| Invasion-associated MMP-2 and MMP-9 are up-regulated intracellularly in concert with apoptosis linked to melanoma cell detachment. | |
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MedLine Citation:
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PMID: 16170665 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Matrix metalloproteinases, like MMP-2 and MMP-9 gelatinases, show multiple functions as extracellular/cell-surface enzymes, and are broadly recognised for their matrix-degrading ability and involvement in cell motility. Given that adherent cells have reduced attachment during migration and also detach from their substratum during apoptosis, we now investigated whether extracellular matrix-bound gelatinases and intracellular MMP-2 and MMP-9 are modified with progression of death-inducing stimuli. This report shows that melanoma cells undergoing death in response to 2-acetyl furanonaphtoquinone (FNQ) as evidenced by greater Annexin V binding, increased cytosolic expression of pro-MMP-2 and intracellular activation of particulate MMP-9. These changes were associated with early activation of a substrate-attached 40 kDa gelatinase reciprocal with changes in extracellular matrix-bound activated MMP-2. A subsequent activation of secreted MMP-9 and induction of apoptosis-associated fragmentation of poly ADP-Ribose polymerase (PARP) correlated with cell detachment. Our data suggests that intracellularly activated gelatinases may cleave survival-associated substrates other than gelatin that share the Gly-Leu/Iso-Pro like collagen-binding acetylcholinesterase, thereby linking them to apoptosis associated with cell detachment. |
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Authors:
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Ana Maria Mendes Pereira; Mary Strasberg-Rieber; Manuel Rieber |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Clinical & experimental metastasis Volume: 22 ISSN: 0262-0898 ISO Abbreviation: Clin. Exp. Metastasis Publication Date: 2005 |
Date Detail:
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Created Date: 2005-09-19 Completed Date: 2005-12-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8409970 Medline TA: Clin Exp Metastasis Country: Netherlands |
Other Details:
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Languages: eng Pagination: 285-95 Citation Subset: IM |
Affiliation:
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Laboratory of Tumor Cell Biology, Centre for Microbiology and Cell Biology, IVIC, Apartado 21827, Caracas, 1020 A, Venezuela. mrieber@ivic.ve |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Annexin A5 / metabolism Apoptosis* Cell Line, Tumor Cell Membrane / enzymology Enzyme Activation Extracellular Matrix / drug effects, enzymology Humans Matrix Metalloproteinase 2 / analysis, metabolism* Matrix Metalloproteinase 9 / analysis, metabolism* Melanoma / enzymology*, pathology Mice Naphthoquinones / pharmacology Neoplasm Invasiveness Poly(ADP-ribose) Polymerases / metabolism Proto-Oncogene Proteins c-bcl-2 / metabolism Skin Neoplasms / enzymology*, pathology Up-Regulation Water / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Annexin A5; 0/Naphthoquinones; 0/Proto-Oncogene Proteins c-bcl-2; 7732-18-5/Water; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.4.24.24/Matrix Metalloproteinase 2; EC 3.4.24.35/Matrix Metalloproteinase 9 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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