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EPHB2 — PGF

Text-mined interactions from Literome

Rao et al., J Biol Chem 1999 : These findings demonstrate that 1 ) PI3-kinase dependent and independent mechanisms appear to be involved in PGF2alpha induced activation of ERK2 ; 2 ) PGF2alpha induced eIF4E and 4E-BP1 phosphorylation appear to be mediated by both ERK dependent and PI3-kinase dependent rapamycin-sensitive mechanisms ; and 3 ) ERK dependent eIF4E phosphorylation but not PI3-kinase dependent p70 ( S6k ) activation correlates with PGF2alpha induced global protein synthesis and bFGF-2 expression in VSMC
Caverzasio et al., J Bone Miner Res 2000 : In contrast to their implication in epidermal growth factor (EGF) receptor tyrosine kinase signaling, the adaptor protein Shc, the Grb2/Sos complex, and the small G protein Ras were not involved in the activation of Erk induced by either LPA or PGF2alpha in MC3T3-E1 cells, suggesting that activation of Erk by Gi and Gq protein coupled receptors is Ras independent in these cells
Chen et al., Endocrinology 2001 : By using a PKC inhibitor and a PKC-deficient luteal cell model, we observed that phorbol ester-responsive isoforms of PKC were required for ERK phosphorylation and activation by PGF2alpha ( 1 microM ) or phorbol 12-myristate 13-acetate ( PMA ) ( 20 nM ) ... PGF2alpha induced ERK phosphorylation was dose-dependently inhibited by the MEK1 inhibitor PD098059 ( 1-50 microM )
Ahmed et al., Mol Endocrinol 2003 : In TMOb cells, stimulation of endogenous Gs/Gq coupled PTH receptors, Gq-coupled PGF2 alpha receptors, and Gi/Gq coupled lysophosphatidic acid receptors, but not Gs-coupled PGE2 receptors, caused a rapid 5- to 10-fold increase in ERK1/2 phosphorylation
Dekanty et al., J Biol Chem 2006 : However, LIF and PGF2alpha can trigger increases in ERK1/2 activity, which are required for their mitogenic responses because U0126, a MEK1/2 inhibitor, prevents both ERK1/2 activation and induction of DNA synthesis by LIF or PGF2alpha treatment
Arvisais et al., J Biol Chem 2006 : It is established that PGF2alpha binds to a G-proteincoupled receptor ( GPCR ) to stimulate protein kinase C ( PKC ) and Raf-MEK-Erk signaling in luteal cells
Krishnaswamy et al., Endocrinology 2010 : Because LY294002 did not affect ERK1/2 phosphorylation, but inhibited PGF ( 2 alpha ) production and down-regulated COX2 expression, it is likely that the Akt pathway is also involved in PGF ( 2 alpha ) production
Rice et al., Ann Clin Lab Sci 2010 : These findings suggest that aging does not affect the ability of the rat aorta to activate ERK ( 1/2 ) -, p38-MAPK, and JNK-MAPK phosphorylation in response to PGF2alpha stimulation
Chang et al., Int Endod J 2010 (Second Messenger Systems) : PGF ( 2alpha ) induced both ERK and CREB/ATF-1 phosphorylation in pulp cells
Goupil et al., J Biol Chem 2010 (Obstetric Labor, Premature) : In contrast to its negative allosteric modulating effects on Rho/ROCK signaling, PDC113.824 acted as a positive allosteric modulator on PGF2alpha mediated protein kinase C and ERK1/2 signaling
Taylor et al., Br J Cancer 2010 (Breast Neoplasms) : In the presence of PlGF , BP-1 decreased cellular motility, reversed ERK1/2 phosphorylation, and decreased nuclear and peripheral pERK1/2
Tveteraas et al., J Exp Clin Cancer Res 2012 (Carcinoma, Hepatocellular...) : In the MH1C1 hepatocarcinoma cells, stimulation with PGE2 or PGF2a caused phosphorylation of the EGFR, Akt, and ERK , which could be blocked by the EGFR tyrosine kinase inhibitor gefitinib
Kunapuli et al., J Biol Chem 1998 (Cardiomegaly) : Moreover, PGF2alpha causes a robust activation ( approximately 50-fold ) of Erk2 , whereas 8,12-iso-iPF2alpha-III has no effect