Redox modulation of Ecto-NOX1 in human platelets

Mol Membr Biol. 2010 Aug;27(4-6):160-9. doi: 10.3109/09687688.2010.485936.

Abstract

By modulating the cellular redox state, the plasma membrane electron transport (PMET) is important in platelet biology; indeed, the oxidant/antioxidant balance plays a central role during activation of the coagulation pathway. None the less, in human platelets, the PMET system has not yet been fully characterized and the molecular identities of most components are unknown. Here, for the first time, the presence of the plasma membrane hydroquinone (NADH) oxidase Ecto-NOX1 in human platelets has been described. We found that Ecto-NOX1 expression is modulated by capsaicin: Indeed, it is positively regulated through a mechanism requiring binding of capsaicin to its receptor, namely the transient receptor potential vanilloid subtype 1 (TRPV1). Ligand-receptor interaction triggers a signalling cascade leading to ROS production, which in turn enhances expression and activity of Ecto-NOX1. Redox regulation of Ecto-NOX1 may be important to platelet recruitment and activation during inflammatory diseases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Analysis of Variance
  • Blood Platelets / drug effects
  • Blood Platelets / enzymology*
  • Blotting, Western
  • Capsaicin / pharmacology
  • Electron Transport
  • Humans
  • Membrane Proteins / blood*
  • Membrane Proteins / chemistry
  • NAD / blood
  • NADP / blood
  • NADPH Oxidase 1
  • NADPH Oxidases / biosynthesis
  • NADPH Oxidases / blood*
  • NADPH Oxidases / chemistry
  • Oxidation-Reduction
  • Reactive Oxygen Species / metabolism
  • TRPV Cation Channels / blood
  • Young Adult

Substances

  • Membrane Proteins
  • Reactive Oxygen Species
  • TRPV Cation Channels
  • TRPV1 protein, human
  • NAD
  • NADP
  • NADPH Oxidase 1
  • NADPH Oxidases
  • NOX1 protein, human
  • Capsaicin