| Literature DB >> 18275847 |
Yuko Katsuki1, Kei Sakamoto, Tokutaro Minamizato, Hatsune Makino, Akihiro Umezawa, Masa-Aki Ikeda, Bernard Perbal, Teruo Amagasa, Akira Yamaguchi, Ken-Ichi Katsube.
Abstract
CCN3/NOV activates the Notch signal through the carboxyl terminal cysteine-rich (CT) domain. CCN3 transfection to Kusa-A1 inhibited osteogenic differentiation and cell proliferation, which is accompanied by upregulation of Hes/Hey, Notch downstream targets, and p21, a CDK inhibitor. Upregulation of Hes/Hey and p21 was abrogated by the deletion of CT domain. Anti-proliferative activity of CCN3 was also abrogated by CT domain deletion whereas anti-osteogenic activity was not completely abrogated. We found that CT domain-deleted CCN3 still possesses antagonistic effect on BMP-2. These results suggest that CCN3 employs Notch and BMP pathways in anti-osteogenic activity while it inhibits cell proliferation uniquely by Notch/p21 pathway.Entities:
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Year: 2008 PMID： 18275847 DOI： 10.1016/j.bbrc.2008.02.010
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575