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* Inflammatory Diseases Research Unit, School of Medical Sciences, University of New South Wales, Sydney, Australia;
Centre for Vascular Research, School of Medical Sciences, University of New South Wales, Sydney, Australia; and
Department of Cardiology and ANZAC Research Institute Vascular Biology Group, Concord Hospital, University of Sydney, Sydney, Australia
C-reactive protein (CRP) and serum amyloid A (SAA) increase in the blood of patients with inflammatory conditions and CRP-induced monocyte tissue factor (TF) may contribute to inflammation-associated thrombosis. This study demonstrates that SAA is a potent and rapid inducer of human monocyte TF. SAA induced TF mRNA in PBMC within 30 min and optimal procoagulant activity within 4 h, whereas CRP (25 µg/ml)-induced activity was minimal at this time. Unlike CRP, SAA did not synergize with LPS. Procoagulant activity was inhibited by anti-TF and was dependent on factors VII and X, and TF Ag levels were elevated on CD14+ monocytes. Responses were optimal with lymphocytes, although these were not obligatory. Inhibitor studies indicate activation of NF-
B through the ERK1/2 and p38 MAPK pathways; the cyclo-oxygenase pathway was not involved. SAA-induced TF was partially inhibited by high-density lipoprotein, but not by low-density lipoprotein or by apolipoprotein A-I. SAA is a ligand for the receptor for advanced glycation end products (RAGE), and TF generation was suppressed by 
50% by a RAGE competitor, soluble RAGE, and by 85% by anti-RAGE IgG. However, another RAGE ligand, high mobility group box-1 protein, capable of inducing monocyte chemotactic protein-1 mRNA in 2 h, did not induce TF within 24 h. Cross-linking studies confirmed SAA binding to soluble RAGE. Elevated SAA is a marker of disease activity in patients with rheumatoid arthritis, and PBMC from patients with rheumatoid arthritis were more sensitive to SAA than normals, suggesting a new link between inflammation and thrombosis.
The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 This study was supported by the National Health and Medical Research Council of Australia and the Arthritis Foundation of Australia. C.S. held a University Postgraduate Award of the University New South Wales.
2 H.C. and C.S. contributed equally to this study.
3 Address correspondence and reprint requests to Dr. Carolyn L. Geczy, Inflammatory Diseases Research Unit, School of Medical Sciences, University of New South Wales, Sydney 2052, Australia. E-mail address: c.geczy{at}unsw.edu.au
4 Abbreviations used in this paper: SAA, serum amyloid A; ApoA-I, apolipoprotein A-I; CRP, C-reactive protein; DSS, disuccinimidyl suberate; HDL, high-density lipoprotein; HMGB1, high mobility group box-1 protein; HSAB, N-hydroxysuccinimidyl 4-azidobenzoate; LAL, Limulus amebocyte lysate; LDL, low-density lipoprotein; MCF, mean channel fluorescence; PCA, procoagulant activity; RA, rheumatoid arthritis; RAGE, receptor for advanced glycation end products; SI, stimulation index; sRAGE, soluble RAGE; TF, tissue factor.
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