Overexpression of a constitutively active form of phosphatidylinositol 3-kinase is sufficient to promote Glut 4 translocation in adipocytes. - Wikidata - wikimedia - TriplyDB

Overexpression of a constitutively active form of phosphatidylinositol 3-kinase is sufficient to promote Glut 4 translocation in adipocytes.

Overexpression of a constitutively active form of phosphatidylinositol 3-kinase is sufficient to promote Glut 4 translocation in adipocytes.

http://www.wikidata.org/entity/Q42523326

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Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes Potential role of 3-phosphoinositide-dependent protein kinase 1 (PDK1) in insulin-stimulated glucose transporter 4 translocation in adipocytes Expression of a prenylation-deficient Rab4 inhibits the GLUT4 translocation induced by active phosphatidylinositol 3-kinase and protein kinase B Liver X receptors as insulin-mediating factors in fatty acid and cholesterol biosynthesis Insulin increases the association of Akt-2 with Glut4-containing vesicles Identification of the APS protein as a novel insulin receptor substrate Activation of glycogen synthase by insulin in 3T3-L1 adipocytes involves c-Cbl-associating protein (CAP)-dependent and CAP-independent signaling pathways.Munc18c regulates insulin-stimulated glut4 translocation to the transverse tubules in skeletal muscle.Diversification of cardiac insulin signaling involves the p85 alpha/beta subunits of phosphatidylinositol 3-kinase.From insulin receptor signalling to Glut 4 translocation abnormalities in obesity and insulin resistance.Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts Spatiotemporal Regulators for Insulin-Stimulated GLUT4 Vesicle Exocytosis.Muscle-specific Pten deletion protects against insulin resistance and diabetes Normal insulin-dependent activation of Akt/protein kinase B, with diminished activation of phosphoinositide 3-kinase, in muscle in type 2 diabetes A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes.Differential regulation of phosphoinositide 3-kinase adapter subunit variants by insulin in human skeletal muscle.Regulated in development and DNA damage responses -1 (REDD1) protein contributes to insulin signaling pathway in adipocytes.Turning signals on and off: GLUT4 traffic in the insulin-signaling highway.Suppression of nuclear factor-κB activation and inflammation in microglia by physically modified saline.Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes.Optogenetic activation reveals distinct roles of PIP3 and Akt in adipocyte insulin action.Inhibition of Soluble Epoxide Hydrolase Limits Mitochondrial Damage and Preserves Function Following Ischemic Injury.Involvement of phosphatidylinositol 3-kinase-mediated up-regulation of I kappa B alpha in anti-inflammatory effect of gemfibrozil in microglia Naringenin inhibits adipogenesis and reduces insulin sensitivity and adiponectin expression in adipocytes.Hesperetin impairs glucose uptake and inhibits proliferation of breast cancer cells.Thiazolidinediones block tumor necrosis factor-alpha-induced inhibition of insulin signaling.Impaired activation of phosphoinositide 3-kinase by insulin in fibroblasts from patients with severe insulin resistance and pseudoacromegaly. A disorder characterized by selective postreceptor insulin resistance.Skeletal muscle insulin resistance: the interplay of local lipid excess and mitochondrial dysfunction.Phosphatidylinositol 3-phosphate [PtdIns3P] is generated at the plasma membrane by an inositol polyphosphate 5-phosphatase: endogenous PtdIns3P can promote GLUT4 translocation to the plasma membrane.Activation of phosphatidylinositol 3-kinase is sufficient for cell cycle entry and promotes cellular changes characteristic of oncogenic transformation.Insulin signaling.Insulin stimulates hypoxia-inducible factor 1 through a phosphatidylinositol 3-kinase/target of rapamycin-dependent signaling pathway.Differential effects of phosphatidylinositol 3-kinase inhibition on intracellular signals regulating GLUT4 translocation and glucose transport.Reconstitution of insulin signaling pathways in rat 3Y1 cells lacking insulin receptor and insulin receptor substrate-1. Evidence that activation of Akt is insufficient for insulin-stimulated glycogen synthesis or glucose uptake in rat 3Y1 cells.Membrane-targeted phosphatidylinositol 3-kinase mimics insulin actions and induces a state of cellular insulin resistance.Actin filaments participate in the relocalization of phosphatidylinositol3-kinase to glucose transporter-containing compartments and in the stimulation of glucose uptake in 3T3-L1 adipocytes.Effects of acutely inhibiting PI3K isoforms and mTOR on regulation of glucose metabolism in vivo Insulin and insulin-like growth factor I up-regulate GLUT4 gene expression in fetal brown adipocytes, in a phosphoinositide 3-kinase-dependent manner.Parathyroid hormone suppresses insulin signaling in adipocytes.Regulation of system A amino acid transport in 3T3-L1 adipocytes by insulin.

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P2860

Overexpression of a constitutively active form of phosphatidylinositol 3-kinase is sufficient to promote Glut 4 translocation in adipocytes.

http://www.wikidata.org/entity/Q42523326

description

1996 nî lūn-bûn

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1996年の論文

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年學術文章

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1996年學術文章

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name

Overexpression of a constituti ...... 4 translocation in adipocytes.

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Overexpression of a constituti ...... 4 translocation in adipocytes.

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type

label

Overexpression of a constituti ...... 4 translocation in adipocytes.

@en

Overexpression of a constituti ...... 4 translocation in adipocytes.

@nl

prefLabel

Overexpression of a constituti ...... 4 translocation in adipocytes.

@en

Overexpression of a constituti ...... 4 translocation in adipocytes.

@nl

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JBC.271.41.25227

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Journal of Biological Chemistry

P1476

Overexpression of a constituti ...... 4 translocation in adipocytes.

@en

P2093

Calleja V

http://www.w3.org/2001/XMLSchema#string

Grillo S

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Grémeaux T

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Klippel A

http://www.w3.org/2001/XMLSchema#string

Le Marchand-Brustel Y

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Tanti JF

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Van Obberghen E

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Williams LT

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P2860

1-Phosphatidylinositol 3-kinase activity is required for insulin-stimulated glucose transport but not for RAS activation in CHO cells

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells

Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction

The inability of phosphatidylinositol 3-kinase activation to stimulate GLUT4 translocation indicates additional signaling pathways are required for insulin-stimulated glucose uptake.

Tyrosine kinase-deficient mutant human insulin receptors (Met1153-->Ile) overexpressed in transfected rat adipose cells fail to mediate translocation of epitope-tagged GLUT4.

Roles of 1-phosphatidylinositol 3-kinase and ras in regulating translocation of GLUT4 in transfected rat adipose cells

The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity.

Phosphoinositide kinases.

Mitogen-activated protein kinase kinase inhibition does not block the stimulation of glucose utilization by insulin.

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25227-25232

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41

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271

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14395290

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8810283

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