Yin Wei, Ghebrehiwet Berhane, Peerschke Ellinor I B
Department of Pathology and Laboratory Medicine, Weill Medical College of Cornell University, New York, NY, USA.
Platelets. 2008 May;19(3):225-33. doi: 10.1080/09537100701777311.
Platelet microparticles (PMP) are released from activated platelets and play an important role in hemostasis, thrombosis and inflammation. Since platelets were recently found to demonstrate an intrinsic capacity for activating both classical and alternative pathways of the complement system, the present study extended these observations to PMP. PMP were generated by treating platelets with 10 microM A23187 (37 degrees C, 5 min). PMP were identified by flow cytometry, based on size, Annexin V binding, and expression of P-selectin and GPIIb (CD41). PMP expressed gC1qR/p33, a multifunctional cellular protein that was recently described to activate the classical complement cascade. PMP also expressed the classical pathway and contact system regulator, C1 inhibitor (C1-INH), as well as CD55 and CD59. Despite C1-INH expression, PMP supported classical pathway C4 activation in the presence of purified C1 and C4. Moreover, statistically significant deposition of C3b and C5b-9 was detected on PMP exposed to plasma, concurrently with expression of CD55 and CD59. These data provide the first evidence for the ability of PMP to support in situ complement activation. Complement activation contributes to a variety of vascular and inflammatory disease states including atherosclerosis and ischemia/reperfusion injury.
血小板微粒(PMP)由活化的血小板释放,在止血、血栓形成和炎症中起重要作用。由于最近发现血小板具有激活补体系统经典途径和替代途径的内在能力,本研究将这些观察结果扩展至PMP。通过用10微摩尔A23187(37℃,5分钟)处理血小板来生成PMP。基于大小、膜联蛋白V结合以及P-选择素和糖蛋白IIb(CD41)的表达,通过流式细胞术鉴定PMP。PMP表达gC1qR/p33,这是一种多功能细胞蛋白,最近被描述为可激活经典补体级联反应。PMP还表达经典途径和接触系统调节剂C1抑制剂(C1-INH)以及CD55和CD59。尽管表达了C1-INH,但在存在纯化的C1和C4的情况下,PMP仍支持经典途径C4的激活。此外,在暴露于血浆的PMP上检测到C3b和C5b-9有统计学意义的沉积,同时伴有CD55和CD59的表达。这些数据为PMP支持原位补体激活的能力提供了首个证据。补体激活导致包括动脉粥样硬化和缺血/再灌注损伤在内的多种血管和炎症性疾病状态。