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J. Biol. Chem., Vol. 278, Issue 6, 3639-3647, February 7, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/6/3639    most recent M207483200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Palmieri, D. Articles by Manduca, P. Search for Related Content PubMed PubMed Citation Articles by Palmieri, D. Articles by Manduca, P. Social Bookmarking                      What's this?

Pro-collagen I COOH-terminal Trimer Induces Directional Migration and Metalloproteinases in Breast Cancer Cells^*

Daniela Palmieri, Silvia Poggi, Valentina Ulivi, GianLuigi Casartelli^§, and Paola Manduca^¶

From the  Genetica, Dipartimento di Oncologia, Biologia e Genetica, Università di Genova, 26 C. Europa and ^§ Istituto per la Ricerca sul Cancro, Viale Benedetto XIV, Genova 16132, Italy

Breast and prostatic carcinomas, melanoma, and endothelial cell lines are chemoattracted by medium conditioned by mature osteoblasts. The chemoattractant for endothelial cells was identified with C3, carboxyl-terminal trimer of pro-collagen type I. We report that C3 induces directional migration and proliferation, the expression of tissue inhibitor of metalloproteinases-2, pro-metalloproteinase-2 and -9, and their activation in MDA MB231 cells, without changing the expression of tissue inhibitor of metalloproteinases-1 and of metalloproteinase-14. Antiserum against metalloproteinase-2 or -9 or -14, tissue inhibitor of metalloproteinases-1, or GM6001 inhibits the C3-induced migration. Urokinase and its receptor are detected and unchanged upon exposure to C3. The antibody against urokinase or addition of plasminogen activator inhibitor inhibits migration. Blocking antibodies to integrins ₂, ₆, ₁, and ₃ inhibit chemotaxis and do not change urokinase and urokinase receptor expression. Blockage of ₂, ₁, and ₃ integrins affect differently the induction by C3 of pro-metalloproteinase-2 and -9 and of tissue inhibitor of metalloproteinases-2. Chemotaxis to C3 is also inhibited by genistein, by pertussis toxin, which also inhibits C3-induced pro-metalloproteinase -2 and -9, but not urokinase expression. Wortmannin partially inhibits C3-induced cell migration. Other, but not all, breast carcinoma lines tested responded to C3 with migration and pro-metalloproteinase-2 induction. Presently C3 is the only agent known to induce migration specifically of both endothelial and breast carcinoma cells. The mitogenic and motogenic role of C3 in vitro might prefigure a role in in vivo carcinogenesis and in the establishment of metastasis.

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