The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1
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.
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Cites
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Self-citationThe Stromal Proteinase MMP3/Stromelysin-1 Promotes Mammary Carcinogenesis
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Self-citationN-Cadherin Promotes Motility in Human Breast Cancer Cells Regardless of Their E-Cadherin Expression
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The metalloproteinase matrilysin is a target of β-catenin transactivation in intestinal tumors
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Self-citationInflammatory Bowel Disease and Adenomas in Mice Expressing a Dominant Negative N-Cadherin
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Cited by
New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
How Matrix Metalloproteinases Regulate Cell Behavior
Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959
Matrix metalloproteinases and the regulation of tissue remodelling
Page-McCaw, A., Ewald, A. J., & Werb, Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2125 · Cited by 2,630
Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
Gialeli, C., Theocharis, A. D., & Karamanos, N. K. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07919.x · Cited by 1,607
Metadata
- Authors
- Noë, V., Fingleton, B., Jacobs, K., Crawford, H. C., Vermeulen, S., Steelant, W., Bruyneel, E., Matrisian, L. M., & Mareel, M.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2001-01-01
- Volume
- 114
- Issue
- 1
- Pages
- 111-118
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1919303367
- Cited by
- 695
- References
- 43
- FWCI
- 13.08
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. https://app.cochat.ai/papers/10.1242/jcs.114.1.111
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- Noë, V., Fingleton, B., Jacobs, K., Crawford, H. C., Vermeulen, S., Steelant, W., Bruyneel, E., Matrisian, L. M., & Mareel, M. (2001). Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. Journal of Cell Science. https://doi.org/10.1242/jcs.114.1.111
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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