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IFI44 — IGF1
Text-mined interactions from Literome
Misawa et al., Cancer Res 2000
(Neuroblastoma) :
Exogenous
IGF-I induced phosphorylation and activation of extracellular signal regulated kinases
p44/42 ( ERK1 and ERK2 ), with a maximal level 30 min after the stimulation ... The MEK1 inhibitor PD98059 reduced
IGF-I mediated
p44/42 MAPKs phosphorylation and produced a parallel reduction of IGF-I stimulated N-Myc induction
Flint et al., Domest Anim Endocrinol 2002
:
But since
IGF-I did not
activate p42/p44 , a different MAP kinase, not detected by the antibody used here, is implicated
Li et al., Mol Cell Biochem 2002
(MAP Kinase Signaling System) :
In both skeletal and cardiac muscle, des
IGF-I increased the phosphorylation of Akt-1 at Ser 473 ( p < 0.01 ) with no change in the phosphorylation of
p44 and p42 MAP kinases at Thr202/Tyr204
Boehm et al., Arthritis Rheum 2007
:
Inhibition of Hsp90 with 100 nM or 500 nM geldanamycin blocked
IGF-1 induced cell proliferation, Akt and
p42/44 activation, and COL2A1 expression
Harwood et al., J Biol Chem 2008
(MAP Kinase Signaling System) :
The effect of rapamycin on
IGF-I or insulin
activation of
p44/42 was recapitulated by amino acid deprivation
Chenal et al., Eur J Neurosci 2008
:
Investigation of the putative signalling pathways leading to translation activation revealed that insulin and
IGF-1 induced
p44- and p42 MAPK, Akt and mTOR phosphorylation
Madhala-Levy et al., J Cell Physiol 2012
(MAP Kinase Signaling System) :
In cultures derived from Smo ( mut ) ( MCre ; Smo ( flox/flox ) ) mice lacking Smo expression specifically in hindlimb muscles,
IGF-I induced Akt and
p42/44 phosphorylation was significantly reduced compared to IGF-I 's effect on Smo ( cont ) cells ... In cultures derived from Smo ( mut ) ( MCre ; Smo ( flox/flox ) ) mice lacking Smo expression specifically in hindlimb muscles,
IGF-I induced Akt and
p42/44 phosphorylation was significantly reduced compared to IGF-I 's effect on Smo ( cont ) cells
Mendivil et al., Reprod Sci 2011
(Endometrial Neoplasms...) :
Treatment with AMG 479 rapidly blocked
IGF-1 induced phosphorylation of IFG-1-R, Akt, and
p44/42
Blakesley et al., J Biol Chem 1998
:
In addition, these mutant IGF-I receptors do not affect
IGF-I stimulated
p42/p44 mitogen activated protein kinase activation or phosphatidylinositol (PI) 3'-kinase activity