Abstract:
:Matrix metalloproteases from the cell surface cleave an 80 kDa E-cadherin fragment (sE-CAD) that induces invasion of cancer cells into collagen type I and inhibits cellular aggregation. Conditioned media from MDCKts.srcCl2 cells at 40 degrees C and 35 degrees C, PCm.src5 and COLO-16 cells at 37 degrees C contained spontaneously released sE-CAD; these 48 h old conditioned media were capable of inhibiting E-cadherin functions in a paracrine way. Here we show direct cleavage of the extracellular domain of E-cadherin by the serine protease plasmin. sE-CAD released by plasmin inhibits E-cadherin functions as evidenced by induction of invasion into collagen type I and inhibition of cellular aggregation. This functional inhibition by sE-CAD was reversed by aprotinin or by immunoadsorption on protein Sepharose 4 fast flow beads with antibodies against the extracellular part of E-cadherin. Our results demonstrate that plasmin produces extracellular E-cadherin fragments which regulate E-cadherin function in cells containing an intact E-cadherin/catenin complex.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Ryniers F,Stove C,Goethals M,Brackenier L,Noë V,Bracke M,Vandekerckhove J,Mareel M,Bruyneel Edoi
10.1515/BC.2002.016keywords:
subject
Has Abstractpub_date
2002-01-01 00:00:00pages
159-65issue
1eissn
1431-6730issn
1437-4315journal_volume
383pub_type
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