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Glioblastoma infiltration into central nervous system tissue in vitro: involvement of a metalloprotease.
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MedLine Citation:
PMID:  3198688     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Differentiated oligodendrocytes and central nervous system (CNS) myelin are nonpermissive substrates for neurite growth and for cell attachment and spreading. This property is due to the presence of membrane-bound inhibitory proteins of 35 and 250 kD and is specifically neutralized by monoclonal antibody IN-1 (Caroni, P., and M. E. Schwab. 1988. Neuron. 1:85-96). Using rat optic nerve explants, CNS frozen sections, cultured oligodendrocytes or CNS myelin, we show here that highly invasive CNS tumor line (C6 glioblastoma) was not inhibited by these myelin-associated inhibitory components. Lack of inhibition was due to a specific mechanism as the metalloenzyme blocker 1,10-phenanthroline and two synthetic dipeptides containing metalloprotease-blocking sequences (gly-phe, tyr-tyr) specifically impaired C6 cell spreading on CNS myelin. In the presence of these inhibitors, C6 cells were affected by the IN-1-sensitive inhibitors in the same manner as control cells, e.g., 3T3 fibroblasts or B16 melanomas. Specific blockers of the serine, cysteine, and aspartyl protease classes had no effect. C6 cell spreading on inhibitor-free substrates such as CNS gray matter, peripheral nervous system myelin, glass, or poly-D-lysine was not sensitive to 1,10-phenanthroline. The nonpermissive substrate properties of CNS myelin were strongly reduced by incubation with a plasma membrane fraction prepared from C6 cells. This reduction was sensitive to the same inhibitors of metalloproteases. In our in vitro model for CNS white matter invasion, cell infiltration of optic nerve explants, which occurred with C6 cells but not with 3T3 fibroblasts or B16 melanomas, was impaired by the presence of the metalloprotease blockers. These results suggest that C6 cell infiltrative behavior in CNS white matter in vitro occurs by means of a metalloproteolytic activity, which probably acts on the myelin-associated inhibitory substrates.
Authors:
P A Paganetti; P Caroni; M E Schwab
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of cell biology     Volume:  107     ISSN:  0021-9525     ISO Abbreviation:  J. Cell Biol.     Publication Date:  1988 Dec 
Date Detail:
Created Date:  1989-01-19     Completed Date:  1989-01-19     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0375356     Medline TA:  J Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2281-91     Citation Subset:  IM    
Affiliation:
Brain Research Institute of the University of Zurich, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Animals
Brain / pathology*
Cell Membrane / physiology
Cell Movement
Glioma / pathology*
Melanoma, Experimental / pathology
Metalloendopeptidases / antagonists & inhibitors,  physiology*
Models, Biological
Myelin Sheath / physiology
Oligodendroglia / physiology
Optic Nerve / pathology
Phenanthrolines / pharmacology
Rats
Chemical
Reg. No./Substance:
0/Phenanthrolines; 66-71-7/1,10-phenanthroline; EC 3.4.24.-/Metalloendopeptidases
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Full Text
Journal Information
Journal ID (nlm-ta): J Cell Biol
ISSN: 0021-9525
ISSN: 1540-8140
Publisher: The Rockefeller University Press
Article Information
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Print publication date: Day: 1 Month: 12 Year: 1988
Volume: 107 Issue: 6
First Page: 2281 Last Page: 2291
ID: 2115648
Publisher Id: 89066893
PubMed Id: 3198688

Glioblastoma infiltration into central nervous system tissue in vitro: involvement of a metalloprotease


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