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Glucose regulates diacylglycerol intracellular levels and protein kinase C activity by modulating diacylglycerol-kinase subcellular localization. (Articolo in rivista)

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Glucose regulates diacylglycerol intracellular levels and protein kinase C activity by modulating diacylglycerol-kinase subcellular localization. (Articolo in rivista) (literal)

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Miele C; Paturzo F; Teperino R; Sakane F; Fiory F; Oriente F; Ungaro P; Valentino R; Beguinot F; Formisano P (2007)
Glucose regulates diacylglycerol intracellular levels and protein kinase C activity by modulating diacylglycerol-kinase subcellular localization.
in The Journal of biological chemistry (Print); American Society Of Biochemistry And Molecular Biology Inc. (ASBMB), Rockville (Stati Uniti d'America)
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Miele C; Paturzo F; Teperino R; Sakane F; Fiory F; Oriente F; Ungaro P; Valentino R; Beguinot F; Formisano P (literal)

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Dipartimento di Biologia e Patologia Cellulare e Molecolare & Istituto di Endocrinologia ed Oncologia Sperimentale del CNR, Federico II University of Naples, Via Pansini 5, Naples 80131, Italy and the §Department of Biochemistry, Sapporo Medical University School of Medicine, South-1, West-17, Chuo-ku, Sapporo 060-8556, Japan (literal)

Titolo

Glucose regulates diacylglycerol intracellular levels and protein kinase C activity by modulating diacylglycerol-kinase subcellular localization. (literal)

Abstract

Although chronic hyperglycemia reduces insulin sensitivity and leads to impaired glucose utilization, short term exposure to high glucose causes cellular responses positively regulating its own metabolism. We show that exposure of L6 myotubes overexpressing human insulin receptors to 25 mM glucose for 5 min decreased the intracellular levels of diacylglycerol (DAG). This was paralleled by transient activation of diacylglycerol kinase (DGK) and of insulin receptor signaling. Following 30-min exposure, however, both DAG levels and DGK activity returned close to basal levels. Moreover, the acute effect of glucose on DAG removal was inhibited by >85% by the DGK inhibitor R59949. DGK inhibition was also accompanied by increased protein kinase C-? (PKC?) activity, reduced glucose-induced insulin receptor activation, and GLUT4 translocation. Glucose exposure transiently redistributed DGK isoforms ? and ?, from the prevalent cytosolic localization to the plasma membrane fraction. However, antisense silencing of DGK?, but not of DGK? expression, was sufficient to prevent the effect of high glucose on PKC? activity, insulin receptor signaling, and glucose uptake. Thus, the short term exposure of skeletal muscle cells to glucose causes a rapid induction of DGK, followed by a reduction of PKC? activity and transactivation of the insulin receptor signaling. The latter may mediate, at least in part, glucose induction of its own metabolism. (literal)

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