BRIEF REVIEWSThe Importance of Tyrosine Phosphorylation in Angiotensin II Signaling
Section snippets
• Protein Phosphorylation and Dephosphorylation
The existence of regulatory kinases was suggested by Fischer and Krebs (1955)and Rall et al. (1957)when they observed both an active phosphorylated and an inactive dephosphorylated form of the enzyme glycogen phosphorylase. Ten years later, the first protein kinase isolated was the cAMP-dependent protein kinase, PKA (Walsh et al. 1968). An enormous number of other protein kinases and phosphoprotein phosphatases have now been characterized; it is predicted that there are over a thousand such
• Angiotensin II Stimulated Activation of Phospholipase C
Our group has investigated the role of angiotension II-induced tyrosine phosphorylation in three separate signaling pathways. One pathway is the activation of PLC, leading to the intracellular generation of 1,4,5-IP3 and diacylglycerol. This signaling pathway is activated almost immediately upon ligand binding and serves as the stimulus for many downstream signaling events, including the very rapid release of intracellular calcium stores (Berridge 1987). To understand this basic signaling
• Angiotensin II and the Jak-STAT Pathway
In 1992, Dr. Arnold Katz published an article entitled “Is Angiotensin II a Growth Factor Masquerading as a Vasopressor?” (Katz et al. 1992). This article underlined a host of observations owing that angiotensin II acts as a smooth muscle growth factor both in vivo and in vitro. For instance, in RASM cells, Chiu et al. (1991)showed that adding angiotensin II (10−7M) to quiescent cells increased protein synthesis 45% and DNA synthesis 56% after 24 h (Chiu et al. 1991). Both responses were
• Angiotensin II and the Ras Pathway
The best understood signaling pathway associated with cell growth is activated when ligands such as PDGF bind to their cell surface receptors. These receptors contain intracellular kinase domains, which become active and lead to a cascade of protein phosphorylation events (Pimental 1994, Van Der Geer et al. 1994). Central to this cascade is the membrane-associated protein Ras. Ras is similar to heterotrimeric G proteins in that it becomes activated when bound GDP is exchanged with GTP (Bollag
• Conclusion
Until very recently, the importance of protein phosphorylation in signaling cascades initiated by seven-transmembrane receptors had not been fully appreciated. Our data strongly suggest that within minutes of ligand binding to the AT1 receptor, protein tyrosine phosphorylation plays a major role in PLC-γ1, Jak-STAT, and Ras signaling pathway activation. At present, the exact biochemical role of heterotrimeric G-protein components in this activation is not fully understood. The exact
Acknowledgements
This work was supported by National Institute of Health grants DK39777, DK44280, and DK45215, as well as Grants-In-Aid from the American Heart Association and the Georgia affiliate of the American Heart Association. M.B.M. is an American Heart Association Minority Developmental Award Scientist.
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