Electroporation of pp60c-src antibodies inhibits the angiotensin II activation of phospholipase C-γ1 in rat aortic smooth muscle cells

Mario B Marrero, Bernhard Schieffer, William G. Paxton, Elisabeth Schieffer, Kenneth E. Bernstein

Research output: Contribution to journalArticle

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Abstract

Our previous study has shown that angiotensin II induces the rapid tyrosine phosphorylation and activation of phospholipase C-γ1 in cultured rat aortic smooth muscle (RASM) cells (Marrero, M. B., Paxton, W. G., Duff, J. L., Berk, B. C., and Bernstein, K. E. (1994) J. Biol. Chem. 269, 10935-10939). This signaling pathway is initiated by ligand binding to the AT1 receptor, a cell surface G protein-coupled receptor. Antibodies to pp60c-Src were introduced into RASM cells by electroporation. Angiotensin II-stimulated tyrosine phosphorylation of phospholipase C-γ1 was eliminated by the anti-pp60c-src antibodies but not by anti-mouse IgG or bovine serum albumin. Angiotensin II also induced the rapid tyrosine phosphorylation of pp120, a known pp60c-src kinase substrate, and this phosphorylation was also specifically inhibited by anti-pp60c-arc antibodies. Electroporation of RASM cells with anti-pp60c-src antibodies had no effect on platelet-derived growth factor-stimulated tyrosine phosphorylation of PLC-γ1. Anti-pp60c-src also reduced the angiotensin II-stimulated inositol 1,4,5-trisphosphate production by 78%, while it had no effect on the platelet-derived growth factor-stimulated inositol 1,4,5-trisphosphate production. These data provide the first evidence for a direct involvement of pp60c-src kinase in angiotensin II-mediated PLC-γ1 phosphorylation and activation. Furthermore, it also describes a pathway in which a seven-transmembrane receptor can stimulate an intracellular tyrosine kinase.

Original languageEnglish (US)
Pages (from-to)15734-15738
Number of pages5
JournalJournal of Biological Chemistry
Volume270
Issue number26
DOIs
StatePublished - Jun 30 1995

Fingerprint

Phosphorylation
Electroporation
Type C Phospholipases
Angiotensin II
Smooth Muscle Myocytes
Muscle
Rats
Chemical activation
Cells
Tyrosine
Antibodies
Inositol 1,4,5-Trisphosphate
src-Family Kinases
Platelet-Derived Growth Factor
Programmable logic controllers
Bovine Serum Albumin
G-Protein-Coupled Receptors
Protein-Tyrosine Kinases
Membrane Proteins
Immunoglobulin G

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Electroporation of pp60c-src antibodies inhibits the angiotensin II activation of phospholipase C-γ1 in rat aortic smooth muscle cells. / Marrero, Mario B; Schieffer, Bernhard; Paxton, William G.; Schieffer, Elisabeth; Bernstein, Kenneth E.

In: Journal of Biological Chemistry, Vol. 270, No. 26, 30.06.1995, p. 15734-15738.

Research output: Contribution to journalArticle

Marrero, Mario B ; Schieffer, Bernhard ; Paxton, William G. ; Schieffer, Elisabeth ; Bernstein, Kenneth E. / Electroporation of pp60c-src antibodies inhibits the angiotensin II activation of phospholipase C-γ1 in rat aortic smooth muscle cells. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 26. pp. 15734-15738.
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