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INS — PTK7

Text-mined interactions from Literome

Corry et al., Am J Hypertens 2002 (Hyperinsulinism...) : Insulin induced protein tyrosine kinase activity was decreased in erythrocytes from hypertensive versus control subjects
Radu et al., Psychopharmacologia 2002 : It has also been shown that CCK-4 can stimulate insulin release and thus C-peptide release from pancreatic islet cells
Jou et al., Planta Med 2004 : Moreover, genistein can activate alpha ( 1A ) -AR at a concentration ( 1 micromol/L ) lower than that ( 50 micromol/L ) needed to abolish the insulin stimulated phosphorylation of PTK
Strobel et al., Biochem J 2005 : On the whole, the experimental evidence and computer simulation data favour a transport inhibition mechanism in which flavonoids and GLUT4 interact directly, rather than by a mechanism related to protein-tyrosine kinase and insulin signalling inhibition
Tavaré et al., J Biol Chem 1991 : Furthermore, insulin stimulated exogenous protein-tyrosine kinase activity of the mutant receptors is unaffected, as assessed following either phosphorylation of receptors in intact cells or following immunopurification of receptors and their autophosphorylation in vitro
Spicarova et al., Neuroscience 2010 (Pain...) : The membrane permeable protein tyrosine kinase inhibitor, lavendustin A ( 10 microM ), prevented the insulin induced AMPA EPSC depression
Loh et al., Diabetologia 2012 (Diabetes Mellitus, Type 2...) : Insulin activates insulin receptor protein tyrosine kinase and downstream phosphatidylinositol-3-kinase (PI3K)/Akt signalling in muscle to promote glucose uptake
Rosen et al., Science 1987 : Three recent advances pertinent to the mechanism of insulin action include ( i ) the discovery that the insulin receptor is an insulin dependent protein tyrosine kinase , functionally related to certain growth factor receptors and oncogene encoded proteins, ( ii ) the molecular cloning of the insulin proreceptor complementary DNA, and ( iii ) evidence that the protein tyrosine kinase activity of the receptor is essential for insulin action
Chou et al., J Biol Chem 1989 (Carcinoma, Hepatocellular...) : The receptor showed an insulin dependent protein tyrosine kinase activity
Cordera et al., Endocrinology 1987 : It was observed that MA 10 inhibits insulin binding to human, but not rat, tissues while inhibiting insulin stimulated receptor autophosphorylation and protein tyrosine kinase activity in both human and rat tissues
Ellis et al., J Virol 1988 : The human insulin receptor (IR) is a transmembrane glycoprotein, whose cytoplasmic domain contains an insulin activated protein-tyrosine kinase ( EC 2.7.1.112 )
Gherzi et al., Biochem Biophys Res Commun 1988 : We previously demonstrated that the anti-insulin receptor monoclonal antibody MA-10 decreases insulin stimulated receptor protein tyrosine kinase activity `` in vitro '', without inhibiting insulin receptor binding
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
Sandberg et al., Pharmacol Toxicol 1988 : In contrast, CCK-4 , CCK-6 and CCK-33 ( 1-21 ) had no effect on insulin secretion
Petruzzelli et al., J Biol Chem 1985 : Acquisition of insulin dependent protein tyrosine kinase activity during Drosophila embryogenesis ... Insulin dependent protein tyrosine kinase activity has now been identified in Drosophila ... However, during the 6-12- and 12-18-h periods of embryogenesis when insulin dependent protein tyrosine kinase activity is expressed, another protein ( Mr = 100,000 ) becomes cross linked to 125I-insulin ... We conclude that the insulin binding and insulin dependent protein tyrosine kinase activities of the mammalian insulin receptor are conserved in Drosophila ... However, the insulin dependent protein tyrosine kinase activity of the receptor is detected only during specific times in embryogenesis
Hermansen et al., Endocrinology 1984 : CCK-4 and CCK-8 at concentrations of 1, 10, and 100 nM dose dependently stimulated pancreatic SRIF, insulin , and glucagon release
Carter et al., Biochemistry 1996 : Phosphorylation of serine 1078 of the insulin receptor to high stoichiometry by the kinase did not affect insulin stimulated exogenous protein tyrosine kinase activity of the insulin receptor
Enan et al., Reprod Toxicol 1996 : In the presence of insulin , TCDD did not induce any additional changes in postnuclear or nuclear PTK
Brown et al., Carcinogenesis 1998 (Neuroblastoma) : The results showed that genistein down-regulated intrinsic PTK activity by approximately 33 % and inhibited insulin-like growth factor (IGF) stimulated PTK activity by 75 %
Persaud et al., J Mol Endocrinol 1999 (Second Messenger Systems) : We have examined the effects of glucose, the major physiological insulin secretagogue, on the tyrosine phosphorylation state of islet proteins, and assessed beta cell insulin secretory responses in the presence of PTK inhibitors ... The PTK inhibitors genistein ( GS ) and tyrphostin A47 ( TA47 ) inhibited islet tyrosine kinase activities and glucose-, 4alpha ketoisocaproic acid ( KIC ) - and sulphonylurea stimulated insulin release, without affecting glucose metabolism