Cathepsin X cleaves the ß2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and [alpha]-actinin-1 binding
Jevnikar, Zala (Author), Obermajer, Nataša (Author), Pečar Fonović, Urša (Author), Karaoglanovic-Carmona, Adriana (Author), Kos, Janko (Author)

URLURL - Presentation file, Visit http://www3.interscience.wiley.com/journal/122522175/issue This link opens in a new window

The motility of T cells depends on the dynamic spatial regulation of integrin-mediated adhesion and de-adhesion. Cathepsin X, a cysteine protease, has been shown to regulate T cell migration by interaction with lymphocyte function associated antigen-1 (LFA-1). LFA-1 adhesion to the intercellular adhesion molecule-1 (ICAM-1) is controlled by the association of actin-bindingproteins with the cytoplasmic tail of the 2 chain of LFA-1. Cleavage by cathepsin X of the amino acid residues S769, E768 and A767 from the C-terminal of the 2 cytoplasmic tail of LFA-1 is shown to promote binding of the actin-binding protein -actinin-1. Furthermore, cathepsin X overexpression reduced LFA-1 clustering and induced an intermediate affinity LFA-1 conformation that is known to associate with -actinin-1. Increased levels of intermediate affinity LFA-1 resulted in augmented cell spreading dueto reduced attachment of T cells to the ICAM-1 coated surface. Gradual cleavage of LFA-1 by cathepsin X enables the transition between intermediate and high affinity LFA-1, an event that is crucial for effective T cell migration.

Keywords:katepsin X, T celice, cisteinske proteaze, LFA-1
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Number of pages:str. 3217-3227
Numbering:Vol. 39, Issue 11
ISSN on article:0014-2980
DOI:10.1002/eji.200939562 Link is opened in a new window
COBISS.SI-ID:2654321 Link is opened in a new window
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Record is a part of a journal

Title:European Journal of Immunology
Shortened title:Eur J Immunol
Publisher:Verlag Chemie GmbH, Academic Press
COBISS.SI-ID:25429248 This link opens in a new window

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