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Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells.

Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells. Research Abstract Details 

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  • Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells. Abstract Text:

    hiroki yokooHiroki Yokoo,takayuki nemotoTakayuki Nemoto,toshihiko yanagitaToshihiko Yanagita,shinya satohShinya Satoh,norie yoshikawaNorie Yoshikawa,toyoaki marutaToyoaki Maruta,akihiko wadaAkihiko Wada,hiroki yokooHiroki Yokoo,takayuki nemotoTakayuki Nemoto,toshihiko yanagitaToshihiko Yanagita,shinya satohShinya Satoh,norie yoshikawaNorie Yoshikawa,toyoaki marutaToyoaki Maruta,akihiko wadaAkihiko Wada,

    In cultured bovine adrenal chromaffin cells, 48 h-treatment with 20 mmol/L LiCl, 1 mmol/L valproic acid, 30 micromol/L SB216763, 30 micromol/L SB415286, or 100 nmol/L insulin, a condition that inhibits constitutive active glycogen synthase kinase-3 (GSK-3), decreased cell surface (125)I-insulin binding capacity by approximately 39%, without altering the K(d) value; LiCl, SB216763 or insulin decreased insulin receptor (IR) and IR precursor levels, attenuating insulin-induced Tyr-autophosphorylation of IR. LiCl increased inhibitory Ser9-phosphorylation of GSK-3beta at 6 h, decreasing (125)I-insulin binding at 24 h. SB216763-induced (125)I-insulin binding reduction (IC(50) = 3 micromol/L) was preceded by beta-catenin level increase by SB216763 (EC(50) = 11 micromol/L), a hallmark of GSK-3 inhibition. Insulin-induced rapid (> 1 min) Ser9-phosphorylation of GSK-3beta (Nemoto et al. 2006) was followed by approximately 48% decrease of IR level. LiCl did not stimulate endocytosis, nor proteolysis of IR. LiCl destabilized IR mRNA (t(1/2) = 9.3 vs. 6.5 h), decreasing IR mRNA level by approximately 47%, without altering IR gene transcription. Decreases of (125)I-insulin binding and IR level, as well as increased Ser9-phosphorylation of GSK-3beta were restored to the control levels by washing the test compound-treated cells. Thus, GSK-3beta regulates IR level via controlling IR mRNA stability.

    Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells. Publishing Authors By Initials

    h yokooH Yokoo,t nemotoT Nemoto,t yanagitaT Yanagita,s satohS Satoh,n yoshikawaN Yoshikawa,t marutaT Maruta,a wadaA Wada,h yokooH Yokoo,t nemotoT Nemoto,t yanagitaT Yanagita,s satohS Satoh,n yoshikawaN Yoshikawa,t marutaT Maruta,a wadaA Wada,

    For similar abstracts research abstracts see: abstracts research

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    Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of neurochemistry

    VOLUME: 103

    Page Numbers: 1883-96

    Journal Abbreviation: J. Neurochem.

    ISSN: 1471-4159

    DAY: 18

    MONTH: 09

    YEAR: 2007

    Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985190

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    Grant and Affiliation Information for Glycogen synthase kinase-3beta: homologous regulation of cell surface insulin receptor level via controlling insulin receptor mRNA stability in adrenal chromaffin cells.

    AFFILIATION: Department of Pharmacology, Miyazaki Medical College, University of Miyazaki, Miyazaki, Japan.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: J Neurochem

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