Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor

Mario B. Marrero, Bernhard Schieffer, William G. Paxton, Lauri Heerdt, Bradford C. Berk, Patrick Delafontaine, Kenneth E. Bernstein

Research output: Contribution to journalArticlepeer-review

654 Scopus citations


THE peptide angiotensin II is the effector molecule of the renin-angiotensin system. All the haemodynamic effects of angiotensin II, including vasoconstriction and adrenal aldosterone release, are mediated through a single class of cell-surface receptors known as AT1 (refs 1, 2). These receptors contain the structural features of the G-protein-coupled receptor superfamily3. We show here that angiotensin II induces the rapid phosphorylation of tyrosine in the intracellular kinases Jak2 and Tyk2 in rat aortic smooth-muscle cells and that this phosphorylation is associated with increased activity of Jak2. The Jak family substrates STAT1 and STAT2 (for signal transducers and activators of transcription) are rapidly tyrosine-phosphorylated in response to angiotensin II. We also find that Jak2 co-precipitates with the AT1, receptor, indicating that G-protein-coupled receptors may be able to signal through the intracellular phosphorylation pathways used by cytokine receptors4,5.

Original languageEnglish (US)
Pages (from-to)247-250
Number of pages4
Issue number6528
StatePublished - May 18 1995

ASJC Scopus subject areas

  • General


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