Urokinase receptor is a multifunctional protein: influence of receptor occupancy on macrophage gene expression.

摘要: Binding of urokinase to the glycolipid-anchored receptor (uPAR) has been implicated in macrophage differentiation. However, no biochemical markers differentiation have yet directly linked uPAR occupancy. As extensive changes proteolytic profile characterize monocytic differentiation, we examined role occupancy on protease expression by differentiating phagocytes. Antibodies either or that prevent binding inhibited induction cathepsin B cultured monocytes and both 92-kD gelatinase mRNA protein phorbol diester-stimulated myeloid cells. Mannosamine, an inhibitor glycolipid anchor assembly, also blocked expression. Anti-catalytic antibodies, excess inactive urokinase, aprotinin had effect, indicating per se regulated integrins CD11a CD29 proteins CD14 CD55 effect. Protease was independent matrix attachment. affected neither decrease G nor increase tumor necrosis factor-alpha ester-stimulated These data establish is a multifunctional receptor, not only promoting pericellular proteolysis attachment, but effecting cysteine- metallo-protease during