Document Detail


Matrix metalloproteinase-9 (92 kDa gelatinase/type IV collagenase) from U937 monoblastoid cells: correlation with cellular invasion.
MedLine Citation:
PMID:  8314909     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The role of matrix metalloproteinase-9 (MMP-9, 92 kDa gelatinase/type IV collagenase) in invasion of mononuclear phagocytes was studied with U937 monoblastoid cells. 12-o-tetradecanoyl 13-phorbol acetate (TPA) differentiated them to macrophage-like cells with induction of MMP-9, and tumor necrosis factor alpha (TNF alpha) and interleukin-1 alpha (IL-1 alpha) stimulated the production of MMP-9 by TPA-treated cells. TNF alpha also induced the production of MMP-9 by TPA-untreated U937 cells without morphological differentiation. Other agents including dimethyl sulfoxide (DMSO), all-trans-retinoic acid (all-trans-RA), platelet-derived growth factor and 3';5'-cyclic monophosphate had no effects on MMP-9 production by TPA-treated or -untreated cells, but all-trans-RA and DMSO did have a morphological effect on the differentiation of the cells. These data suggest that MMP-9 production by U937 cells is regulated by a mechanism independent of the differentiation to macrophage-like cells. MMP-9 was purified to homogeneity as an inactive zymogen with M(r) 92,000 (proMMP-9) from TPA-differentiated U937 cells treated with TNF alpha. ProMMP-9 was activated by p-aminophenylmercuric acetate (APMA) generating an active species of M(r) 67,000. Trypsin and cathepsin G also attained activation of the zymogen to its full activity obtained by APMA activation, but plasmin, leukocyte elastase, thrombin and plasma kallikrein had no ability to activate it. APMA-activated MMP-9 degraded type I gelatin readily and cleaved native collagen types III, IV and V. Invasion assays using reconstituted basement membrane coupled with a type IV collagenolysis assay showed good correlations between invasiveness, type IV collagenolysis and proMMP-9 production. Invasion was significantly inhibited by EDTA, alpha 2-macroglobulin and tissue inhibitor of metalloproteinases-1, but not by inhibitors of cathepsin G and leukocyte elastase. These data suggest that MMP-9 plays an important role in the invasion of mononuclear phagocytes through basement membranes.
Authors:
H Watanabe; I Nakanishi; K Yamashita; T Hayakawa; Y Okada
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cell science     Volume:  104 ( Pt 4)     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  1993 Apr 
Date Detail:
Created Date:  1993-07-28     Completed Date:  1993-07-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  991-9     Citation Subset:  IM    
Affiliation:
Department of Pathology, School of Medicine, Kanazawa University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Basement Membrane / pathology
Cell Differentiation / physiology
Cell Movement / physiology
Collagenases / biosynthesis,  physiology*
Enzyme Activation / drug effects
Enzyme Induction / drug effects
Enzyme Precursors / biosynthesis,  isolation & purification
Humans
Macrophages / drug effects,  enzymology*
Matrix Metalloproteinase 9
Monocytes / drug effects,  enzymology*
Serine Endopeptidases / metabolism
Tetradecanoylphorbol Acetate
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Enzyme Precursors; 16561-29-8/Tetradecanoylphorbol Acetate; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.24.-/Collagenases; 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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