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GSK3B — INS

Text-mined interactions from Literome

Summers et al., J Biol Chem 1999 : To further evaluate the role of GSK3beta in insulin signaling, the GSK3beta inhibitor lithium was used to mimic the consequences of insulin stimulated GSK3beta inactivation ... These data support the hypothesis that GSK3beta contributes to insulin regulation of glycogen synthesis, but is not responsible for the increase in glucose transport
Summers et al., J Biol Chem 1999 : Similarly, in 3T3-L1 adipocytes, only insulin stimulated phosphorylation of Akt 's endogenous substrate, GSK-3beta
Williams et al., Trends Pharmacol Sci 2000 : Among the proposed mechanisms, two lithium-sensitive signal transduction pathways are active in the brain ; these are mediated by glycogen synthase kinase 3beta ( GSK-3beta ) and inositol ( 1,4,5 ) -trisphosphate [ Ins ( 1,4,5 ) P3 ] signalling
Ding et al., J Biol Chem 2000 : Differential regulation of glycogen synthase kinase 3beta by insulin and Wnt signaling ... Insulin and Wnt pathways regulate GSK3beta through different mechanisms, and therefore lead to distinct downstream events
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
Wada et al., Mol Cell Biol 2001 : In addition, insulin induced phosphorylation of GSK-3beta and activation of PP1 followed by activation of glycogen synthase and glycogen synthesis were decreased by expression of WT-SHIP2 and increased by the expression of Delta IP-SHIP2
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
Dajani et al., Cell 2001 : Glycogen synthase kinase 3 beta ( GSK3 beta ) plays a key role in insulin and Wnt signaling, phosphorylating downstream targets by default, and becoming inhibited following the extracellular signaling event
Ballou et al., J Biol Chem 2001 : Insulin induced GSK-3beta phosphorylation is mediated by the phosphatidylinositol 3-kinase/Akt signaling pathway ... PE treatment does not activate phosphatidylinositol 3-kinase or Akt ( Ballou, L. M., Cross, M. E., Huang, S., McReynolds, E. M., Zhang, B. X., and Lin, R. Z. ( 2000 ) J. Biol. Chem. 275, 4803-4809 ), but instead inhibits insulin induced Akt activation and GSK-3beta phosphorylation ... One pathway inhibits insulin induced GSK-3beta phosphorylation by blocking insulin activation of Akt
Semiz et al., Mol Cell Biochem 2002 (Diabetes Mellitus) : Diabetes, vanadium, and insulin in vivo treatment did not affect muscle GSK-3beta activity as compared to controls
Semiz et al., Mol Cell Biochem 2002 : Insulin resistance, vanadium and insulin in vivo treatment did not affect muscle GSK-3beta activity in either fatty or lean rats
Ragolia et al., J Biol Chem 2003 (Hyperglycemia) : Furthermore, we examined the effect of L-PGDS incubation on insulin stimulated Akt, glycogen synthase kinase-3beta ( GSK-3beta ), and ERK phosphorylation
Kanzaki et al., J Cell Biol 2004 : Furthermore, insulin induced GSK-3beta phosphorylation was mediated by both PI 3-kinase-PKB and the TC10-Par6-atypical PKC signaling pathways
Pérez et al., Diabetes 2004 : However, at elevated concentrations, leptin impaired insulin stimulated MAPK activity, glycogen synthase kinase (GSK)3beta phosphorylation, and insulin receptor tyrosine phosphorylation without altering vanadate stimulation ... Central administration of leptin decreased insulin effects on adipocyte MAPK and GSK3beta phosphorylation
Schubert et al., Proc Natl Acad Sci U S A 2004 (Insulin Resistance...) : Thus, lack of insulin signaling in the brain may lead to changes in Akt and GSK3 beta activity and Tau hyperphosphorylation but must interact with other mechanisms for development of Alzheimer 's disease
Gupta et al., Biochim Biophys Acta 2004 : The effects of tumor necrosis factor-alpha (TNF-alpha) on insulin induced phosphorylation of protein kinase B-alpha (PKB-alpha) and downstream enzyme glycogen synthase kinase-3 beta ( GSK-3 beta ) was examined in HepG2 liver cells ... However, long-term pretreatments of cells with TNF-alpha reduced insulin stimulated phosphorylation of PKB-alpha and GSK-3 beta
Ouwens et al., Diabetologia 2005 : HFD reduced insulin stimulated IRS1 associated phosphatidylinositol 3'-kinase activity and phosphorylation of protein kinase B, glycogen synthase kinase-3beta , endothelial nitric oxide synthase, and forkhead transcription factors by 40-60 % ( all p < 0.05 )
Longnus et al., Diabetologia 2005 : Insulin induced phosphorylation of glycogen synthase kinase 3 (GSK3) beta , p70 S6 kinase (p70S6K) ( Thr389 ) and IRS1 ( Ser636/639 ) were significantly increased following AMPK activation
Sale et al., Biochemistry 2006 : Triple antisense knock down of PKB alpha, beta, and gamma so that total PKB was < 6 % blocked insulin stimulated phosphorylation of endogenous GSK-3alpha and GSK-3beta isoforms by 67 % and 45 %, respectively, showing that GSK-3alpha and GSK-3beta are controlled by endogenous PKB ... Knock down of total PKB incompletely blocked insulin stimulated phosphorylation of GSK-3alpha and GSK-3beta , and a pathway involving atypical PKCs, zeta/lambda, was shown to contribute to the signal
Dugo et al., Crit Care Med 2006 (Inflammation...) : In vitro, insulin or TDZD-8 caused similar reductions in the nuclear factor-kappaB p65 activity and similar increases in the phosphorylation of Ser9 of glycogen synthase kinase-3beta ... We propose that the inhibitory effect of insulin on the activity of glycogen synthase kinase-3beta contributes to the protective effect of insulin against the organ injury/dysfunction caused by excessive systemic inflammation independently of any effects on blood glucose
Sugano et al., J Neurochem 2006 : Enhancement of insulin induced PI3K/Akt/GSK-3beta and ERK signaling by neuronal nicotinic receptor/PKC-alpha/ERK pathway : up-regulation of IRS-1/-2 mRNA and protein in adrenal chromaffin cells ... Thus, stimulation of nAChRs up-regulated expression of IRS-1/IRS-2 via Ca ( 2+ ) -dependent sequential activation of cPKC-alpha and ERK, and enhanced insulin induced PI3K/Akt/GSK-3beta and ERK signaling pathways
Vahsen et al., Horm Metab Res 2006 (Insulin Resistance) : Insulin regulated serine phosphorylation of Akt and GSK3alpha and GSK3beta was unaltered in heart and skeletal muscle of knockout mice, suggesting unaltered insulin signaling
Palanivel et al., Metabolism 2006 : Neither short-term ( 1 hour ) nor long-term ( 24 hours ) treatment with leptin ( 60 nmol/L ) altered basal or insulin stimulated glucose uptake and oxidation, glycogen synthesis, insulin receptor substrate 1 tyrosine, Akt, or glycogen synthase kinase 3beta phosphorylation
Nemoto et al., Brain Res 2006 : Insulin ( 100 nM for 24 h ) increased Ser ( 9 ) phosphorylation of GSK-3beta by approximately 104 %, while decreasing IRS-1 and IRS-2 levels by approximately 41 and approximately 72 % ; the insulin induced Ser ( 9 ) phosphorylation of GSK-3beta, as well as down-regulations of IRS-1 and IRS-2 levels were restored to the control levels of nontreated cells at 24 h after the washout of the insulin ( 100 nM for 12 h ) -treated cells
Ghosh et al., Endocrinology 2007 (Insulin Resistance) : Western blot analysis of L6 cell lysates demonstrated impaired insulin stimulated phosphorylation of Akt, serine/arginine-rich protein 40, and glycogen synthase kinase 3beta in response to TNFalpha and the short chain C6 ceramide analog ... Effects of TNFalpha and C6 on insulin stimulated phosphorylation of glycogen synthase kinase 3beta were prevented by myriocin and tautomycin, a PP1 inhibitor, further implicating a de novo ceramide-PP1 pathway
Eguchi et al., Mol Cell Endocrinol 2007 : However, the expected functional consequences were not observed, as we saw no change in basal or insulin stimulated glucose uptake and phosphorylation of GSK3beta , Akt ( T308 and S473 ) or ERK1/2
Xue et al., J Biol Chem 2007 (Diabetes Mellitus, Experimental...) : Insulin stimulated phosphorylation of IR, IRS proteins, Akt/protein kinase B, glycogen synthase kinase 3beta , and p70 ( S6K ) was impaired in DHet mouse muscle and liver and was differentially improved by PTP1B deficiency
Henriksen et al., Metabolism 2007 (Diabetes Mellitus, Type 2) : Maximally insulin stimulated ( 5 mU/mL ) GSK-3beta serine phosphorylation was significantly less ( 35 %, P < .05 ) in soleus muscle of ZDF rats compared with insulin-sensitive lean Zucker rats, indicating GSK-3 overactivity
Pandey et al., J Cardiovasc Pharmacol 2007 (Hypertension) : Immunoblotting revealed that hyperglycemia and PPAR-gamma inhibition significantly ( P < 0.001 ) decreased insulin stimulated insulin receptor (IR)-beta, Akt, and glycogen synthase kinase (GSK)-3beta phosphorylation, whereas phosphotyrosine phosphatase (PTP)-1B expression was increased in VSMC from both strains
Frasca et al., J Biol Chem 2007 : Inhibition of c-Abl tyrosine kinase by STI571 attenuates the effect of insulin on Akt/GSK-3beta phosphorylation and glycogen synthesis, and at the same time, it enhances the effect of insulin on ERK activation, cell proliferation, and migration
Mordier et al., Biochem Biophys Res Commun 2007 (Insulin Resistance...) : The insulin stimulated phosphorylation of GSK-3beta , a metabolic substrate of PKB, was diminished in palmitate hepatocytes
MacAulay et al., Cell Metab 2007 : Insulin stimulated protein kinase B ( PKB/Akt ) and GSK-3beta phosphorylation was higher in GSK-3alpha KO livers compared to wild-type littermates, and IRS-1 expression was markedly increased
Dokken et al., Am J Physiol Endocrinol Metab 2008 (Insulin Resistance) : Moreover, a small, but significant, portion of this oxidative stress induced insulin resistance is associated with a reduced insulin mediated suppression of the active form of GSK-3beta
Liu et al., Acta Pharmacol Sin 2008 (Insulin Resistance) : Resistin attenuated multiple effects of insulin, including insulin stimulated glycogen synthesis and phosphorylation of IRS, protein kinase B/Akt, as well as GSK-3beta
Yang et al., Life Sci 2008 : PI3K-GSK3beta signaling may be responsible for insulin stimulation of ET-1 production associated with insulin resistance and hyperinsulinemia
Frangioudakis et al., J Endocrinol 2008 (Insulin Resistance) : However, there was no insulin stimulated protein kinase B (PKB) Ser473 or glycogen synthase kinase (GSK)-3beta Ser9 phosphorylation in the LIP rats, compared with at least a twofold increase over basal in GLYC rats for both proteins
Anilkumar et al., Arterioscler Thromb Vasc Biol 2008 : After angiotensin II or TNFalpha treatment, JNK activation was augmented in Nox2 but not Nox4 transfected cells, whereas insulin augmented phosphorylation of p38MAPK, Akt, and GSK3beta specifically in Nox4 overexpressing cells and JNK specifically in Nox2 overexpressing cells
Mariappan et al., J Biol Chem 2008 (Diabetes Mellitus, Type 2...) : Dominant negative Akt, but not dominant negative p70S6 kinase, inhibited GSK3beta phosphorylation induced by high glucose and high insulin , suggesting Akt but not p70S6 kinase was upstream of GSK3beta
Kim et al., Diabetes Res Clin Pract 2009 (Glucose Intolerance...) : The insulin stimulated incremental changes in phosphorylated IR-beta, IRS, Akt, and GSK-3 beta and in the membrane associated PKC-zeta protein level were reduced in the IGT group compared with those in the control group ( p < 0.05 )
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
Gebhardt et al., J Cell Mol Med 2010 : It is concluded that L4 represents a potent insulin sensitizing agent favouring physiological effects of insulin mediated by GSK-3beta inhibition but avoiding hazardous effects such as activation of beta-catenin dependent gene expression which may lead to aberrant induction of cell proliferation and cancer
Xiong et al., BMB Rep 2009 : Insulin induced phosphorylation of Akt ( protein kinase B ) and GSK-3beta ( Glycogen synthase kinase ), subsequent dephosphorylation of glycogen synthase and glycogen synthesis were increased by inhibiting the expression of SKIP, whereas the insulin induced glycogen synthesis was decreased by overexpression of WT-SKIP
Genua et al., Vitam Horm 2009 : Inhibition of c-Abl tyrosine kinase by STI571 attenuates the effect of insulin on Akt/GSK-3beta phosphorylation and glycogen synthesis, and at the same time, it enhances the effect of insulin on ERK activation, cell proliferation and migration
de Abreu et al., Comp Biochem Physiol B Biochem Mol Biol 2009 : Additionally, treatment with Wortmannin increased the expression level of the insulin regulated downstream target glycogen synthase kinase 3 beta ( GSK3beta )
Biswas et al., Molecular vision 2009 : However, imatinib exposure did not affect insulin induced insulin receptor substrate (IRS) associated PI 3-kinase activity and the downstream phosphorylation of Akt, GSK-3beta , and p70S6kinase
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
Parisi et al., BMC biology 2011 : Drosophila insulin and target of rapamycin ( TOR ) pathways regulate GSK3 beta activity to control Myc stability and determine Myc expression in vivo
Lesort et al., J Neurochem 1999 (Neuroblastoma) : The insulin induced increase in tau phosphorylation and concurrent activation of GSK-3beta was rapid ( < 2 min ) and transient, and was associated with increased tyrosine phosphorylation of GSK-3beta ... Thus, insulin rapidly and transiently activated GSK-3beta and modulated tau phosphorylation, alterations that may contribute to neuronal plasticity