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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