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

Lamia KA, Peroni OD, Kim YB, Rameh LE, Kahn BB, Cantley LC
Mol Cell Biol. 2004 24 (11): 5080-7

PMID: 15143198 · PMCID: PMC416424 · DOI:10.1128/MCB.24.11.5080-5087.2004

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.

MeSH Terms (12)

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

Connections (1)

This publication is referenced by other Labnodes entities:

Links