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A Cysteine Proteinase, Which Cleaves Human C3, the Third Component of Complement, Is Involved in Tumorigenicity and Metastasis of Human Melanoma¹

Immunochimie des Régulations Cellulaires et des Interactions Virales, INSERM U.354, Centre INSERM, Hôpital Saint-Antoine, 184 rue du Faubourg, 75012 Paris, France [D. J., F. R-L., J. H., R. F.], and Department of Cell Biology, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030 [M. B-E., S. H., K. X.]

The DM-4 human melanoma cell line, which is highly metastatic in nude mice, expresses a C3-cleaving activity that proteolyzes labeled as well as unlabeled human C3. This C3-cleaving activity is a cysteine proteinase characterized by a M_r 41,000. The p41 proteinase shares antigenis determinants with murine p39 procathepsin-L and human procathepsin-L. Preincubation of DM-4 cells with anti-p39 F(ab')₂ induced up to 45% decrease in their complement resistance. Pretreatment of DM-4 cells with anti-p39 Ab strongly inhibited their tumorigenicity and significantly decreased their metastatic potential in nude mice. Thus, the p41 C3-cleaving proteinase contributes to tumorigenicity and metastasis of human melamoma DM-4 cells.

¹ This work was supported by Institut National de la Sante et de la Recherche Medicale, Association pour la Recherche contre le Cancer, Comité de Paris de la Ligue Nationale Francaise contre le Cancer (to R.F.), and in part by NIH grant CA 41525 (to M. B-E.).

² To whom requests for reprints should be addressed.

Received 10/31/95. Accepted 11/29/95.

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