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Journal of Biochemistry Advance Access published online on January 23, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn006
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© 2008 The Japanese Biochemical Society

Matrix Metalloproteinase-9 Associated with Heparan Sulfate Chains of GPI-anchored Cell Surface Proteoglycans Mediates Motility of Murine Colon Adenocarcinoma Cells

Yoshie Koyama1,2, Hideaki Naruo1, Yasuo Yoshitomi1, Seiichi Munesue1, Shinsuke Kiyono1, Yuri Kusano2, Katsunori Hashimoto3, Toyoharu Yokoi3, Hayao Nakanishi4, Satoru Shimizu1, Minoru Okayama1 and Kayoko Oguri2,*

1Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University, Kamigamo Motoyama, Kitaku, Kyoto 603-8555, 2Clinical Research Center, National Hospital Organization Nagoya Medical Center, 4-1-1 Sannomaru, Nakaku, Nagoya 460-0001, 3Department of Medical Technology, Nagoya University School of Health Sciences, 1-1-20 Daikohigashi, Higashiku, Nagoya 461-8673, and 4Department of Oncological Pathology, Aichi Cancer Center Research Institute, 1-1 Kanokoden, Chikusaku, Nagoya 464-0021, Japan

* To whom correspondence should be addressed. Phone: +81-52-951-1111, Fax: +81-52-951-9075, E-mail: ogurik{at}nnh.hosp.go.jp

Received September 25, 2007; Accepted January 4, 2008


  Abstract

Using murine colon adenocarcinoma-derived clones with different metastatic potentials, the cellular localization of matrix metalloporteinase-9 (MMP-9) and its role in the cell motility were examined. Highly metastatic LuM1 clone aggressively invaded into adjacent tissue in vivo, but low metastatic NM11 clone did not. As compared with the NM11 clone, the LuM1 clone expressed and secreted a remarkably large amount of MMP-9, and exhibited higher abilities of cell migration and invasion in vitro, which were suppressed by MMP-2/MMP-9 Inhibitor IV. MMP-9, exhibiting high affinity to heparin, was demonstrated to be condensed on tips of cellular podia. Treatment of the cells with heparitinase-I or heparin resulted in release of MMP-9 from the cell surface, which caused concomitant suppression of their motility to a similar level to that with the MMP inhibitor. Immunoprecipitation of an LuM1 cell lysate with an anti-MMP-9 antibody resulted in coprecipitation of phosphatidylinositol phospholipase C-susceptible heparan sulfate proteoglycans having 66 and 64 kDa core proteins. Taken together, the present results demonstrate that secreted MMP-9 associates with glypican-like proteoglycans through their heparan sulfate chains, and plays a crucial role in cell motility of LuM1 cells.

Key Words: cell motility, cell surface heparan sulfate, glypican, invasion, matrix metalloproteinase-9


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