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EPHB2 — IGF2

Text-mined interactions from Literome

Dews et al., Endocrinology 2000 : The type 1 insulin-like growth factor receptor ( IGF-IR ) activates the extracellular signal regulated kinases ( ERK1 and -2 )
Kurihara et al., Endocr J 2000 (Neuroblastoma) : PD98059 inhibited activation of Erk and LY294002 repressed activation of Akt in response to IGF-I, but did not affect tyrosine phosphorylation of the IGF-IR , IRS-1, IRS-2, or Shc
Tsakiridis et al., Biochem Biophys Res Commun 2001 (MAP Kinase Signaling System) : ERK activation by insulin, IGF-I , or PDGF was unaffected by the phosphatidylinositol 3-kinase inhibitor wortmannin but was abolished by the MEK inhibitor PD98059
Wittrock et al., Anticancer Res 2002 (MAP Kinase Signaling System...) : Stimulation of neuroblastoma cells with IGF-II leads to an increased activity of the MAP-kinase Erk1 , an induction of N-myc expression and an enhanced proliferation rate
Duplomb et al., Endocrinology 2003 : Confirming this idea, ERK1/2 and AKT/protein kinase B, the kinases necessary for cell proliferation and survival, were activated by IGF-II alone or by the association of IL-6-type cytokines and IGF-II ... Activation of ERK1/2 and AKT by IGF-II thus appears essential to sustain cellular expansion driven by IL-6-type cytokines
Kwon et al., J Invest Dermatol 2004 (MAP Kinase Signaling System...) : Particularly, we determined that phosphorylation of ERK2 but not p38 and JNK1/2 was activated by IGF-II in a time dependent manner
Sivaprasad et al., Endocrinology 2004 (MAP Kinase Signaling System) : Although ERK 1/2 was maximally stimulated by TGFalpha between 5 and 15 min, IGF-I did not stimulate discernible activation of ERK 1/2
El-Shewy et al., Mol Endocrinol 2004 : In human embryonic kidney 293 cells, IGF-I triggered proteolysis of heparin binding (HB)-EGF, increased tyrosine autophosphorylation of EGF receptors, stimulated EGF receptor inhibitor ( AG1478 ) -sensitive ERK1/2 phosphorylation, and promoted EGF receptor endocytosis
Kim et al., J Invest Dermatol 2004 (MAP Kinase Signaling System) : These results suggest that IGF-II induces COX-2 expression through the tyrosine kinase-Src-ERK and tyrosine kinase-PI3-kinase pathways, but not via p38 MAPK pathway, and that the basal JNK activity is required for the upregulation of COX-2 by IGF-II, as well
Alexia et al., Ann N Y Acad Sci 2004 (Carcinoma, Hepatocellular...) : Role of constitutively activated and insulin-like growth factor stimulated ERK1/2 signaling in human hepatoma cell proliferation and apoptosis : evidence for heterogeneity of tumor cell lines ... Altogether, our data demonstrate the heterogeneous response of human hepatoma cells to an IGF stimulus and suggest ( 1 ) that auto/paracrine effects of IGF-I/-II might contribute to the proliferation of HCC cells and to their protection against apoptosis in vivo and ( 2 ) that drug induced activation of ERK1/2 plays a role in drug induced apoptosis in human hepatoma cells
Hwang et al., Toxicology 2007 : Compared with AAP treatment alone, IGF-I and AAP co-treatment increased ERK1/2 phosphorylation but inhibited PARP cleavage
Ogura et al., J Toxicol Sci 2007 : After induction of differentiation in the presence of 1 microM simvastatin for 2 days, IGF-1 induced activation of ERK1/2 and Akt was significantly decreased
El-Shewy et al., J Biol Chem 2007 (MAP Kinase Signaling System) : Only IGF-1 and IGF-2 potently activated ERK1/2 ... In contrast, IGF-2 receptor knockdown markedly reduced IGF-2 stimulated ERK1/2 phosphorylation, with no effect on the IGF-1 response ... These data indicate that endogenous IGF-1 and IGF-2 receptors can independently initiate ERK1/2 signaling and point to a potential physiologic role for IGF-2 receptors in the cellular response to IGF-2
Lerner-Marmarosh et al., Proc Natl Acad Sci U S A 2008 (MAP Kinase Signaling System) : hBVR is a nuclear transporter of ERK ; experiments with hBVR nuclear export signal (NES) and nuclear localization signal ( NLS ) mutants demonstrated its critical role in the nuclear localization of IGF stimulated ERK for Elk1 activation
Li et al., J Biol Chem 2009 (Hypertrophy) : 3 ) Unlike PP2, pNaKtide does not affect IGF induced ERK activation in cardiac myocytes
Carter et al., J Cell Sci 2009 : Exogenous IGF-2 increased MHC levels, myogenic E box promoter-reporter activity, ERK5 phosphorylation and kinase activity, and rapidly induced nuclear localisation of ERK5
Yin et al., J Biol Chem 2009 : In normal human chondrocytes, IGF-I initiated a strong and sustained phosphorylation of IRS-1 ( Tyr-612 ) and Akt ( Ser-473 ) and transient ERK phosphorylation
Wang et al., Invest Ophthalmol Vis Sci 2010 : Rat lens epithelial explants were used to compare the ability of vitreous, IGF-1 , PDGF-A, EGF, and FGF-2 to stimulate the phosphorylation of ERK1/2 and Akt leading to fiber differentiation, in the presence or absence of selective receptor tyrosine kinase ( RTK ) inhibitors ... Similar to vitreous, FGF induced a sustained ERK1/2 signaling profile, unlike IGF , PDGF, and EGF, which induced a more transient ( shorter ) activation of ERK1/2
Denner et al., Endocrinology 2010 : The aim of the present study was to investigate IGF stimulated ERK signaling regulating P450scc gene expression in the immortalized porcine granulosa cell line JC-410 ... Inhibition of ERK phosphorylation with U0126 [ 1,4-diamino-2,3-dicyano-1,4-bis ( o-aminophenylmercapto ) butadiene ] blocked IGF-I induction of IGF response element reporter gene activity
Zhang et al., Neurochem Res 2011 : Furthermore, IGF-1 increased the phosphorylation of Akt and ERK1/2
Jiang et al., Am J Physiol Endocrinol Metab 2011 (MAP Kinase Signaling System) : In carp pituitary cells, IGF-I and -II could induce rapid phosphorylation of IGF-I receptor, MEK1/2, ERK1/2 , MKK3/6, and p38 MAPK ; and SLa and SLß secretion, protein production, and mRNA expression caused by IGF-I and -II stimulation were negated by inactivating MEK1/2 and p38 MAPK ... In carp pituitary cells, IGF-I and -II could induce rapid phosphorylation of IGF-I receptor, MEK1/2, ERK1/2 , MKK3/6, and p38 MAPK ; and SLa and SLß secretion, protein production, and mRNA expression caused by IGF-I and -II stimulation were negated by inactivating MEK1/2 and p38 MAPK
Ohashi et al., Cancer Sci 2012 (Biliary Tract Neoplasms) : BMS-536924 blocked autophosphorylation of IGF-IR and both Akt and ERK activation by both IGF-I and insulin
Ku et al., Mol Nutr Food Res 2012 : Pretreatment with antiserum against the EGCG receptor ( also known as the 67-kDa laminin receptor ; 67LR ), but not with an adenosine monophosphate ( AMP ) -activated protein kinase ( AMPK ) inhibitor, prevented the inhibitory actions of EGCG on IGF-I- and IGF-II stimulated ERK1/2 phosphorylation and subsequent preadipocyte proliferation
Schmeisser et al., J Neurosci 2012 (Learning Disorders) : This process depends on Igf2/Igf2R mediated MEK/ERK activation
Fujita et al., J Biol Chem 2013 : Inhibitors of IGF1R, Src, AKT, and ERK1/2 did not suppress avß3-IGF-IGF1R ternary complex formation, suggesting that activation of these kinases are not required for ternary complex formation
Geng et al., J Clin Invest 1996 : However, ERK was also activated by PDGF, IGF-1 , and IL-6
Chaudhary et al., Mol Cell Biochem 1998 : Mainly ERK2 was rapidly activated ( within 10 min ) by bFGF, IGF-I and PDGF-BB in normal HOB, HBMS and human osteosarcoma cells, whereas both ERK1 and ERK2 were activated by growth factors in rat osteoblast-like cell lines, ROS 17/2.8 and UMR-106
Putz et al., Cancer Res 1999 (Prostatic Neoplasms) : We have studied the effects of EGF, IGF-I , and the protein kinase A (PKA) activator forskolin on the activation of p42/ extracellular signal regulated kinase ( ERK ) 2, which is a key kinase in mediation of growth factor induced mitogenesis in prostate cancer cells