Annexin A5

膜联蛋白 A5
  • 文章类型: Journal Article
    背景:促凝血血小板是高度活化的血小板亚群,可通过表面暴露促进凝血,带负电荷的磷脂,特别是磷脂酰丝氨酸(PS)。促凝血血小板对于止血期间的血块稳定是重要的,并且这些血小板的数量增加与血栓形成风险相关。在该领域需要协调,因为用于评估促凝血血小板的许多标记和方法在单独使用时不是特异性的,但也与血小板凋亡相关。
    目的:我们启动了该项目,以确定可以检测和区分促凝血血小板与凋亡血小板的一组最少的标志物和/或方法。
    结果:研究设计涉及一个主要小组,有二十七位国际专家参加在线调查,并主持虚拟焦点小组会议。然后邀请主要和次要小组成员就焦点小组产生的主题和声明提供意见。这导致建议使用流式细胞术和以下三种表面标志物的组合来区分促凝血剂和凋亡血小板:P-选择素(CD62P),PS(附件五认可),和血小板特异性受体GPIX(CD42a)或αIIb整合素(CD41,GPIIb)。
    结论:促凝血血小板对所有三种标志物均为阳性,而凋亡的血小板对膜联蛋白V和血小板特异性表面受体呈阳性,但对P-选择素呈阴性。
    Procoagulant platelets are a subpopulation of highly activated platelets that promote coagulation through surface-exposed, negatively charged phospholipids, especially phosphatidylserine. Procoagulant platelets are important for clot stabilization during hemostasis, and an increased number of these platelets is associated with thrombotic risk. There is a need for harmonization in this area since many of the markers and methods used to assess procoagulant platelets are not specific when used in isolation but are also associated with platelet apoptosis.
    We initiated this project to identify a minimum set of markers and/or methods that can detect and distinguish procoagulant platelets from apoptotic platelets.
    The study design involved a primary panel with 27 international experts who participated in an online survey and moderated virtual focus group meetings. Primary and secondary panel members were then invited to provide input on themes and statements generated from the focus groups.
    This led to a recommendation to use flow cytometry and a combination of the following 3 surface markers to differentiate procoagulant platelets from apoptotic platelets: P-selectin (CD62P), phosphatidylserine (recognized by annexin V), and the platelet-specific receptor GPIX (CD42a) or αIIb integrin (CD41, GPIIb).
    Procoagulant platelets are expected to be positive for all 3 markers, while apoptotic platelets are positive for annexin V and the platelet-specific surface receptor(s) but negative for P-selectin.
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  • 文章类型: Comparative Study
    A group of calcium-binding proteins which bind to biomembranes has recently been identified in widely different cells and tissues (refs 1-7, reviewed in ref. 8). Three of these proteins (p70, p36 and p32.5) cross-react with antiserum to calelectrin, a Ca2+-binding protein (relative molecular mass 34,000 (34K] from the ray Torpedo marmorata, giving rise to their designation as calelectrin-related proteins. We now report that calelectrin, p36 and p32.5 contain a 17-amino-acid consensus sequence which is conserved and present in multiple copies. We suggest that this sequence may be common to other members of this new group of Ca2+-binding proteins and may underlie their unusual mode of combination with biomembranes.
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