論文

査読有り
2010年

Interaction between myostatin and extracellular matrix components

ANIMAL SCIENCE JOURNAL
  • Takayuki Miura
  • ,
  • Yasuhiro Kishioka
  • ,
  • Jun-ichi Wakamatsu
  • ,
  • Akihito Hattori
  • ,
  • Takanori Nishimura

81
1
開始ページ
102
終了ページ
107
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1111/j.1740-0929.2009.00700.x
出版者・発行元
WILEY-BLACKWELL PUBLISHING, INC

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)similar to 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.

Web of Science ® 被引用回数 : 19

リンク情報
DOI
https://doi.org/10.1111/j.1740-0929.2009.00700.x
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/20163680
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000274157500015&DestApp=WOS_CPL
ID情報
  • DOI : 10.1111/j.1740-0929.2009.00700.x
  • ISSN : 1344-3941
  • PubMed ID : 20163680
  • Web of Science ID : WOS:000274157500015

エクスポート
BibTeX RIS