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CAV1 — INS

Text-mined interactions from Literome

Nystrom et al., Mol Endocrinol 1999 : To investigate the potential role of caveolin-1 in insulin signaling we overexpressed wild-type ( Cav-WT ) or mutant ( Cav-Mut ; F92A/V94A in SD ) caveolin-1 in either Cos-7 cells cotransfected with IR or rat adipose cells ( low and high levels of endogenous caveolin-1, respectively )
Caselli et al., J Biol Chem 2001 : Insulin stimulation of these cells induces a strong increase of caveolin phosphorylation
Müller et al., Mol Cell Biol 2001 : Insulin-mimetic signaling by both CBD peptide and PIG as well as redistribution induced by CBD peptide, but not by PIG, was blocked by synthetic intracellular caveolin scaffolding domain ( CSD ) peptide
James et al., Diabetes 2001 (Genetic Predisposition to Disease...) : Skeletal muscle of stroke-prone spontaneously hypertensive rats exhibits reduced insulin stimulated glucose transport and elevated levels of caveolin and flotillin
Kimura et al., J Biol Chem 2002 : Insulin stimulated the phosphorylation of caveolin-1 on Tyr ( 14 ) ... Although previous studies demonstrated that the Src family kinase Fyn was highly enriched in caveolae, an inhibitor of this kinase had no effect on insulin stimulated caveolin phosphorylation
Maggi et al., Biochem Biophys Res Commun 2002 : The role of caveolin 1 in the Insulin Receptor (IR) signalling has been well investigated
Lin et al., Invest Ophthalmol Vis Sci 2003 : Phorbol ester ( TPA ) and insulin-like growth factor (IGF)-1 recruited PKCgamma into Cav-1 containing lipid rafts and stimulated the interactions of PKCgamma with Cav-1 and Cx43
Ishikawa et al., Cell Signal 2005 : These findings suggest that caveolin plays an important role in insulin signal to maintain glucose metabolism in intact animals ... However, the role of caveolin in insulin signal may differ from that in other transmembrane receptor signals
Salani et al., Biochem Biophys Res Commun 2005 : Insulin stimulates caveolin-1 and eNOS phosphorylation
Repetto et al., Biochem Biophys Res Commun 2005 : Since Insulin and IGF-I phosphorylate and activate eNOS, we investigated the role of caveolin-1 in Insulin and IGF-I stimulated eNOS activity ... These results suggest that caveolae could represent an intracellular site that contributes to differentiate IR and IGF-IR activity, and demonstrate the role of caveolin-1 in the eNOS activation by Insulin and IGF-I
Liu et al., J Pharmacol Exp Ther 2006 : Using the same system, we found that insulin secretion in 7.5 mM glucose plus 1 mM 8-bromo-cAMP ( 8-Br-cAMP ) is mediated by both Cav1.2 and Cav1.3
Doucey et al., Cell Mol Life Sci 2006 : Our data support the notion that the caveolin-filamin interaction contributes to restore insulin mediated phosphorylation of caveolin , thus allowing the release of active TCP-1
Wang et al., Am J Physiol Endocrinol Metab 2006 : Furthermore, insulin increased the tyrosine phosphorylation of caveolin-1 , and filipin ( which inhibits caveolae formation ) blocked insulin uptake
Schulman et al., Am J Physiol Heart Circ Physiol 2007 (Insulin Resistance) : Expression of caveolin-1 , a regulator of eNOS activity and insulin signaling, was 55 % lower in 24- than 3-mo rats ( P = 0.002 )
Puddu et al., Biochem Biophys Res Commun 2008 : Caveolin-1 is essential for glimepiride induced insulin secretion in the pancreatic betaTC-6 cell line ... The aim of this work was to investigate the possible role of caveolin-1 in glimepiride induced insulin secretion ... These results demonstrate that Cav-1 plays a critical role for glucose and sulfonylurea stimulated insulin secretion
Hahn-Obercyger et al., J Lipid Res 2009 (Body Weight) : The role of caveolin-1 in insulin receptor (IR) signaling has been widely investigated in vitro mainly in 3T3-L1 adipocyte cells
Wang et al., Mol Endocrinol 2009 : The decline of NO production correlated temporally to insulin induced translocation of eNOS and CAV-1 to PM. Knockdown of CAV-1 expression with a specific small interfering RNA duplex resulted in eNOS redistributing to the perinuclear region and nearly doubled insulin induced NO production ... Inhibition of phosphatidylinositol 3-kinase activity with wortmannin not only significantly inhibited insulin induced translocation of eNOS and CAV-1 to PM but also blocked insulin induced interaction of CAV-1 with eNOS at PM. Insulin increased incorporation of [ ( 3 ) H ] palmitic acid into eNOS immunoprecipitates by approximately 140 % ... Insulin induced translocation of eNOS and CAV-1 to PM was palmitoylation dependent ... These data show that insulin acutely regulates eNOS and CAV-1 trafficking to PM of vascular endothelial cells where their interaction can regulate eNOS activity
Otsu et al., Am J Physiol Cell Physiol 2010 (Diabetes Mellitus, Type 2...) : However, the role of caveolin in regulating insulin signals remains controversial ... Here, we demonstrate that caveolin potently enhances insulin receptor (IR) signaling when overexpressed in the liver in vivo
Wang et al., Am J Physiol Endocrinol Metab 2011 : Knockdown of caveolin-1 also inhibited insulin induced caveolin-1 and IGF-1 receptor translocation to the plasma membrane
Ormazabal et al., Horm Metab Res 2013 : However, in testosterone treated cells acute insulin stimulation did not increase phospho-S473Akt and phospho-Y14caveolin-1 levels and reduced 2-DOG uptake was observed compared to control cells
Mastick et al., J Cell Biol 1995 : Insulin stimulates the tyrosine phosphorylation of caveolin ... Stimulation of 3T3-L1 adipocytes with insulin significantly increased the tyrosine phosphorylation of caveolin and a 29-kD caveolin associated protein in caveolin enriched Triton-insoluble complexes ... Thus, the insulin dependent tyrosine phosphorylation of caveolin represents a novel, insulin-specific signal transduction pathway that may involve activation of a tyrosine kinase downstream of the insulin receptor
Mastick et al., J Biol Chem 1997 : Insulin stimulated tyrosine phosphorylation of caveolin is specific for the differentiated adipocyte phenotype in 3T3-L1 cells ... In adipocytes, overexpression of wild type Fyn leads to increased basal phosphorylation of caveolin and hyperphosphorylation of caveolin in response to insulin