Platelet-endothelial cell adhesion molecule-1 regulates endothelial NO synthase activity and localization through signal transducers and activators of transcription 3-dependent NOSTRIN expression

Arterioscler Thromb Vasc Biol. 2011 Mar;31(3):643-9. doi: 10.1161/ATVBAHA.110.216200. Epub 2010 Dec 23.

Abstract

Background: NO produced by the endothelial NO synthase (eNOS) is an important regulator of cardiovascular physiological and pathological features. eNOS is activated by numerous stimuli, and its activity is tightly regulated. Platelet-endothelial cell adhesion molecule-1 (PECAM-1) has been implicated in regulating eNOS activity in response to shear stress. The current study was conducted to determine the role of PECAM-1 in the regulation of basal eNOS activity.

Methods and results: We demonstrate that PECAM-1-knockout ECs have increased basal eNOS activity and NO production. Mechanistically, increased eNOS activity is associated with a decrease in the inhibitory interaction of eNOS with caveolin-1, impaired subcellular localization of eNOS, and decreased eNOS traffic inducer (NOSTRIN) expression in the absence of PECAM-1. Furthermore, we demonstrate that activation of blunted signal transducers and activators of transcription 3 (STAT3) in the absence of PECAM-1 results in decreased NOSTRIN expression via direct binding of the signal transducers and activators of transcription 3 to the NOSTRIN promoter.

Conclusions: Our results reveal an elegant mechanism of eNOS regulation by PECAM-1 through signal transducers and activators of transcription 3-mediated transcriptional control of NOSTRIN.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Binding Sites
  • Caveolin 1 / metabolism
  • Cells, Cultured
  • DNA-Binding Proteins
  • Endothelial Cells / drug effects
  • Endothelial Cells / enzymology*
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Nitric Oxide / metabolism*
  • Nitric Oxide Synthase Type III / antagonists & inhibitors
  • Nitric Oxide Synthase Type III / genetics
  • Nitric Oxide Synthase Type III / metabolism*
  • Phosphorylation
  • Platelet Endothelial Cell Adhesion Molecule-1 / genetics
  • Platelet Endothelial Cell Adhesion Molecule-1 / metabolism*
  • Promoter Regions, Genetic
  • Protein Transport
  • RNA Interference
  • Recombinant Fusion Proteins / metabolism
  • STAT3 Transcription Factor / metabolism*
  • Signal Transduction* / drug effects
  • Time Factors
  • Transcriptional Activation

Substances

  • Adaptor Proteins, Signal Transducing
  • Cav1 protein, mouse
  • Caveolin 1
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • Intracellular Signaling Peptides and Proteins
  • NOSTRIN protein, human
  • Platelet Endothelial Cell Adhesion Molecule-1
  • Recombinant Fusion Proteins
  • STAT3 Transcription Factor
  • STAT3 protein, human
  • Stat3 protein, mouse
  • Nitric Oxide
  • NOS3 protein, human
  • Nitric Oxide Synthase Type III
  • Nos3 protein, mouse