The role of fibrin fibrils in the dissociation of a cell surface protease-inhibitor complex and evidence for the recapture of the inhibitor protein.
J Enzyme Inhib
; 5(4): 299-315, 1992.
Article
in En
| MEDLINE
| ID: mdl-1285251
ABSTRACT
Colonic epithelial cells possess a cell surface protease referred to as guanidinobenzoatase (GB). Active GB can be located by the fluorescent active site directed competitive inhibitor 9-amino acridine (9AA) followed by fluorescence microscopy. The cell surface GB can be transferred to fibrin fibrils, which have a higher affinity for GB than the cell surface. The cytoplasm of colonic epithelial cells contains a protein which inhibits membrane bound GB, forming a latent form of GB or GB-inhibitor complex. This complex can also be dislodged from the epithelial cell surface due to the high affinity of fibrin for GB, with the consequent dissociation of the enzyme-inhibitor complex and solubilisation of the inhibitor. This use of fibrin has led to the demonstration of the transfer of a selective inhibitor protein from one cell surface (the donor) to a second cell surface (the target).
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endopeptidases
/
Protease Inhibitors
/
Fibrin
/
Carboxylic Ester Hydrolases
/
Colon
Limits:
Humans
Language:
En
Journal:
J Enzyme Inhib
Journal subject:
BIOQUIMICA
Year:
1992
Document type:
Article
Affiliation country:
United kingdom