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Expression and Regulation of MMP-20 in Human Tongue Carcinoma Cells

Department of Diagnostics and Oral Medicine, Institute of Dentistry, University of Oulu, PO Box 5281, FIN-90014 Oulu, Finland

R. Srinivas

Faculty of Medicine, University of Helsinki, Helsinki, Finland

M. Parikka

Department of Diagnostics and Oral Medicine, Institute of Dentistry, University of Oulu, PO Box 5281, FIN-90014 Oulu, Finland

H. Palosaari

Department of Diagnostics and Oral Medicine, Institute of Dentistry, University of Oulu, PO Box 5281, FIN-90014 Oulu, Finland

J.D. Bartlett

Department of Biomineralization & Harvard-Forsyth Department of Oral Biology, Forsyth Institute, Boston, MA, USA

K. Iwata

Biopharmaceutical Department, Fuji Chemical Industries Ltd., Chokeiji, Takaoka, Toyama, Japan

R. Grenman

Department of Otolaryngology, Turku University Hospital, Turku, Finland

U.-H. Stenman

Department of Clinical Chemistry, Helsinki University Hospital, Helsinki, Finland

T. Sorsa

Faculty of Medicine, University of Helsinki, Helsinki, Finland

T. Salo

Department of Diagnostics and Oral Medicine, Institute of Dentistry, University of Oulu, PO Box 5281, FIN-90014 Oulu, Finland, Oulu University Hospital, Oulu, Finland, Tuula.Salo{at}oulu.fi

Human matrix metalloproteinase-20 (MMP-20, enamelysin) fragments the enamel-specific protein amelogenin and has been shown to be synthesized exclusively by odontoblasts and ameloblasts and in certain odontogenic tumors. Here we demonstrate, for the first time, the expression of MMP-20 mRNA and protein in two carcinoma cell lines originating from the tongue. Treatment of the SCC-25 and HSC-3 cells with phorbol 12-myristate 13-acetate (10 nmol/L) up-regulated MMP-20 mRNA and protein expression by up to 1.6-fold, but transforming growth factor beta (10 ng/mL) had no effect. The latent proform of recombinant (r) human MMP-20 was converted by tumor-related trypsin-2. Activated rMMP-20 did not degrade type I or type II collagen, but efficiently hydrolyzed fibronectin, type IV collagen, laminin-1 and -5, tenascin-C, and (3-casein. This implies that MMP-20 not only participates in dental matrix remodeling but is also present in tongue carcinoma cells.

Key Words: matrix metalloproteinases • enamelysin • tongue carcinoma • trypsin-2.

Journal of Dental Research, Vol. 80, No. 10, 1884-1889 (2001)
DOI: 10.1177/00220345010800100501


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