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Details on Person Following tyrosine phosphorylation and activation, PLCG1 dis...

Class:IdSummation:4420175
_displayNameFollowing tyrosine phosphorylation and activation, PLCG1 dis...
_timestamp2014-01-10 16:32:18
created[InstanceEdit:4420157] Garapati, P V, 2013-08-30
literatureReference[LiteratureReference:195484] A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells
[LiteratureReference:5218539] VEGF activates protein kinase C-dependent, but Ras-independent Raf-MEK-MAP kinase pathway for DNA synthesis in primary endothelial cells
[LiteratureReference:5218512] Characterization of vascular endothelial growth factor's effect on the activation of protein kinase C, its isoforms, and endothelial cell growth
modified[InstanceEdit:5218600] Garapati, P V, 2013-12-19
[InstanceEdit:5228340] Jupe, S, 2014-01-10
textFollowing tyrosine phosphorylation and activation, PLCG1 dissociates from the VEGFR2 receptor and associates with its substrate phosphatidylinositol (4,5)-bisphosphate (PIP2) in the plasma membrane. PLCG1 hydrolyses PIP2 resulting in the generation of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG is an activator of PKC which leads to subsequent activation of MAP kinase, resulting in increased endothelial cell proliferation. IP3 acts upon receptors in the endoplasmic reticulum causing release of intracellular calcium. Elevation of cytosolic Ca2+ stimulates eNOS to produce nitric oxide (NO) causing vascular dilation. Entry of extracellular calcium through specific channels is important for the activation of certain proteins (Takahashi et al. 2001, Takahashi et al. 1999, Xia et al. 1996).
(summation)[Reaction:4420202] PLCG1 disassociates from VEGFR2 and translocate to PM [Homo sapiens]
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