Interaction between myostatin and extracellular matrix components |
| |
Authors: | Takayuki MIURA Yasuhiro KISHIOKA Jun-ichi WAKAMATSU Akihito HATTORI Takanori NISHIMURA |
| |
Institution: | Laboratory of Animal Products Science and Technology, School of Food Science and Technology, Faculty of Applied Life Science, Nippon Veterinary and Life Science University, Musashino, Tokyo, and;Meat Science Laboratory, Graduate School of Agriculture, Hokkaido University, Kita, Sapporo, Japan |
| |
Abstract: | Myostatin, a member of the TGF-β superfamily, is a negative regulator of skeletal muscle mass. We have recently demonstrated that decorin binds to myostatin in vitro , and that immobilized decorin within the collagen matrix prevents myostatin-mediated inhibition of myoblast proliferation. However, little is known about other ECM molecules that bind to myostatin and modulate its activity. Thus, in the present study, we investigated the interaction of several other ECM molecules with myostatin. We here show that fibromodulin, fibronectin and laminin bind to myostatin in the presence of Zn2+ with a dissociation constant ( KD ) of 10−10∼10−8 mol/L. Fibromodulin shows the highest affinity for myostatin among them. These results suggest that these ECM molecules may modulate myostatin activity like decorin does. |
| |
Keywords: | extracellular matrix glycoprotein myostatin proteoglycan |
|
|