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Journal of Dental Research
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Biological

MMP-9 Activation by Tumor Trypsin-2 Enhances in vivo Invasion of Human Tongue Carcinoma Cells

P. Nyberg1, M. Moilanen1, A. Paju2, A. Sarin1, U.-H. Stenman2, T. Sorsa3 and T. Salo1,*

1 Departments of Diagnostics and Oral Medicine, Institute of Dentistry, University of Oulu, PO Box 5281, FIN-90014, Oulu, Finland;
2 Department of Clinical Chemistry, Helsinki University Central Hospital, FIN-00029, Helsinki, Finland; and
3 Biomedicum and Oral Pathology Unit, Institute of Dentistry, Laboratory Diagnostics, Helsinki University Central Hospital, University of Helsinki, FIN-00014, Helsinki, Finland;

Correspondence: *corresponding author, Tuula.Salo{at}oulu.fi

Various human cancer cells express tumor-associated trypsinogen-2 (TAT-2), which can efficiently activate matrix metalloproteinases (MMPs) in vitro. MMP-2 and MMP-9 are particularly associated with the invasive malignant potential of several tumors. To investigate the role of TAT-2 in tumor invasion, we overexpressed TAT-2 in two malignant human squamous cell carcinoma cell lines of tongue and in non-malignant human papilloma virus transformed gingival keratinocytes. The TAT-2 overexpression significantly increased the levels of active MMP-9 in the most malignant cell line. TAT-2-transfected cells intravasated (invaded blood vessels) up to 60% more efficiently than did the control cells in an in vivo chick embryo chorioallantoic membrane invasion model. This increased intravasation was almost completely abolished by a specific tumor-associated trypsin inhibitor (TATI). These results indicate that TAT-2 has a role in the invasive growth of tumors, either alone or in cascade with gelatinases, especially by generating active MMP-9.

Key Words: MMP-9 • tumor-associated trypsin-2 • tumor invasion

Journal of Dental Research, Vol. 81, No. 12, 831-35 (2002)
DOI: 10.1177/154405910208101207
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P. Nyberg, P. Heikkila, T. Sorsa, J. Luostarinen, R. Heljasvaara, U.-H. Stenman, T. Pihlajaniemi, and T. Salo
Endostatin Inhibits Human Tongue Carcinoma Cell Invasion and Intravasation and Blocks the Activation of Matrix Metalloprotease-2, -9, and -13
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