Literature DB >> 11434672

The role of protein kinase C isoforms in insulin action.

P Formisano1, F Beguinot.   

Abstract

Insulin action on target tissues is mediated by specific tyrosine kinase receptors. Upon ligand binding insulin receptors autophosphorylate and phosphorylate intracellular substrates on tyrosine residues. These early events of insulin action are followed by the activation of a number of enzymes, including protein kinase C (PKC). At least 14 PKC isoforms have been identified and cloned to date. PKCs appear to play dual roles in insulin signaling. For instance, they are involved in transduction of specific insulin signals but also contribute to the generation of insulin resistance. In this article, we will analyze the experimental evidence addressing the mechanism by which insulin might activate individual PKC isoforms as well as the role of single PKCs in insulin-induced bioeffects.

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Year:  2001        PMID: 11434672     DOI: 10.1007/BF03351048

Source DB:  PubMed          Journal:  J Endocrinol Invest        ISSN: 0391-4097            Impact factor:   4.256


  49 in total

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Journal:  J Clin Invest       Date:  1999-04       Impact factor: 14.808

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Journal:  Cell Signal       Date:  1992-03       Impact factor: 4.315

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Journal:  J Biol Chem       Date:  1995-08-11       Impact factor: 5.157

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Journal:  Curr Opin Cell Biol       Date:  1997-04       Impact factor: 8.382

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Journal:  Endocrinology       Date:  1996-07       Impact factor: 4.736

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Authors:  V Donchenko; A Zannetti; P M Baldini
Journal:  Biochim Biophys Acta       Date:  1994-07-21

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Authors:  C E Chalfant; H Mischak; J E Watson; B C Winkler; J Goodnight; R V Farese; D R Cooper
Journal:  J Biol Chem       Date:  1995-06-02       Impact factor: 5.157

9.  Expression of the major isoenzyme of protein kinase-C in skeletal muscle, nPKC theta, varies with muscle type and in response to fructose-induced insulin resistance.

Authors:  R Donnelly; M J Reed; S Azhar; G M Reaven
Journal:  Endocrinology       Date:  1994-12       Impact factor: 4.736

10.  In L6 skeletal muscle cells, glucose induces cytosolic translocation of protein kinase C-alpha and trans-activates the insulin receptor kinase.

Authors:  M Caruso; C Miele; F Oriente; A Maitan; G Bifulco; F Andreozzi; G Condorelli; P Formisano; F Beguinot
Journal:  J Biol Chem       Date:  1999-10-01       Impact factor: 5.157

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  4 in total

1.  The beta-specific protein kinase C inhibitor ruboxistaurin (LY333531) suppresses glucose-induced adhesion of human monocytes to endothelial cells in vitro.

Authors:  Thomas Kunt; Thomas Forst; Christof Kazda; Oliver Harzer; Martin Engelbach; Mirjam Löbig; Jürgen Beyer; Andreas Pfützner
Journal:  J Diabetes Sci Technol       Date:  2007-11

2.  PKCδ regulates hepatic insulin sensitivity and hepatosteatosis in mice and humans.

Authors:  Olivier Bezy; Thien T Tran; Jussi Pihlajamäki; Ryo Suzuki; Brice Emanuelli; Jonathan Winnay; Marcelo A Mori; Joel Haas; Sudha B Biddinger; Michael Leitges; Allison B Goldfine; Mary Elizabeth Patti; George L King; C Ronald Kahn
Journal:  J Clin Invest       Date:  2011-05-16       Impact factor: 14.808

3.  In skeletal muscle advanced glycation end products (AGEs) inhibit insulin action and induce the formation of multimolecular complexes including the receptor for AGEs.

Authors:  Angela Cassese; Iolanda Esposito; Francesca Fiory; Alessia P M Barbagallo; Flora Paturzo; Paola Mirra; Luca Ulianich; Ferdinando Giacco; Claudia Iadicicco; Angela Lombardi; Francesco Oriente; Emmanuel Van Obberghen; Francesco Beguinot; Pietro Formisano; Claudia Miele
Journal:  J Biol Chem       Date:  2008-10-27       Impact factor: 5.157

4.  Functional involvement of protein kinase C-betaII and its substrate, myristoylated alanine-rich C-kinase substrate (MARCKS), in insulin-stimulated glucose transport in L6 rat skeletal muscle cells.

Authors:  D S Chappell; N A Patel; K Jiang; P Li; J E Watson; D M Byers; D R Cooper
Journal:  Diabetologia       Date:  2009-02-28       Impact factor: 10.122

  4 in total

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