超大血管性血友病因子诱导的血小板聚集以及血栓性血小板减少性紫癜和溶血尿毒综合征中替代补体途径的激活。
Ultralarge von Willebrand factor-induced platelet clumping and activation of the alternative complement pathway in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndromes.
作者信息
Turner Nancy, Sartain Sarah, Moake Joel
机构信息
Department of Bioengineering, Rice University, 6500 Main Street, Houston, TX 77030, USA.
Department of Bioengineering, Rice University, 6500 Main Street, Houston, TX 77030, USA; Section of Hematology-Oncology, Department of Pediatrics, Texas Children's Cancer and Hematology Centers, Baylor College of Medicine, 6701 Fannin St., Houston, TX 77004, USA.
出版信息
Hematol Oncol Clin North Am. 2015 Jun;29(3):509-24. doi: 10.1016/j.hoc.2015.01.008. Epub 2015 Mar 12.
The molecular linkage between ultralarge (UL) von Willebrand factor (VWF) multimers and the alternative complement pathway (AP) has recently been described. Endothelial cell (EC)-secreted and anchored ULVWF multimers (in long stringlike structures) function as both hyperadhesive sites that initiate platelet adhesion and aggregation and activating surfaces for the AP. In vitro, the active form of C3, C3b binds to the EC-anchored ULVWF multimeric strings and initiates the assembly on the strings of C3 convertase (C3bBb) and C5 convertase (C3bBbC3b). In vivo, activation of the AP via this mechanism proceeds all the way to generation of terminal complement complexes (C5b-9).
超大（UL）血管性血友病因子（VWF）多聚体与替代补体途径（AP）之间的分子联系最近已被描述。内皮细胞（EC）分泌并锚定的ULVWF多聚体（呈长串状结构）既作为启动血小板黏附和聚集的高黏附位点，又作为AP的激活表面。在体外，补体C3的活性形式C3b与EC锚定的ULVWF多聚体链结合，并启动C3转化酶（C3bBb）和C5转化酶（C3bBbC3b）在链上的组装。在体内，通过这种机制激活AP一直持续到终末补体复合物（C5b-9）的产生。
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