complexes by nitrosylating critical cysteine residues of NSF. NO may regulate exocytosis in a variety of physiological processes, including vascular inflammation, neurotransmission, thrombosis, and cytotoxic T lymphocyte cell killing.

Publication types

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

MeSH terms

  • Animals
  • Aorta / cytology
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cells, Cultured
  • Cysteine / genetics
  • Cysteine / metabolism
  • Endothelium, Vascular / drug effects
  • Endothelium, Vascular / metabolism
  • Exocytosis / drug effects
  • Exocytosis / physiology*
  • Gene Expression Regulation
  • Humans
  • Membrane Proteins / drug effects
  • Membrane Proteins / metabolism
  • Mice
  • Mutagenesis, Site-Directed
  • N-Ethylmaleimide-Sensitive Proteins
  • NG-Nitroarginine Methyl Ester / pharmacology
  • Nitric Oxide / pharmacology*
  • Recombinant Proteins / metabolism
  • SNARE Proteins
  • Thrombin / pharmacology
  • Vascular Endothelial Growth Factor A / pharmacology
  • Vesicular Transport Proteins*
  • Weibel-Palade Bodies / drug effects
  • Weibel-Palade Bodies / metabolism
  • von Willebrand Factor / metabolism

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Recombinant Proteins
  • SNARE Proteins
  • Vascular Endothelial Growth Factor A
  • Vesicular Transport Proteins
  • von Willebrand Factor
  • Nitric Oxide
  • Thrombin
  • N-Ethylmaleimide-Sensitive Proteins
  • Nsf protein, mouse
  • Cysteine
  • NG-Nitroarginine Methyl Ester