Send to

Choose Destination
  • Showing results for amp activated protein kinase attenuates wnt catenin signal. Your search for AMP-activated protein kinase attenuates Wnt-?-catenin signa retrieved no results.
Mol Cell Endocrinol. 2011 Jun 6;339(1-2):114-9. doi: 10.1016/j.mce.2011.04.003. Epub 2011 Apr 8.

AMP-activated protein kinase attenuates Wnt/β-catenin signaling in human osteoblastic Saos-2 cells.

Author information

Department of Pediatrics, Graduate School of Medicine, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba-shi, Chiba 260-8670, Japan.


AMP-activated protein kinase (AMPK) is a key sensor of cellular energetic conditions. Recent studies suggest that AMPK affects osteoblast differentiation, although its role and mechanism are not fully understood. One of the most important signals in osteoblast differentiation is the Wnt/β-catenin pathway which induces T-cell transcription factor 1 (TCF)-dependent transcription. Using human osteoblast-like Saos-2 cells, we determined whether AMPK modulates Wnt/β-catenin signaling in osteoblasts. Chemical activators of AMPK (AICAR [5-aminoimidazole-4-carboxamide riboside], metformin) suppressed Wnt3a-induced TCF-dependent transcriptional activity. Transactivation by Wnt was potentiated by inhibiting β-catenin degradation with lithium chloride (LiCl). LiCl-induced Wnt transactivation was suppressed by addition of metformin. Metformin increased the phosphorylation of β-catenin and decreased β-catenin protein levels leading to suppression of Wnt/β-catenin signaling. Our present study showed that AMPK attenuates Wnt/β-catenin signaling by reducing β-catenin protein levels in osteoblast-like cells.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center