Low molecular weight inhibitors of matrix metalloproteinases can enhance the expression of matrix metalloproteinase-2 (gelatinase A) without inhibiting its activation. (Q47172154)

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scientific article published in March 2003

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English	Low molecular weight inhibitors of matrix metalloproteinases can enhance the expression of matrix metalloproteinase-2 (gelatinase A) without inhibiting its activation.	scientific article published in March 2003

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12627524%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

Low molecular weight inhibitors of matrix metalloproteinases can enhance the expression of matrix metalloproteinase-2 (gelatinase A) without inhibiting its activation (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12627524%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

Ton Schoenmaker

3

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1 November 2019

Wouter Beertsen

5

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1 November 2019

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Erika H M Kerkvliet

1

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1 November 2019

Ineke D C Jansen

2

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1 November 2019

Andy J P Docherty

4

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1 November 2019

Vincent Everts

6

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1 November 2019

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1 March 2003

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1 November 2019

1 reference

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1 November 2019

97

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1 November 2019

6

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1 November 2019

1582-1588

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1 November 2019

Matrix metalloproteinase inhibition prevents colon cancer peritoneal carcinomatosis development and prolongs survival in rats

1 reference

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Inhibition of gelatinase A (MMP-2) by batimastat and captopril reduces tumor growth and lung metastases in mice bearing Lewis lung carcinoma

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Matrix metalloproteinase (MMP) inhibition selectively decreases type II MMP activity in a murine model of pancreatic cancer

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Effect of matrix metalloproteinase inhibition on pancreatic cancer invasion and metastasis: an additive strategy for cancer control

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Differing effects of endogenous and synthetic inhibitors of metalloproteinases on intestinal tumorigenesis

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Matrix metalloproteinases-2 and 9 do not play a role in the growth of preneoplastic liver lesions in F344 rats.

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Multiple functions of tissue inhibitors of metalloproteinases (TIMPs): a new aspect involving osteoclastic bone resorption

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Tissue inhibitor of metalloproteinases (TIMP-1) stimulates the secretion of collagenase from human skin fibroblasts

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Increased TIMP-1 activity results in increased expression of gelatinases and altered cell motility

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Inhibition of bone resorption in vitro by selective inhibitors of gelatinase and collagenase

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Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme

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Metalloproteinases are not involved in the phagocytosis of collagen fibrils by fibroblasts

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Direct extraction and assay of bone tissue collagenase and its relation to parathyroid-hormone-induced bone resorption

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Quantification of matrix metalloproteinases in tissue samples

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Fluorometric analysis of DNA in cell cultures

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Gelatinase A (MMP-2) and cysteine proteinases are essential for the degradation of collagen in soft connective tissue

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Collagen breakdown in soft connective tissue explants is associated with the level of active gelatinase A (MMP-2) but not with collagenase.

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Stimulation of matrix metalloproteinase-9 expression in human fibrosarcoma cells by synthetic matrix metalloproteinase inhibitors

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Increased stromal expression of murine urokinase plasminogen activator in a human breast cancer xenograft model following treatment with the matrix metalloprotease inhibitor, batimastat

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Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes

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Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2

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Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme

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Tissue inhibitor of metalloproteinase (TIMP)-2 acts synergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (Membrane type 1)-MMP-dependent activation of pro-MMP-2.

1 reference

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7 January 2021

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inferred from DOI database lookup

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