Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue

Darren A.E. Cross, Peter W. Watt, Morag Shaw, Jeroen Van Der Kaay, C. Peter Downes, Julie C. Holder, Philip Cohen

    Research output: Contribution to journalArticle

    181 Citations (Scopus)

    Abstract

    Insulin stimulated protein kinase Bα (PKBα) more than 10-fold and decreased glycogen synthase kinase-3 (GSK3) activity by 50 ± 10% in skeletal muscle and adipocytes. Rapamycin did not prevent the activation of PKB, inhibition of GSK3 or stimulation of glycogen synthase up to 5 min. Thus rapamycin-insensitive pathways mediate the acute effect of insulin on glycogen synthase in the major insulin-responsive tissues. The small and very transient effects of EGF on phosphatidylinositol (3,4,5)P3 PKBα and GSK3 in adipocytes, compared to the strong and sustained effects of insulin, explains why EGF does not stimulate glucose uptake or glycogen synthesis in adipocytes.

    Original languageEnglish
    Pages (from-to)211-215
    Number of pages5
    JournalFEBS Letters
    Volume406
    Issue number1-2
    DOIs
    Publication statusPublished - 7 Apr 1997

    Keywords

    • EGF
    • Glycogen synthase
    • Glycogen synthase kinase 3
    • Insulin
    • Protein kinase B
    • Rapamycin

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