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PLCG1 — VEGFA

Pathways - manually collected, often from reviews:

• NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2: VEGFR1/2 (dimer)/VEGFA (dimer) complex (VEGFA-FLT1-KDR) → PLCgamma1 (PLCG1) (modification, activates) Huang et al., Int J Biochem Cell Biol 2001*, Cunningham et al., Biochem Biophys Res Commun 1997
  Evidence: assay, physical interaction
• Reactome Reaction: PLCG1 → VEGFA (indirect_complex) Takahashi et al., EMBO J 2001*, McLaughlin et al., Am J Physiol Cell Physiol 2001*, Serrano et al., J Immunol 2005, Gresset et al., J Biol Chem 2010*
• Reactome Reaction: PLCG1 → VEGFA (reaction) Takahashi et al., EMBO J 2001*, McLaughlin et al., Am J Physiol Cell Physiol 2001*

Text-mined interactions from Literome

Bernatchez et al., Br J Pharmacol 2001 : 2. Using specific inhibitors and Western blot analysis, we herein report that in bovine aortic endothelial cells ( BAEC ), VEGF induces the synthesis of PAF through the cascade activation of Flk-1 receptor, phospholipase Cgamma ( PLCgamma ) , protein kinase C ( PKC ) and p42/44 mitogen activated protein kinases ( MAPK )
Ito et al., Angiogenesis 1999 : In accordance, VEGF induced tyrosine phosphorylation of phospholipase Cgamma ( PLCgamma ) and DNA synthesis were augmented by heparin
Eun et al., Biochem Biophys Res Commun 2004 : Our biochemical assays indicated that sanguinarine strongly suppressed basal and VEGF induced Akt phosphorylation, while it did not produce any changes in VEGF induced activation of ERK1/2 and PLCgamma1
Sakurai et al., Proc Natl Acad Sci U S A 2005 : Recently, we showed that, among tyrosine residues of KDR, tyrosine residues 1175 ( Y1175, corresponding to Y1173 in murine Flk-1 ) and Y1214 ( Y1212 in Flk-1 ) are autophosphorylated in response to VEGF, and that Y1175 is important for VEGF dependent phospholipase Cgamma/PKC/mitogen activated protein kinase activation leading to DNA synthesis in cultured endothelial cells
Leung et al., Blood 2006 : Moreover, loss of gng2 function inhibits the ability of VEGF to promote the angiogenic sprouting of blood vessels by attenuating VEGF induced phosphorylation of phospholipase C-gamma1 ( PLCgamma1 ) and serine/threonine kinase ( AKT )
Kamiyama et al., Oncol Res 2008 : VEGF stimulated phosphorylation of VEGF receptor 2 (VEGFR2), phospholipase Cgamma-1 ( PLCgamma1 ), and p44/42 MAP kinases ( ERK ) was inhibited by EPQB in a dose dependent manner, and in vitro assay using kinase domain of VEGFR2 showed that EPQB covalently bound and inhibited the VEGFR2 kinase
Tahir et al., Cancer Biol Ther 2009 (Prostatic Neoplasms) : Downregulation of cav-1 in prostate cancer cell line PC-3 or human umbilical vein endothelial cells ( HUVECs ) through cav-1 siRNA significantly reduced basal and VEGF stimulated phosphorylation of VEGFR2 ( Y951 ), PLCgamma1 ( Y783 ) and/or Akt ( S473 & T308 ) relative to those in control siRNA treated cells ... Interestingly, treatment of HUVECs with cav-1 scaffolding domain ( CSD ) caused significant reduction in the VEGF stimulated phosphorylation of VEGFR2, PLCgamma1 and Akt suggesting that CSD inhibits cav-1 mediated angiogenic signaling
Li et al., Mol Biol Rep 2012 (MAP Kinase Signaling System) : Moreover, VEGF ( 165 ) induced phosphorylation of VEGFR-2, PLC-?1 , PKC-a, MEK, and p44/42 MAPK ( ERK1/2 ) in a time dependent manner