| First Author | Kato K | Year | 2010 |
| Journal | Biochem Biophys Res Commun | Volume | 400 |
| Issue | 1 | Pages | 123-7 |
| PubMed ID | 20708602 | Mgi Jnum | J:164799 |
| Mgi Id | MGI:4835342 | Doi | 10.1016/j.bbrc.2010.08.024 |
| Citation | Kato K, et al. (2010) AMP-activated protein kinase positively regulates FGF-2-stimulated VEGF synthesis in osteoblasts. Biochem Biophys Res Commun 400(1):123-7 |
| abstractText | AMP-activated protein kinase (AMPK) is recognized as a regulator of energy homeostasis. We have previously reported that basic fibroblast growth factor (FGF-2) stimulates vascular endothelial growth factor (VEGF) release through the activation of p44/p42 mitogen-activated protein (MAP) kinase and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in osteoblast-like MC3T3-E1 cells. In the present study, we investigated the involvement of AMPK in FGF-2-stimulated VEGF release in these cells. FGF-2 time-dependently induced the phosphorylation of AMPK alpha-subunit (Thr-172). Compound C, an AMPK inhibitor, which suppressed the FGF-2-induced phosphorylation of AMPK, significantly inhibited the VEGF release stimulated by FGF-2. The AMPK inhibitor also reduced the mRNA expression of VEGF induced by FGF-2. The FGF-2-induced phosphorylation of both p44/p42 MAP kinase and SAPK/JNK was attenuated by compound C. These results strongly suggest that AMPK positively regulates the FGF-2-stimulated VEGF synthesis via p44/p42 MAP kinase and SAPK/JNK in osteoblasts. |
