| First Author | Riuzzi F | Year | 2011 |
| Journal | J Cell Sci | Volume | 124 |
| Issue | Pt 14 | Pages | 2389-400 |
| PubMed ID | 21693575 | Mgi Jnum | J:183046 |
| Mgi Id | MGI:5317383 | Doi | 10.1242/jcs.084491 |
| Citation | Riuzzi F, et al. (2011) S100B protein regulates myoblast proliferation and differentiation by activating FGFR1 in a bFGF-dependent manner. J Cell Sci 124(Pt 14):2389-400 |
| abstractText | S100B protein has been shown to exert anti-myogenic and mitogenic effects in myoblast cultures through inhibition of the myogenic p38 MAPK and activation of the mitogenic ERK1/2. However, the receptor mediating these effects had not been identified. Here, we show that S100B increases and/or stabilizes the binding of basic fibroblast growth factor (bFGF) to bFGF receptor 1 (FGFR1) by interacting with bFGF, thereby enhancing FGFR1 activation and the mitogenic and anti-myogenic effects of FGFR1. S100B also binds to its canonical receptor RAGE (receptor for advanced glycation end-products), a multi-ligand receptor previously shown to transduce a pro-myogenic signal when activated by HMGB1, and recruits RAGE into a RAGE-S100B-bFGF-FGFR1 complex. However, when bound to S100B-bFGF-FGFR1, RAGE can no longer stimulate myogenic differentiation, whereas in the absence of either bFGF or FGFR1, binding of S100B to RAGE results in stimulation of RAGE anti-mitogenic and promyogenic signaling. An S100B-bFGF-FGFR1 complex also forms in Rage(-/-) myoblasts, leading to enhanced proliferation and reduced differentiation, which points to a dispensability of RAGE for the inhibitory effects of S100B on myoblasts under the present experimental conditions. These results reveal a new S100B-interacting protein - bFGF - in the extracellular milieu and suggest that S100B stimulates myoblast proliferation and inhibits myogenic differentiation by activating FGFR1 in a bFGF-dependent manner. |
