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Báo cáo y học: "Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài:Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis. | Available online http arthritis-research.eom content 7 2 R268 Research article Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis Xiaotian Chang1 Ryo Yamada1 and Kazuhiko Yamamoto1 2 Laboratory for Rheumatic Diseases SNP Research Center The Institute of Physical and Chemical Research RIKEN Kanagawa Japan 2Department of Allergy and Rheumatology Graduate School of Medicine University of Tokyo Tokyo Japan Corresponding author Xiaotian Chang xchang@src.riken.go.jp Received 10 Jul 2004 Revisions requested 27 Sep 2004 Revisions received 26 Nov 2004 Accepted 1 Dec 2004 Published 11 Jan 2005 Arthritis Res Ther 2005 7 R268-R273 DOI 10.1186 ar1487 2005 Chang et al. licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is cited. Open Access Abstract Thrombin is a key factor in the stimulation of fibrin deposition angiogenesis proinflammatory processes and proliferation of fibroblast-like cells. Abnormalities in these processes are primary features of rheumatoid arthritis RA in synovial tissues. Tissue destruction in joints causes the accumulation of large quantities of free hyaluronic acid HA in RA synovial fluid. The present study was conducted to investigate the effects of HA and several other glycosaminoglycans on antithrombin a plasma inhibitor of thrombin. Various glycosaminoglycans including HA chondroitin sulfate keratan sulfate heparin and heparan were incubated with human antithrombin III in vitro. The residual activity of antithrombin was determined using a thrombin-specific chromogenic assay. HA concentrations ranging from 250 to 1000 pg ml significantly blocked the ability of antithrombin to inhibit thrombin in the presence of Ca2 or Fe3 and chondroitin A B and C also reduced this ability .