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Institut Jožef Stefan, Ljubljana (IJS)
  • Cysteine protease cathepsin X modulates immune response via activation of ▫$\beta_2$▫ integrins
    Obermajer, Nataša ...
    Cathepsin X is a lysosomal, cysteine dependent carboxypeptidase. Its expression is restricted to cells of the immune system, suggesting a function related to the processes of inflammatory and immune ... responses. It has been shown to stimulate macrophage antigen-1 (Mac-1) receptor-dependent adhesion and phagocytosis via interaction with integrin Ž2 subunit. Here its potential role in regulating lymphocyte proliferation via Mac-1 and the other Ž2 integrin receptor, lymphocyte function-associated antigen-1 (LFA-1) has been investigated. Cathepsin X has been shown to suppress proliferation of human peripheral blood mononuclear cells, by activation of Mac-1, known as a suppressive factor for lymphocyte proliferation. On the other hand, co-localization of cathepsin X and LFA-1 supports the role of cathepsin X in regulating LFA-1 activity, which enhances lymphocyte proliferation. As shown by fluorescence resonance energy transfer, using U-937 and Jurkat cells transfected with ŽL-mCFP and Ž2-mYFP, recombinant cathepsin X directly activates LFA-1. The activation was confirmed by increased binding of monoclonal antibody 24, recognizing active LFA-1. We demonstrate that cathepsin X is involved in the regulation of two Ž2 integrin receptors, LFA-1 and Mac-1, which exhibit opposing roles in lymphocyte activation.
    Vir: Immunology. - ISSN 0019-2805 (Vol. 124, no. 1, 2008, str. 76-88)
    Vrsta gradiva - članek, sestavni del
    Leto - 2008
    Jezik - angleški
    COBISS.SI-ID - 2217841

vir: Immunology. - ISSN 0019-2805 (Vol. 124, no. 1, 2008, str. 76-88)

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