Extrinsic regulators of epithelial tumor progression: metalloproteinases (Q33840437)

29 July 2017

title

Extrinsic regulators of epithelial tumor progression: metalloproteinases (English)

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29 July 2017

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Bergers G

1

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29 July 2017

Coussens LM

series ordinal

2

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29 July 2017

publication date

1 February 2000

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Current Opinion in Genetics & Development

29 July 2017

published in

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29 July 2017

volume

10

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29 July 2017

issue

1

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29 July 2017

page(s)

120-127

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publication type of scholarly work

29 July 2017

review article

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Matrix metalloproteinases and the development of cancer

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The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

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ADAMs: focus on the protease domain

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METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity

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ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family

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Insulin-like Growth Factor II Is Focally Up-regulated and Functionally Involved as a Second Signal for Oncogene-induced Tumorigenesis

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Insulin-like growth factor II signaling in neoplastic proliferation is blocked by transgenic expression of the metalloproteinase inhibitor TIMP-1.

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IGFBPs and neoplastic models. New concepts for roles of IGFBPs in regulation of cancer cell growth

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Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3

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The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells

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Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis

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The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases

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A secreted FGF-binding protein can serve as the angiogenic switch in human cancer.

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Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors.

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Inflammatory mast cells up-regulate angiogenesis during squamous epithelial carcinogenesis

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A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells

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Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha

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An essential role for ectodomain shedding in mammalian development

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Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor

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Matrix Metalloproteinase-3 Releases Active Heparin-binding EGF-like Growth Factor by Cleavage at a Specific Juxtamembrane Site

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Matrix Metalloproteinase Stromelysin-1 Triggers a Cascade of Molecular Alterations That Leads to Stable Epithelial-to-Mesenchymal Conversion and a Premalignant Phenotype in Mammary Epithelial Cells

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The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

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The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis

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Collagenase expression in transgenic mouse skin causes hyperkeratosis and acanthosis and increases susceptibility to tumorigenesis

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Angiostatin: A novel angiogenesis inhibitor that mediates the suppression of metastases by a lewis lung carcinoma

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Effects of angiogenesis inhibitors on multistage carcinogenesis in mice

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Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma

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Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance

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Identifiers

DOI

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29 July 2017

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