Document Detail


Inhibition of tumour cell invasion by protease inhibitors: correlation with the protease profile.
MedLine Citation:
PMID:  9860288     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The invasive potential of eight established human tumour cell lines of different origin has been studied in the Matrigel assay. Between 25% and 70% of the cells migrated through the Matrigel layer within 24 h, indicating that invasiveness varies with the cell type. Semiquantitative measurements of the proteases MMP-2 and MMP-9, and cathepsins B and L were performed in these cell lines and the cell culture media. High invasive potential was found in those cell lines expressing high levels of cathepsins B and L or matrix metal proteases (MMP), either alone or in combination. Overexpression of one of these enzymes is enough to explain a high invasive potential of a cell line. Selective protease inhibitors at 10 nM concentration in the culture medium were used to inhibit the migration of tumour cells in the Matrigel assay. The MMP inhibitor Batimastat reduced the invasive potential of all cell lines studied independently of the MMP expression. The effect of cysteine protease inhibitors was strongly correlated with the protease profile of the tumour cell line. Our findings support the hypothesis of a very complex activation cascade of matrix-degrading proteolytic enzymes and they underline the need to analyse the protease profile of any tumour before beginning an antiproteolytic tumour treatment.
Authors:
V Kolkhorst; J Stürzebecher; B Wiederanders
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cancer research and clinical oncology     Volume:  124     ISSN:  0171-5216     ISO Abbreviation:  J. Cancer Res. Clin. Oncol.     Publication Date:  1998  
Date Detail:
Created Date:  1998-12-29     Completed Date:  1998-12-29     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  7902060     Medline TA:  J Cancer Res Clin Oncol     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  598-606     Citation Subset:  IM    
Affiliation:
Institut für Biochemie, Klinikum, Friedrich Schiller Universität, Jena, Germany.
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MeSH Terms
Descriptor/Qualifier:
Cathepsin B / metabolism
Cathepsin L
Cathepsins / metabolism
Cell Movement
Collagen
Collagenases / metabolism
Culture Media
Cysteine Endopeptidases
Drug Combinations
Endopeptidases*
Gelatinases / metabolism
Humans
Laminin
Matrix Metalloproteinase 2
Matrix Metalloproteinase 9
Metalloendopeptidases / metabolism
Neoplasm Invasiveness / prevention & control*
Protease Inhibitors / pharmacology*
Proteoglycans
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Culture Media; 0/Drug Combinations; 0/Laminin; 0/Protease Inhibitors; 0/Proteoglycans; 119978-18-6/matrigel; 9007-34-5/Collagen; EC 3.4.-/Cathepsins; EC 3.4.-/Endopeptidases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.1/Cathepsin B; EC 3.4.22.15/CTSL1 protein, human; EC 3.4.22.15/Cathepsin L; EC 3.4.24.-/Collagenases; EC 3.4.24.-/Gelatinases; EC 3.4.24.-/Metalloendopeptidases; 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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