Cysteine protease cathepsin X modulates immune response via activation of beta2 integrins

Immunology
Nataša ObermajerJanko Kos

Abstract

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 beta2 subunit. Here its potential role in regulating lymphocyte proliferation via Mac-1 and the other beta2 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 alpha(L)-mCFP and beta2-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 beta2 i...Continue Reading

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Citations

Feb 17, 2011·ACS Chemical Biology·Margot G Paulick, Matthew Bogyo
Aug 6, 2011·Arteriosclerosis, Thrombosis, and Vascular Biology·Jiusong SunGuo-Ping Shi
Dec 18, 2013·Hypertension·Lina HuMasafumi Kuzuya
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Aug 12, 2009·Cell Motility and the Cytoskeleton·Zala JevnikarJanko Kos
Dec 19, 2008·The Journal of Pathology·Sabine KruegerAlbert Roessner
Jul 29, 2011·IUBMB Life·Zala JevnikarJanko Kos
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Apr 28, 2021·Journal of Medicinal Chemistry·Hong-Rae KimEuna Yoo

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