Increased insulin sensitivity and reduced adiposity in phosphatidylinositol 5-phosphate 4-kinase β-/- mice Academic Article uri icon

Overview

MeSH Major

  • Adipose Tissue
  • Insulin
  • Phosphatidylinositol Phosphates
  • Phosphotransferases

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.

publication date

  • June 2004

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC416424

Digital Object Identifier (DOI)

  • 10.1128/MCB.24.11.5080-5087.2004

PubMed ID

  • 15143198

Additional Document Info

start page

  • 5080

end page

  • 7

volume

  • 24

number

  • 11