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Urokinase in rheumatoid arthritis: causal or coincidental?
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The past 10 years have witnessed an increased
interest in the plasminogen activation system and its potential role(s)
in rheumatoid arthritis (RA). Two types of plasminogen activators
(PAs), urokinase (uPA) and tissue type PA (tPA), which are
structurally, immunologically, and genetically distinct, have been
identified in mammals. Both PAs are secreted as a single chain protein,
which in the case of uPA is essentially inactive (pro-uPA). Pro-uPA is
then converted by a single enzymatic cleavage into two chain active
enzyme. uPA and tPA are highly specific serine proteases catalysing the
conversion of plasminogen into plasmin.1 2 Plasminogen,
present in plasma and extracellular fluids, can bind to fibrin and also
to cell surface plasminogen receptors (PlnR), via its lysine binding
sites. The activity of PAs is controlled by natural inhibitors (PAls), which include PAI-1, the main PAI in the circulation, and PAI-2. In
addition, uPA activity is blocked by protease nexin 1 (PN-1). Another
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This article has been cited by other articles:
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Slot, O., Brünner, N., Locht, H., Oxholm, P., Stephens, R. W
(1999). Soluble urokinase plasminogen activator receptor in plasma of patients with inflammatory rheumatic disorders: increased concentrations in rheumatoid arthritis. Ann Rheum Dis
58: 488-492
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Immunology (including allergy)
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Connective tissue disease
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Degenerative joint disease
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Musculoskeletal syndromes
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Rheumatoid arthritis
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