PMID: 11914123Mar 27, 2002Paper

Ca2+-mediated activation of ERK in hepatocytes by norepinephrine and prostaglandin F2 alpha: role of calmodulin and Src kinases

BMC Cell Biology
O MelienT Christoffersen

Abstract

Previous studies have shown that several agents that stimulate heptahelical G-protein coupled receptors activate the extracellular signal regulated kinases ERK1 (p44mapk) and ERK2 (p42mapk) in hepatocytes. The molecular pathways that convey their signals to ERK1/2 are only partially clarified. In the present study we have explored the role of Ca2+ and Ca2+-dependent steps leading to ERK1/2 activation induced by norepinephrine and prostaglandin (PG)F2alpha. Pretreatment of the cells with the Ca2+ chelators BAPTA-AM or EGTA, as well as the Ca2+ influx inhibitor gadolinium, resulted in a partial decrease of the ERK response. Furthermore, the calmodulin antagonists W-7, trifluoperazine, and J-8 markedly decreased ERK activation. Pretreatment with KN-93, an inhibitor of the multifunctional Ca2+/calmodulin-dependent protein kinase, had no effect on ERK activation. The Src kinase inhibitors PP1 and PP2 partially diminished the ERK responses elicited by both norepinephrine and PGF2alpha. The present data indicate that Ca2+ is involved in ERK activation induced by hormones acting on G protein-coupled receptors in hepatocytes, and suggest that calmodulin and Src kinases might play a role in these signaling pathways.

Citations

Mar 11, 2005·Human Molecular Genetics·Michael D KaytorHarry T Orr
Oct 28, 2005·American Journal of Physiology. Cell Physiology·Karni S MoshalSuresh C Tyagi
Jun 3, 2011·Headache·Saurabh GuptaNancy E J Berman
Mar 3, 2004·Journal of Neuroscience Research·Jin ZhongWei-Hua Lee
Mar 20, 2010·Canadian Journal of Physiology and Pharmacology·Ting Zhang, Qingping Feng
Jun 9, 2005·Experimental Eye Research·Lixin WangGeorge Duncan
Apr 29, 2015·Chemical Research in Toxicology·Gati Krushna PanigrahiMukul Das

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