Gene interactions and pathways from curated databases and text-mining

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IGF1 — NUP43

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
McBain et al., Metabolism 2003 : IGF-1 induced a transient activation of p42/44 MAPK, with peak activation at 15 minutes in cells exposed to 5 mmol/L glucose ; however, no increase in p42/44 MAPK was evident at the higher glucose concentration of 20 mmol/L
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
Grzelkowska-Kowalczyk et al., Cell Mol Biol Lett 2010 : IGF-I caused the phosphorylation of PKB ( an approximate 8-fold increase above the basal value after 40 min of IGF-I treatment ), p42(MAPK) ( a 2.81-fold increase after 50 min ), and the activation of p70 ( S6k ) and p90 ( rsk ), manifesting as gel mobility retardation ... Pretreatment of myogenic cells with IL-1beta did not modify the IGF-I stimulated phosphorylation of PKB, p70 ( S6k ), p42(MAPK) and p90 ( rsk )
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
Hunter et al., Ciba Found Symp 1985 (Cell Transformation, Viral) : IGF I and insulin, whose receptors also have ligand stimulated protein-tyrosine kinase activity, induce p42 phosphorylation in appropriate cells
Porras et al., Mol Endocrinol 1998 : These results indicate that MEK mediates the IGF-I/insulin induced p42/ p44 MAPK activation
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
Putz et al., Cancer Res 1999 (Prostatic Neoplasms) : p42/ERK2 in DU145 cells is highly responsive to IGF-I stimulation, whereas no effect of IGF-I on p42/ERK2 can be measured in LNCaP cells