Requirement of protein kinase C zeta for stimulation of protein synthesis by insulin

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Requirement of protein kinase C zeta for stimulation of protein synthesis by insulin.

The ability of insulin to stimulate protein synthesis and cellular growth is mediated through the insulin receptor (IR), which phosphorylates Tyr residues in the insulin receptor substrate-signaling proteins (IRS-1 and IRS-2), Gab-1, and Shc. These phosphorylated substrates directly bind and activate enzymes such as phosphatidylinositol 3'-kinase (PI3K) and the guanine nucleotide exchange facto...

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Arachidonate activation of protein kinase C may be involved in the stimulation of protein synthesis by insulin in L6 myoblasts.

Insulin stimulated protein synthesis in L6 myoblasts but did not increase the labelling of DAG or the release of phosphocholine from phosphatidylcholine. The DAG lipase inhibitor, RHC 80267, more than doubled the amount of label appearing in DAG but did not stimulate protein synthesis. Even in the presence of the DAG lipase inhibitor insulin failed to have any effect on DAG labelling, and conve...

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Requirement for activation of the serine-threonine kinase Akt (protein kinase B) in insulin stimulation of protein synthesis but not of glucose transport.

A wide variety of biological activities including the major metabolic actions of insulin is regulated by phosphatidylinositol (PI) 3-kinase. However, the downstream effectors of the various signaling pathways that emanate from PI 3-kinase remain unclear. Akt (protein kinase B), a serine-threonine kinase with a pleckstrin homology domain, is thought to be one such downstream effector. A mutant A...

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A Requirement for Carbohydrate Metabolism for the Stimulation of Amino Acid Incorporation into Protein by Insulin.

Insulin has been shown to enhance the incorporation of labeled amino acids into the protein of the isolated rat diaphragm and other tissues (1, 2). The insulin stimulation is not exerted through an effect of the hormone on the transport of external amino acids to intracellular sites of protein synthesis.’ The dependency of this insulin action upon the nutritional status of the animal and a requ...

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Inhibition of insulin signaling by protein kinase C

Background: Insulin actions are decreased in endothelial cells causing vascular dysfunction in diabetic and insulin resistant states. Results: IRS2 and p85 subunit of PI3Kinase are targets of PKC and angiotensin activation inhibiting insulin signaling. Conclusion: PKC and angiotensin activation inhibit selective insulin activation of Akt/eNOS in endothelial cells. Significance: We provide a bio...

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ژورنال

عنوان ژورنال: Molecular and Cellular Biology

سال: 1997

ISSN: 0270-7306,1098-5549

DOI: 10.1128/mcb.17.9.5184