Caveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation

Virginia J. Venema, Rong Zou, Hong Ju, Mario B Marrero, Richard C Venema

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

Caveolin-1 and endothelial nitric oxide synthase (eNOS) are associated within endothelial caveolae. We have shown previously that eNOS is translocated to the detergent-insoluble, cytoskeletal fraction of bovine aortic endothelial cells (BAEC) in response to bradykinin (BK)-stimulation or tyrosine phosphatase inhibition. In the present study, we have examined whether caveolin-1 is similarly translocated in response to these or other stimuli. Exposure of BAEC to the eNOS-activating agonists, BK, histamine, or ATP produces transient increases in the amounts of detergent-insoluble caveolin-1. Increases in insolubility are blocked by tyrosine kinase inhibitors and are potently mimicked by tyrosine phosphatase inhibitors. Increased insolubility is accompanied by an increased association of caveolin-1 with eNOS and inhibition of eNOS catalytic activity. Agonist-activation of eNOS in endothelial cells thus appears to involve tyrosine phosphorylation-dependent changes in the interaction of eNOS with caveolin-1. Increased interaction of eNOS with caveolin-1 may deactivate the enzyme subsequent to its activation by Ca2+/calmodulin.

Original languageEnglish (US)
Pages (from-to)155-161
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume236
Issue number1
DOIs
StatePublished - Jul 9 1997

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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