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The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

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Par-2 in the pathogenesis of collagen-induced arthritis: crucial role in T cell differentiation

Nickdel, M.B. and Palmer, H.S. and Ferrell, W.R. and Lockhart, J.C. and Plevin, R.J. and McInnes, I.B. (2008) Par-2 in the pathogenesis of collagen-induced arthritis: crucial role in T cell differentiation. Rheumatology, 47 (Supple). II54-II54. ISSN 1462-0324

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Abstract

Protease-activated receptor-2 (PAR-2) is a member of a novel family of seven-transmembrane G-protein-coupled receptors (PARs) activated by proteolytic cleavage to reveal a tethered ligand. Serine proteases such as mast cell tryptase cleave PAR-2 at a specific site within the extracellular N-terminus to expose a new N-terminal tethered ligand domain, which binds to and thereby activates the cleaved receptor. We previously demonstrated that adjuvant monoarthritis is substantially inhibited in PAR-2 'knockout' mice (1). The present study extended these earlier finding by investigating the therapeutic potential of a novel PAR-2 antagonist, ENMD-1068, in the murine model of collagen-induced arthritis (CIA); we recently demonstrated this antagonist inhibited TNF generation from the synovial membrane of RA patients (2). We further tested the hypothesis that this receptor contributes to the pathogenesis of arthritis by affecting T lymphocyte activation and/or differentiation to Th1, Th2 and Th17 phenotypes.