PMID: 7539069Jan 1, 1994Paper

Retinoic acid inhibition of a tumour protease immobilised on cell surfaces and in free solution

Journal of Enzyme Inhibition
M Anees, F S Steven

Abstract

Retinoids are inhibitors of tumour cell proliferation in culture and have been shown to suppress carcinogenesis and decrease the levels of proteases. The present study has demonstrated that retinoic acid is a potential non-competitive inhibitor of a protease (GB) immobilised on the surfaces of tumour cells in thin sections and free GB in solution. The enzymic status of GB on the cell surfaces in sections has been determined by challenging the retinoic acid-treated cells with a second fluorescent inhibitor (9-AA), followed by fluorescence microscopic analysis. The inhibition of cell surface GB by retinoic acid was demonstrated to be reversible. The activity of soluble GB has been measured by the MUGB assay in the presence and absence of retinoic acid. It is suggested that retinoic acid acts on GB by interacting with a binding site, different from the active site, and causes major conformational changes, resulting in enzyme inhibition. It is possible that the modulation of GB activity by retinoic acid may play a role in the control of cell migration and metastasis.

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