Selectivity of the plasminogen activator inhibitor (PAI-1) for the iso enzyme of guanidinobenzoatase on the surface of colonic carcinoma cells.

Abstract

The interaction of plasminogen activator-inhibitor (PAI-1) with a cell surface protease, guanidinobenzoatase (GB), has been studied in free solution and on the surface of colonic epithelial cells. It has been demonstrated that PAI-1 recognises and inhibits the iso enzymic form of GB associated with colonic carcinoma cells but fails to bind to the iso enzymic form of GB associated with normal donor colonic epithelial cells. This interaction is mediated by a lysyl binding site on the GB: complex formation prevents GB binding to fibrin fibrils which also involves lysyl binding sites.

• Authors: F S Steven, M Anees, N A Booth
• Journal: Anticancer research (Anticancer Res) 1995 Jan-Feb Vol. 15 Issue 1 Pg. 205-10 ISSN: 0250-7005 [Print] Greece
• PMID: 7733635 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Dansyl Compounds
• Isoenzymes
• Plasminogen Activator Inhibitor 1
• Protease Inhibitors
• dansyl fluoride
• Carboxylic Ester Hydrolases
• guanidinobenzoate esterase
• Endopeptidases
• Tissue Plasminogen Activator

Topics

• Carboxylic Ester Hydrolases (antagonists & inhibitors, isolation & purification, metabolism)
• Cell Membrane (enzymology)
• Colon (enzymology)
• Colonic Neoplasms (enzymology)
• Dansyl Compounds (pharmacology)
• Electrophoresis, Polyacrylamide Gel
• Endopeptidases (chemistry, isolation & purification, metabolism)
• Epithelium (enzymology)
• Histocytochemistry
• Humans
• Isoenzymes (antagonists & inhibitors, isolation & purification, metabolism)
• Kinetics
• Plasminogen Activator Inhibitor 1 (pharmacology)
• Protease Inhibitors (pharmacology)
• Reference Values
• Tissue Plasminogen Activator (isolation & purification, metabolism)