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  • Carboxypeptidase cathepsin X mediates ß2 - integrin dependent adhesion of differentiated U-937 cells
    Obermajer, Nataša ...
    Cathepsin X is a lysosomal carboxypeptidase with a potential role in processesof inflammation and immune response. The integrin-binding motifs RGD and ECD, present respectively in the pro- and in ... mature forms of cathepsin X, suggest that this enzyme might have a function in cell signaling and adhesion.In this study we report that cysteine protease inhibitors E-64 and CA-074 and 2F12 monoclonal antibody, all of which inhibit cathepsin X activity, significantly reduced adhesion of differentiated U-937 cells to polystyrene and fibrinogen coated surfaces via Mac-1 integrin receptor, whereas their binding to vitronectin, fibronectin or Matrigel was not affected. On the other hand, cathepsin X, added to differentiating U-937 cells, stimulated their adhesion. Using confocal microscopy we demonstrated that the pro-form of cathepsin X was co-localized with 2 and 3 integrin subunits and its mature form solely with the 2 integrin subunit with the mostintense signal in cell-cell junctions in differentiated U-937 cells and incocultures with endothelial cells. Our results indicate that active cathepsin X mediates the function of 2 integrin receptors during cell adhesion and that it could also be involved in other processes associated with 2 integrin receptors such as phagocytosis and T cell activation.
    Source: Experimental cell research. - ISSN 0014-4827 (Vol. 312, 2006, str. 2515-2527)
    Type of material - article, component part
    Publish date - 2006
    Language - english
    COBISS.SI-ID - 1920113

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