title: Expression and regulation of MMP-20 in human tongue carcinoma cells.
abstract: 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 beta-casein. This implies that MMP-20 not only participates in dental matrix remodeling but is also present in tongue carcinoma cells.
authors.affiliation: Department of Diagnostics and Oral Medicine, Institute of Dentistry, University of Oulu, Finland.
authors.forename: A
authors.initials: A
authors.lastname: Väänänen
authors.forename: R
authors.initials: R
authors.lastname: Srinivas
authors.forename: M
authors.initials: M
authors.lastname: Parikka
authors.forename: H
authors.initials: H
authors.lastname: Palosaari
authors.forename: J D
authors.initials: JD
authors.lastname: Bartlett
authors.forename: K
authors.initials: K
authors.lastname: Iwata
authors.forename: R
authors.initials: R
authors.lastname: Grenman
authors.forename: U H
authors.initials: UH
authors.lastname: Stenman
authors.forename: T
authors.initials: T
authors.lastname: Sorsa
authors.forename: T
authors.initials: T
authors.lastname: Salo
mesh_terms: D053523:Amelogenin; D002273:Carcinogens / Q000494:pharmacology; D002294:Carcinoma, Squamous Cell / Q000201:enzymology*; D002364:Caseins / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002460:Cell Line; D024042:Collagen Type I / Q000378:metabolism; D024043:Collagen Type II / Q000378:metabolism; D024141:Collagen Type IV / Q000378:metabolism; D003746:Dental Enamel Proteins / Q000235:genetics; D004792:Enzyme Precursors / Q000187:drug effects / Q000235:genetics; D005353:Fibronectins / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D007797:Laminin / Q000378:metabolism; D053519:Matrix Metalloproteinase 20; D061965:Matrix Metalloproteinase Inhibitors; D020782:Matrix Metalloproteinases / Q000187:drug effects / Q000235:genetics*; D012333:RNA, Messenger / Q000187:drug effects / Q000235:genetics; D011994:Recombinant Proteins; D019063:Tenascin / Q000378:metabolism; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014062:Tongue Neoplasms / Q000201:enzymology*; D016212:Transforming Growth Factor beta / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology; D014407:Tumor Cells, Cultured; D015854:Up-Regulation / Q000187:drug effects; D000097794:Kalinin
chemical_list: D053523:Amelogenin; D002273:Carcinogens; D002364:Caseins; D015815:Cell Adhesion Molecules; D024042:Collagen Type I; D024043:Collagen Type II; D024141:Collagen Type IV; D003746:Dental Enamel Proteins; D004792:Enzyme Precursors; D005353:Fibronectins; D007797:Laminin; D053519:Matrix Metalloproteinase 20; D061965:Matrix Metalloproteinase Inhibitors; D020782:Matrix Metalloproteinases; D012333:RNA, Messenger; D011994:Recombinant Proteins; D019063:Tenascin; D013755:Tetradecanoylphorbol Acetate; D016212:Transforming Growth Factor beta; D014357:Trypsin; D000097794:Kalinin; C121346:laminin 1; C507111:MMP20 protein, human