Activation of mitogen-activated protein kinase in freshly isolated rat hepatocytes by both a calcium- and a protein kinase C—dependent pathway☆
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2008, NeuroImmune BiologyCitation Excerpt :DAG activates a Ca2+-phospholipid-dependent protein kinase (PK) C that phosphorylates and alters the activity of certain cellular proteins including cyclic AMP (cAMP) response element-binding protein (CREB) [21,23]. In addition to the classic system, the phospholipase A2–arachidonic acid system and the tyrosine kinase phosphorylation system are also involved [19,20,22]. The β-ARs couple with stimulatory G proteins (Gs proteins) to activate adenylate cyclase (AC).
Signalling mechanisms regulating lipolysis
2006, Cellular SignallingSynergistic activation of mitogen-activated protein kinase by insulin and adenosine triphosphate in liver cells: Permissive role of Ca<sup>2+</sup>
2003, Metabolism: Clinical and ExperimentalCitation Excerpt :This hypothesis also offers an explanation for the synergistic effect of insulin on ATP-induced MAPK stimulation observed in the present study. Indeed, for both Gq-coupled receptor agonists and insulin, MAPK activation may implicate PKC-dependent pathways in hepatocytes,6 as in other cells.40 It is therefore possible that convergent stimulation of MAPK, through different PKC isoforms induced by insulin and ATP, explains the synergy of the 2 hormones at that level in HTC cells.
Effects of Ca<sup>2+</sup> influx through nonselective cation channel on noradrenaline-induced mitogenic responses
2002, European Journal of Pharmacology
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Supported by Grant No. MT-10804 from the Medical Research Council of Canada.
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Present address: A.R., Department of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, MA 02115.