Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1

Veerle Noë, Barbara Fingleton, Kathleen Jacobs, Howard C. Crawford, Stefan Vermeulen, Wim Steelant, Erik Bruyneel, Lynn M. Matrisian, Marc Mareel

Research output: Contribution to journalArticlepeer-review

548 Scopus citations


The function of many transmembrane molecules can be altered by cleavage and subsequent release of their ectodomains. We have investigated ectodomain cleavage of the cell-cell adhesion and signal-transducing molecule E-cadherin. The E-cadherin ectodomain is constitutively shed from the surface of MCF-7 and MDCKts.srcC12 cells in culture. Release of the 80 kDa soluble E-cadherin fragment is stimulated by phorbol-12-myristate-13-acetate and is inhibited by overexpression of the tissue inhibitor of metalloproteinases-2. The metalloproteinases matrilysin and stromelysin-1 both cleave E-cadherin at the cell surface and release sE-CAD into the medium. The soluble E-cadherin fragment thus released inhibits E-cadherin functions in a paracrine way, as indicated by induction of invasion into collagen type I and inhibition of E-cadherin-dependent cell aggregation. Our results, therefore, suggest a novel mechanism by which metalloproteinases can influence invasion.

Original languageEnglish (US)
Pages (from-to)111-118
Number of pages8
JournalJournal of cell science
Issue number1
StatePublished - 2001


  • E-cadherin/catenin complex
  • Ectodomain shedding
  • Invasion
  • Matrix metalloproteinase
  • Proteolysis

ASJC Scopus subject areas

  • Cell Biology


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