作者
Osama A Hamad, Per H Nilsson, Diana Wouters, John D Lambris, Kristina N Ekdahl, Bo Nilsson
发表日期
2010/3/1
期刊
The Journal of Immunology
卷号
184
期号
5
页码范围
2686-2692
出版商
American Association of Immunologists
简介
It has been reported that complement is activated on the surface of activated platelets, despite the presence of multiple regulators of complement activation. To reinvestigate the mechanisms by which activated platelets bind to complement components, the presence of complement proteins on the surfaces of nonactivated and thrombin receptor-activating peptide-activated platelets was analyzed by flow cytometry and Western blot analyses. C1q, C4, C3, and C9 were found to bind to thrombin receptor-activating peptide-activated platelets in lepirudin-anticoagulated platelet-rich plasma (PRP) and whole blood. However, inhibiting complement activation at the C1q or C3 level did not block the binding of C3 to activated platelets. Diluting PRP and chelating divalent cations also had no effect, further indicating that the deposition of complement components was independent of complement activation. Furthermore …
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OA Hamad, PH Nilsson, D Wouters, JD Lambris… - The Journal of Immunology, 2010