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Filip Ryniers, Christophe Stove, Marc Goethals, Liesbeth Brackenier, Veerle Noë, Marc Bracke, Joël Vandekerckhove, Marc Mareel, Erik Bruyneel

Plasmin Produces an E-Cadherin Fragment That Stimulates Cancer Cell Invasion

Matrix metalloproteases from the cell surface cleave an 80 kDa Ecadherin fragment (sECAD) that induces invasion of cancer cells into collagen type I and inhibits cellular aggregation. Conditioned media from MDCKts.srcCl2 cells at 40 C and 35 C, PCm.src5 and COLO-16 cells at 37 C contained spontaneously released sECAD; these 48 h old conditioned media were capable of inhibiting Ecadherin functions in a paracrine way. Here we show direct cleavage of the extracellular domain of Ecadherin by the serine protease plasmin. sECAD released by plasmin inhibits Ecadherin functions as evidenced by induction of invasion into collagen type I and inhibition of cellular aggregation. This functional inhibition by sECAD was reversed by aprotinin or by immunoadsorption on protein Sepharose 4 fast flow beads with antibodies against the extracellular part of Ecadherin. Our results demonstrate that plasmin produces extracellular Ecadherin fragments which regulate Ecadherin function in cells containing an intact Ecadherin/ catenin complex.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 383, 01/2002
Pages: 159 - 165

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