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Okadaic acid inhibits insulin-induced glucose transport in fetal brown adipocytes in an Akt-independent and protein kinase C ζ-dependent manner

AuthorsValverde, Ángela M.; Lorenzo, Margarita; Navarro, Paloma; Mur, Cecilia; Benito, Manuel
KeywordsInsulin resistance
Protein kinase C ζ
Glucose transport
Insulin receptor substrate
Serine/threonine phosphorylation
Okadaic acid
Insulin signaling
IRS, insulin receptor substrate
FCS, fetal calf serum
PBS, phosphate buffered saline
PI, phosphatidylinositol
Issue Date2000
PublisherJohn Wiley & Sons
Federation of European Biochemical Societies
CitationFEBS Letters 472(1): 153-158 (2000)
AbstractIn the present study we have investigated the effect of increased serine/threonine phosphorylation of insulin receptor substrates-1 and -2 (IRS-1 and IRS-2) by okadaic acid pretreatment on brown adipocyte insulin signalling leading to glucose transport, an important metabolic effect of insulin in brown adipose tissue. Okadaic acid pretreatment before insulin stimulation decreased IRS-1 and IRS-2 tyrosine phosphorylation in parallel to a decrease in their sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobility. IRS-1/IRS-2-associated p85α and phosphatidylinositol (PI) 3-kinase enzymatic activity were partly reduced in brown adipocytes pretreated with okadaic acid upon stimulation with insulin. Furthermore, insulin-induced glucose uptake was totally abolished by the inhibitor in parallel with a total inhibition of insulin-induced protein kinase C (PKC) ζ activity. However, activation of Akt/PKB or p70 S6 kinase (p70(s6k)) by insulin remained unaltered. Our results suggest that downstream of PI 3-kinase, insulin signalling diverges into at least two independent pathways through Akt/PKB and PKC ζ, the PKC ζ pathway contributing to glucose transport induced by insulin in fetal brown adipocytes.
Identifiersdoi: 10.1016/S0014-5793(00)01448-4
issn: 0014-5793
e-issn: 1873-3468
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