Document Detail


Inhibition properties of Sepharose-bound trypsin and a protease on the surface of Ehrlich ascites tumour cells.
MedLine Citation:
PMID:  6269636     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ehrlich ascites cells have been shown to possess a protease with beta-naphthylamidase activity located on the surface of these cells. This enzyme is protected from the inhibitory action of protein inhibitors of trypsin (EC 3.4.21.4) in free solution, but is inhibited by high concentrations of active site-directed inhibitors of trypsin. We believe the protection against inhibition is provided by the location of this protease on the cell surface. We employed a model system of trypsin coupled to Sepharose to demonstrate the protective action of an inert surface, resulting in a marked reduction in inhibition of trypsin-Sepharose, compared to trypsin in free solution, when exposed to both high and low molecular weight inhibitors. This cell protease has been shown to play a role in activation of the zymogen of collagenase exported by tumour cells. This role may have important implications for tumour cell invasion of the intercellular matrix.
Authors:
F S Steven; M M Griffin; G S Itzhaki; A Al-Habib
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  660     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1981 Aug 
Date Detail:
Created Date:  1981-12-15     Completed Date:  1981-12-15     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  333-40     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Aminopeptidases / metabolism
Animals
Binding Sites / drug effects
Carcinoma, Ehrlich Tumor / enzymology*
Cell Membrane / enzymology
Enzymes, Immobilized / antagonists & inhibitors
Mice
Microbial Collagenase / metabolism
Peptide Hydrolases / metabolism*
Polysaccharides*
Sepharose*
Trypsin / metabolism*
Trypsin Inhibitors / pharmacology*
Chemical
Reg. No./Substance:
0/Enzymes, Immobilized; 0/Polysaccharides; 0/Trypsin Inhibitors; 9012-36-6/Sepharose; EC 3.4.-/Peptide Hydrolases; EC 3.4.11.-/Aminopeptidases; EC 3.4.21.4/Trypsin; EC 3.4.24.3/Microbial Collagenase

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


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