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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-05

AUTHORS

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

ABSTRACT

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. More... »

PAGES

247-250

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/375247a0

DOI

http://dx.doi.org/10.1038/375247a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037354896

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7746328


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