Inhibition of a Protease Associated with Tumour Cells and the Probable Mechanism of Regulation of this Interactionin Vivo
- 1 January 1989
- journal article
- research article
- Published by Taylor & Francis in Journal of Enzyme Inhibition
- Vol. 3 (2) , 145-157
- https://doi.org/10.3109/14756368909030373
Abstract
The regulation of activity of a protease on the surface of human colonic tumour cells implanted in nude mice has been studied. A synthetic fluorescent probe was used to locate cells possessing active guanidi-nobenzoatase in frozen sections of tumour bearing tissues. These studies demonstrated the presence of intracellular protein inhibitors of guanidinobenzoatase which could be extracted in isotonic saline and transferred to the outer surface of the tumour cells. This study showed that the inhibition of guanidinobenzoatase was pH dependent and that the tumour cell may regulate the activity of its surface guanidinobenzoatase by exporting lactic acid.Keywords
This publication has 8 references indexed in Scilit:
- Inhibition of Guanidinobenzoatase by A Substrate for Trypsin-Like EnzymesJournal of Enzyme Inhibition, 1988
- Inhibition of Guanidinobenzoatase: Evidence for Multiple Forms of This Protease on Different Tumour CellsJournal of Enzyme Inhibition, 1988
- Evidence for Inhibitors of the Cell Surface Protease GuanidinobenzoataseJournal of Enzyme Inhibition, 1986
- The design of fluorescent probes which bind to the active centre of guanidinobenzoatase. Application to the location of cells possessing this enzymeEuropean Journal of Biochemistry, 1985
- Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the moleculeNature, 1984
- Rhodamine-based compounds as fluorogenic substrates for serine proteinasesBiochemical Journal, 1983
- Evidence for an Enzyme which Cleaves the Guanidinobenzoate Moiety from Active‐Site Titrants Specifically Designed to Inhibit and Quantify TrypsinEuropean Journal of Biochemistry, 1983