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The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis

Article Abstract:

Phenotypically normal mammary epithelial cells with tetracycline-regulated expression of matrix metalloproteinases (MMPs)/stromelysin-1 (Str1) are found to be capable of inducing phenotypic conversion and malignant transformation of mammary epithelial cells. Analysis shows that such type of cells produce invasive mesenchymal-like tumors with Str1. Evidence reveals that initiation of tumor and alteration of neoplastic risk can be attributed to Str1.

Author: Werb, Zena, Huey, Bing, Gray, Joe W., Bissell, Mina J., Pinkel, Dan, Sternlicht, Mark D., Lochter, Andre, Sympson, Carolyn J., Rougier, Jean-Philippe
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
Abnormalities, Breast cancer, Growth, Epithelial cells, Transforming growth factors, Tumors, Dyskeratosis congenita

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ECM and cell surface proteolysis: regulating cellular ecology

Article Abstract:

Substrate unfolding and remodeling is an intermediate step in an energy-dependent degradation, to allow substrate entry into the proteolytic cavity. The synergy between adhesion and proteolysis has been advanced by discovery of the association between proteases and signal transduction. ATPase component mediate the conformational changes that facilitate entry of the substrate into the proteolytic components of the protease.

Author: Werb, Zena
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
Cellular signal transduction, Cell membranes, Plasma membranes, Proteolysis

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The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo

Article Abstract:

Research demonstrates the functional interactions between gelatinase B/MMP-9 and neutrophil elastase in the blister formation in bullous pemphigoid disease condition. Data indicate that serpin alpha1-proteinase inhibitor acts as a substrate of the former enzyme, which is cleaved in vivo during dermal-epidermal separation leading to blisters.

Author: Diaz, Luis A., Werb, Zena, Liu, Zhi, Zhou, Xiaoye, Shapiro, Steven D., Shipley, J. Michael, Twining, Sally S., Senior, Robert M.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
United States, Statistical Data Included, Physiological aspects, Protein research, Enzyme inhibitors, Bullous pemphigoid, Blisters

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Subjects list: Research, Analysis
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