Document Detail

Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP).
MedLine Citation:
PMID:  8647259     Owner:  NLM     Status:  MEDLINE    
Gelatinase A is secreted as a proenzyme (progelatinase A) which is activated and bound on the surface of tumor and normal cells. We have reported that the expression of a membrane-type-1-matrix metalloproteinase (MT1-MMP) induces activation of progelatinase A. Here we demonstrate that the expression of MT1-MMP in COS-1 cells induces cell-surface binding of progelatinase A which is consequently processed to an intermediate form. Processing from the intermediate to the fully active form is dependent on the gelatinase A concentration. These results suggest that the cell-surface binding concentrates the gelatinase A intermediate form locally to allow autoproteolytic processing to the fully active form.
H Sato; T Takino; T Kinoshita; K Imai; Y Okada; W G Stetler Stevenson; M Seiki
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  FEBS letters     Volume:  385     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1996 May 
Date Detail:
Created Date:  1996-07-23     Completed Date:  1996-07-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  238-40     Citation Subset:  IM    
Department of Molecular Virology and Oncology, Cancer Research Institute, Kanazawa University, Japan.
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MeSH Terms
Blotting, Western
Cell Membrane / metabolism*
Collagenases / genetics,  metabolism*
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
Enzyme Precursors / genetics,  metabolism*
Gelatinases / genetics,  metabolism*
Gene Expression Regulation, Enzymologic
Matrix Metalloproteinase 1
Matrix Metalloproteinase 2
Metalloendopeptidases / genetics,  metabolism*
Protein Binding
Protein Processing, Post-Translational
Tumor Cells, Cultured
Reg. No./Substance:
0/Enzyme Precursors; EC 3.4.24.-/Collagenases; EC 3.4.24.-/Gelatinases; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.-/progelatinase; EC Metalloproteinase 2; EC Metalloproteinase 1

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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