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GSK3B — IGF1

Text-mined interactions from Literome

Lesort et al., Neuroscience 2000 : These effects were completely inhibited by lithium, revealing that the insulin and insulin-like growth factor-1 induced changes in tau phosphorylation were mediated by glycogen synthase kinase-3beta
Desbois-Mouthon et al., Oncogene 2001 (Carcinoma, Hepatocellular) : This study provides the first evidence that insulin and IGF-1 stimulate the beta-catenin pathway through two signalling cascades bifurcating downstream of PI 3-K and involving GSK-3beta inhibition and Ras activation
Leung-Hagesteijn et al., EMBO J 2001 : Catalytically active, but not mutant ILKAP, strongly inhibited insulin-like growth factor-1 stimulated GSK3beta phosphorylation on Ser9, but did not affect phosphorylation of PKB on Ser473, suggesting that ILKAP selectively affects ILK mediated GSK3beta signalling
Satyamoorthy et al., Cancer Res 2001 (Disease Progression...) : IGF-1 also activated Akt, inhibited its down-stream effector GSK3-beta , and stabilized beta-catenin
Vyas et al., Am J Physiol Cell Physiol 2002 (Hypertrophy...) : LY-294002 ( 100 microM ) and wortmannin ( 150 microM ), specific inhibitors of phosphatidylinositol 3'-kinase, attenuated IGF-I induced GSK-3beta phosphorylation by 67 and 92 %, respectively ... IGF-I suppressed the kinase activity of GSK-3beta
Liu et al., Endocrinology 2002 : IGF-I increased the phosphorylation of glycogen synthase kinase 3beta , BAD, FKHR, and p70 ( S6 ) kinase
Frago et al., Endocrinology 2002 : Phosphorylation of Akt and Bad was stimulated in areas where IGF-I was increased , with no change in MAPK or glycogen synthase kinase-3beta
Linseman et al., J Neurochem 2003 : In contrast to lithium, MEF2D hyperphosphorylation was not inhibited by forskolin, insulin-like growth factor-I , or valproate, three mechanistically distinct inhibitors of GSK-3 beta
Seimi et al., Circ J 2004 (Cardiomegaly) : The phosphatidylinositol (PI) 3-kinase/Akt/GSK-3 beta signaling induced by IGF-1 was investigated using inhibitors of PI 3-kinase and Ad AktAA, a dominant negative form of Akt
Lin et al., Mol Cell Endocrinol 2004 : Further IGF-I was able to sustain Akt activity and thus preventing GSK-3beta activation in the presence of DHEA
Bondy et al., Eur J Pharmacol 2004 : The identification of GSK3beta as a major target of brain IGF1 signaling provides a unifying pathway for IGF1 's well established anabolic and anti-apoptotic functions, with IGF1 induced inhibition of GSK3beta triggering multifaceted anabolic and neuroprotective effects
Kuemmerle et al., Am J Physiol Gastrointest Liver Physiol 2005 : The aim of the present study was to determine whether endogenous IGF-I regulates Akt dependent GSK-3 beta phosphorylation and activity and whether it regulates apoptosis in human intestinal muscle cells ... Endogenous IGF-I stimulated GSK-3 beta phosphorylation and inhibited GSK-3 beta activity ( measured by in vitro kinase assay ) in these cells ... IGF-I dependent GSK-3 beta phosphorylation and the resulting GSK-3 beta inactivation were mediated by activation of a PI3-kinase dependent, phosphoinositide dependent kinase-1 ( PDK-1 ) -dependent, and Akt dependent mechanism
Sjostrom et al., Dev Cell 2005 (Neuroblastoma) : In proliferating cerebellar granule neuron precursors ( CGNPs ), Sonic hedgehog signaling induces N-myc expression, and N-myc protein is stabilized by insulin-like growth factor mediated suppression of GSK-3beta
Jiang et al., J Cell Biochem 2006 (Hypertrophy) : The Akt/GSK-3beta , p38MAPK, and calcineurin pathways may play an important role in IGF-1 signaling, cell-cycle regulation, and matrix gene expression in mesangial cells leading to the development of diabetic glomerulopathy
Bridle et al., J Lab Clin Med 2006 : PDGF and IGF-1 also increased the levels of cyclin D1 and phospho-glycogen synthase kinase-3beta
Singh et al., International journal of biological sciences 2007 : Two dimensional gel electrophoresis followed by MALDI-TOF mass spectrometric analysis of mesangial proteins reveals that IGF-1 treatment or an inhibition of GSK-3beta increases the expression of the phosphorylated Ser/Thr binding signal adapter protein 14-3-3zeta
Frederick et al., Glia 2007 (MAP Kinase Signaling System) : GSK-3beta , a downstream target of the PI3K/Akt pathway, is phosphorylated in the presence of IGF-I in OPs
Liu et al., Carcinogenesis 2008 (Prostatic Neoplasms) : In this study, lycopene, in dietary concentrations, reversed DHT effects of 6S cells on NPE cell death, decreased 6S cell IGF-I production by reducing AR and beta-catenin nuclear localization and inhibited IGF-I stimulated NPE and PREC growth, perhaps by attenuating IGF-I 's effects on serine phosphorylation of Akt and GSK3beta and tyrosine phosphorylation of GSK3
Carter et al., Acta Neuropathol 2008 (Brain Neoplasms...) : Aspartyl (asparaginyl)-beta-hydroxylase ( AAH ) is a mediator of neuronal motility, and stimulated by insulin and IGF activation of PI3 kinase-Akt, or inhibition of GSK-3beta
Satoh et al., Neuropharmacology 2008 : Proteasomal degradation of IRS-2, but not IRS-1 by calcineurin inhibition : attenuation of insulin-like growth factor-I induced GSK-3beta and ERK pathways in adrenal chromaffin cells ... Thus, calcineurin inhibition decreased IRS-2 level via proteasomal IRS-2 degradation, attenuating IGF-I induced GSK-3beta and ERK pathways
Urbanska et al., Int J Cancer 2008 (Medulloblastoma) : Preincubation of BsB8 cells with fenofibrate attenuated IGF-I induced IRS-1, Akt, ERKs and GSK3beta phosphorylation, and inhibited clonogenic growth
Nemoto et al., J Pharmacol Sci 2009 : In cultured bovine adrenal chromaffin cells, 1 ) constitutive and negatively regulated activities of GSK-3beta up- and down-regulated insulin receptor, insulin receptor substrate-1 (IRS-1), IRS-2, and Akt levels via controlling proteasomal degradation and protein synthesis ; 2 ) nicotinic receptor/protein kinase C-alpha (PKC-alpha)/extracellular signal regulated kinase ( ERK ) pathway up-regulated IRS-1 and IRS-2 levels, enhancing insulin induced the phosphoinositide 3-kinase (PI3K)/Akt/GSK-3beta pathway ; 3 ) inhibition of calcineurin by cyclosporin A or FK506 down-regulated IRS-2 level, attenuating insulin-like growth factor-I (IGF-I) induced ERK and GSK-3beta pathways ; and 4 ) insulin, IGF-I or therapeutics ( e.g., lithium ) up-regulated the voltage dependent Na(v)1.7 sodium channel
Shanely et al., Am J Physiol Cell Physiol 2009 : The GSK-3beta inhibitor, LiCl, dramatically enhanced IGF-I induction of the 1.3-kb type IIb MyHC promoter, and constitutively active GSK-3beta attenuated IGF-I induced 1.3-kb type IIb MyHC promoter activity
Sun et al., Toxicology 2010 (Parkinson Disease) : IGF-1 treatment induced sustained phosphorylation of glycogen synthase kinase-3beta ( GSK-3beta ) as shown by western blot analysis
Wang et al., J Bone Miner Res 2010 : T ( 3 ) activates IGF-1/IGF1R signaling and IGF-1 dependent PI3K/Akt/GSK-3beta signaling in growth plate chondrocytes undergoing proliferation and differentiation to prehypertrophy
Ye et al., Glia 2010 : We found that IGF-I increases beta-catenin protein abundance within an hour after IGF-I induced phosphorylation of Akt and GSK3beta
Sugita et al., Mol Cancer Res 2010 (Neoplasm Invasiveness...) : NO donor inhibited insulin/IGF-I stimulated phosphorylation of insulin receptor/IGF-I receptor, IRS-1, Akt/PKB, and glycogen synthase kinase-3beta along with decreased expression of IRS-1 protein in MIAPaCa-2 cells, whereas NO donor enhanced the phosphorylation of extracellular signal regulated kinase-1/2
Zaouali et al., Liver Transpl 2010 (Disease Models, Animal...) : When AKT was inhibited, the effects of EGF and IGF-I on GSK3(beta) , PPAR gamma, hepatic injury and function disappeared
Wang et al., Sichuan Da Xue Xue Bao Yi Xue Ban 2010 : MTT assay was used to measure the survival rate of PC12 cells, Western blot was applied to detect tau phosphorylation level, total tau, glycogen synthase kinase-3beta ( GSK-3beta ), and phosphorylation of GSK-3beta Ser9 for observing the effect of IGF-1 or LiCl, a specific inhibitor of GSK-3beta , on Abeta induced tau protein phosphorylation in PC12 cells