Gene interactions and pathways from curated databases and text-mining
FEBS Lett 2000, PMID: 10781824

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

Valverde, A M; Lorenzo, M; Navarro, P; Mur, C; Benito, M

In 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 p85alpha 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) zeta 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 zeta, the PKC zeta pathway contributing to glucose transport induced by insulin in fetal brown adipocytes.

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Text Mining Data

p85alpha ⊣ insulin: " IRS-1/IRS-2 associated p85alpha and phosphatidylinositol (PI) 3-kinase enzymatic activity were partly reduced in brown adipocytes pretreated with okadaic acid upon stimulation with insulin "

phosphatidylinositol (PI) 3-kinase ⊣ insulin: " IRS-1/IRS-2 associated p85alpha and phosphatidylinositol (PI) 3-kinase enzymatic activity were partly reduced in brown adipocytes pretreated with okadaic acid upon stimulation with insulin "

protein kinase C (PKC) zeta → 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) zeta activity "

Akt/PKB → insulin: " However, activation of Akt/PKB or p70 S6 kinase ( p70 ( s6k ) ) by insulin remained unaltered "

p70 → insulin: " However, activation of Akt/PKB or p70 S6 kinase ( p70 ( s6k ) ) by insulin remained unaltered "

Manually curated Databases

No curated data.