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J. Biol. Chem., Vol. 279, Issue 21, 21888-21896, May 21, 2004

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Hyaluronan Cell Surface Binding Is Induced by Type I Collagen and Regulated by Caveolae in Glioma Cells^*

Borhane Annabi¶, Sébastien Thibeault¶||, Robert Moumdjian**, and Richard Béliveau||

From the Laboratoire d'Oncologie Moléculaire, Chemistry Department, Université du Québec à Montréal, the ^||Laboratoire de Médecine Moléculaire, Centre de Cancérologie Charles-Bruneau, Hôpital Sainte-Justine-Université du Québec a Montréal, and the ^**Department of Surgery, Hôpital Notre-Dame, Montreal, Quebec H2L 4M1, Canada

Hyaluronan (HA) is a component of the brain extracellular matrix environment that is synthesized and secreted by glioma cells. The primary cell surface receptor for HA is CD44, a membrane glycoprotein that is functionally regulated by a membrane type 1 matrix metalloproteinase (MT1-MMP). Both CD44 and MT1-MMP are partially located in Triton X-100-insoluble domains, but no functional link has yet been established between them. In the present study, we studied the regulation of HA cell surface binding in U-87 glioma cells. We show that an MMP-dependent mechanism regulates the intrinsic cell surface binding of HA as ilomastat, a broad MMP inhibitor, increased HA binding to glioma cells. HA binding was also rapidly and specifically up-regulated by 3-fold by type I collagen in U-87 cells, which also induced a significant morphological reorganization associated with the activation of a latent form of MMP-2 through a MT1-MMP-mediated mechanism. Interestingly, caveolae depletion with a cell surface cholesterol-depleting agent -cyclodextrin triggered an additional increase (9-fold) in the binding of HA, in synergy with type I collagen. On the other hand, HA cell surface binding was diminished by the MEK inhibitor PD98059 and by the overexpression of a recombinant, wild type MT1-MMP, whereas its cytoplasmic-deleted form had no effect. Taken together, our results suggest that MT1-MMP regulates, through its cytoplasmic domain, the cell surface functions of CD44 in a collagen-rich pericellular environment. Additionally, we describe a new molecular mechanism regulating the invasive potential of glioma cells involving a MT1-MMP/CD44/caveolin interaction, which could represent a potential target for anti-cancer therapies.

Received for publication, December 15, 2003 , and in revised form, March 4, 2004.

^* This work was supported by a grant from the Canadian Institutes of Health Research (CIHR) (to R. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Holder of a Canada Research Chair in Molecular Oncology (Tier II) from the CIHR.

^¶ These authors contributed equally to this work.

To whom correspondence and reprint requests should be addressed: Laboratoire de Médecine Moléculaire, Université du Québec à Montréal C. P. 8888, Succursalle centre-ville, Montréal, Québec H3C 3P8, Canada. Tel.: 514-987-3000 (ext. 8551); Fax: 514-987-0246; E-mail: oncomol{at}nobel.si.uqam.ca.

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