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Increased insulin sensitivity and reduced adiposity in phosphatidylinositol 5-phosphate 4-kinase beta(-/-) mice

Academic Article
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Overview

authors

  • Lamia, Katja
  • Peroni, O. D.
  • Kim, Y. B.
  • Rameh, L. E.
  • Kahn, B. B.
  • Cantley, L. C.

publication date

  • June 2004

journal

  • Molecular and Cellular Biology  Journal

abstract

  • Phosphorylated derivatives of the lipid phosphatidylinositol are known to play critical roles in insulin response. Phosphatidylinositol 5-phosphate 4-kinases convert phosphatidylinositol 5-phosphate to phosphatidylinositol 4,5-bis-phosphate. To understand the physiological role of these kinases, we generated mice that do not express phosphatidylinositol 5-phosphate 4-kinase beta. These mice are hypersensitive to insulin and have reduced body weights compared to wild-type littermates. While adult male mice lacking phosphatidylinositol 5-phosphate 4-kinase beta have significantly less body fat than wild-type littermates, female mice lacking phosphatidylinositol 5-phosphate 4-kinase beta have increased insulin sensitivity in the presence of normal adiposity. Furthermore, in vivo insulin-induced activation of the protein kinase Akt is enhanced in skeletal muscle and liver from mice lacking phosphatidylinositol 5-phosphate 4-kinase beta. These results indicate that phosphatidylinositol 5-phosphate 4-kinase beta plays a role in determining insulin sensitivity and adiposity in vivo and suggest that inhibitors of this enzyme may be useful in the treatment of type 2 diabetes.

subject areas

  • Adipose Tissue
  • Animals
  • Eating
  • Female
  • Insulin
  • Leptin
  • Male
  • Mice
  • Mice, Knockout
  • Muscle, Skeletal
  • Phosphatidylinositol Phosphates
  • Phosphotransferases
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Identity

PubMed Central ID

  • PMC416424

International Standard Serial Number (ISSN)

  • 0270-7306

Digital Object Identifier (DOI)

  • 10.1128/mcb.24.11.5080-5087.2004

PubMed ID

  • 15143198
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Additional Document Info

start page

  • 5080

end page

  • 5087

volume

  • 24

issue

  • 11

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