Document Detail

Secretion of matrix metalloproteinase-2 (72 kD gelatinase/type IV collagenase = gelatinase A) by malignant human glioma cell lines: implications for the growth and cellular invasion of the extracellular matrix.
MedLine Citation:
PMID:  8740587     Owner:  NLM     Status:  MEDLINE    
Human glioma cells (T98G and A172 cell lines) were cultured on various extracellular matrix (ECM) components including type I, IV and V collagens, fibronectin, laminin, and reconstituted basement membrane (Matrigel), and the role of matrix metalloproteinases (MMPs) in their growth and invasion was examined. T98G glioma cells grew well on these ECM components and invaded the reconstituted basement membrane. In contrast, A172 glioma cells showed growth inhibition on collagen types IV and V and Matrigel without invasion of the Matrigel. Gelatin zymography and enzyme immunoassays demonstrated that T98G glioma cells, but not A172 cells, secrete a large amount of matrix metalloproteinase-2 (MMP-2, 72 kD gelatinase/type IV collagenase = gelatinase A), and this was confirmed by immunoblotting and immunohistochemistry. Of the two different tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2), T98G cells produced only TIMP-1 during culture on Matrigel, whereas A172 cells secreted both. Although both human recombinant TIMP-1 and TIMP-2 stimulated T98G cell growth slightly on Matrigel, the in vitro invasiveness was significantly reduced by only recombinant TIMP-2. These results suggest that MMP-2 plays an important role in the ECM invasion of T98G human glioma cells in vitro.
T Nakagawa; T Kubota; M Kabuto; N Fujimoto; Y Okada
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of neuro-oncology     Volume:  28     ISSN:  0167-594X     ISO Abbreviation:  J. Neurooncol.     Publication Date:  1996 Apr 
Date Detail:
Created Date:  1996-10-31     Completed Date:  1996-10-31     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8309335     Medline TA:  J Neurooncol     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  13-24     Citation Subset:  IM    
Department of Neurosurgery, Fukui Medical School, Japan.
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MeSH Terms
Brain Neoplasms
Cell Division / drug effects
Cell Movement / physiology
Collagenases / physiology,  secretion
Drug Combinations
Extracellular Matrix / pathology
Gelatinases / physiology,  secretion*
Glycoproteins / physiology,  secretion
Matrix Metalloproteinase 1
Matrix Metalloproteinase 2
Matrix Metalloproteinase 3 / physiology,  secretion
Matrix Metalloproteinase 9
Metalloendopeptidases / physiology,  secretion*
Neoplasm Invasiveness / pathology
Neoplasm Proteins / physiology,  secretion
Protease Inhibitors / metabolism
Proteins / physiology,  secretion
Tissue Inhibitor of Metalloproteinase-2
Tissue Inhibitor of Metalloproteinases
Tumor Cells, Cultured / cytology,  drug effects,  secretion
Reg. No./Substance:
0/Drug Combinations; 0/Glycoproteins; 0/Laminin; 0/Neoplasm Proteins; 0/Protease Inhibitors; 0/Proteins; 0/Proteoglycans; 0/Tissue Inhibitor of Metalloproteinases; 119978-18-6/matrigel; 127497-59-0/Tissue Inhibitor of Metalloproteinase-2; 9007-34-5/Collagen; EC 3.4.24.-/Collagenases; EC 3.4.24.-/Gelatinases; EC 3.4.24.-/Metalloendopeptidases; EC Metalloproteinase 3; EC Metalloproteinase 2; EC Metalloproteinase 9; EC Metalloproteinase 1

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

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