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

44 Citations (Scopus)

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

Fingerprint

Caveolin 1
Phosphorylation
Nitric Oxide Synthase Type III
Detergents
Solubility
Tyrosine
Association reactions
Endothelial cells
Endothelial Cells
Bradykinin
Phosphoric Monoester Hydrolases
Chemical activation
Histamine Agonists
Caveolae
Calmodulin
Protein-Tyrosine Kinases
Histamine
Catalyst activity
Adenosine Triphosphate
Enzymes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Caveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation. / Venema, Virginia J.; Zou, Rong; Ju, Hong; Marrero, Mario B; Venema, Richard C.

In: Biochemical and Biophysical Research Communications, Vol. 236, No. 1, 09.07.1997, p. 155-161.

Research output: Contribution to journalArticle

Venema, Virginia J. ; Zou, Rong ; Ju, Hong ; Marrero, Mario B ; Venema, Richard C. / Caveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation. In: Biochemical and Biophysical Research Communications. 1997 ; Vol. 236, No. 1. pp. 155-161.
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