Interaction between myostatin and extracellular matrix components.
Myostatin, a member of the TGF-beta 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 Zn(2+) with a dissociation constant (K(D)) of 10(-10) approximately 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.
Miura
Takayuki
T
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, Japan.
Kishioka
Yasuhiro
Y
Wakamatsu
Jun-ichi
J
Hattori
Akihito
A
Nishimura
Takanori
T
D000818:Animals; D002417:Cattle; D049109:Cell Proliferation; D058575:Decorin; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000737:chemistry* / Q000378:metabolism; D000071235:Fibromodulin; D007797:Laminin / Q000737:chemistry* / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism; D055435:Myostatin / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011509:Proteoglycans / Q000737:chemistry* / Q000378:metabolism; D020349:Surface Plasmon Resonance; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism
D058575:Decorin; D016326:Extracellular Matrix Proteins; D007797:Laminin; D055435:Myostatin; D011509:Proteoglycans; D000071235:Fibromodulin; D015032:Zinc