Journal ArticleDOI
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 F.A. Steelant,Erik Bruyneel,Lynn M. Matrisian,Marc Mareel +8 more
TLDR
The results suggest a novel mechanism by which metalloproteinases can influence invasion, as indicated by induction of invasion into collagen type I and inhibition of E-cadherin-dependent cell aggregation.Abstract:
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.read more
Citations
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New functions for the matrix metalloproteinases in cancer progression
Mikala Egeblad,Zena Werb +1 more
TL;DR: It is shown that the MMPs have functions other than promotion of invasion, have substrates other than components of the extracellular matrix, and that they function before invasion in the development of cancer.
Journal ArticleDOI
Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
Robert Visse,Hideaki Nagase +1 more
TL;DR: This review describes the members of the matrixin family and discusses substrate specificity, domain structure and function, the activation of proMMPs, the regulation of matrixin activity by tissue inhibitors of metalloproteinases, and their pathophysiological implication.
Journal ArticleDOI
How Matrix Metalloproteinases Regulate Cell Behavior
Mark D. Sternlicht,Zena Werb +1 more
TL;DR: Recent advances shed light on how the structure and function of the MMPs are related and on how their transcription, secretion, activation, inhibition, localization, and clearance are controlled.
Journal ArticleDOI
Matrix metalloproteinases and the regulation of tissue remodelling
TL;DR: Recent studies in mice and flies point to essential roles of MMPs as mediators of change and physical adaptation in tissues, whether developmentally regulated, environmentally induced or disease associated.
Journal ArticleDOI
Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
TL;DR: This minireview critically evaluates the role of MMPs in relation to cancer progression, and highlights the challenges, as well as future prospects, for the design, development and efficacy of M MPIs.
References
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Journal ArticleDOI
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Jacques J. Peschon,Jennifer L. Slack,Pranitha Reddy,Kim L. Stocking,Susan W. Sunnarborg,David C. Lee,William E. Russell,Beverly J. Castner,Richard S. Johnson,Jeffrey N. Fitzner,Rogely W. Boyce,Nicole Nelson,Carl J. Kozlosky,Martin F. Wolfson,Charles Rauch,Douglas P. Cerretti,Raymond J. Paxton,Carl J. March,Roy A. Black +18 more
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