Annexin V binds to viable B cells and colocalizes with a marker of lipid rafts upon B cell receptor activation
Annexin V binds to viable B cells and colocalizes with a marker of lipid rafts upon B cell receptor activation
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DOI：
10.4049/jimmunol.164.3.1322
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发表时间：
2000-02-01
影响因子：
4.4
通讯作者：
Schlissel, MS
中科院分区：
文献类型：
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作者：
Dillon, SR;Mancini, M;Schlissel, MS
重组膜联蛋白V（rAnV）已被用于基于其结合磷脂酰丝氨酸（PS）的能力来鉴定凋亡细胞，PS是一种通常限于质膜的细胞质面的脂质，但在凋亡早期被外化。然而，rAnV结合和凋亡的这种关联不是强制性的，我们证明，rAnV结合大部分的小鼠B细胞携带选择性Ag受体，尽管这些细胞是不凋亡的，磷脂酰丝氨酸，其均匀分布在静息B细胞上，被动员与抗IgM处理的B细胞上的IgM共加帽，并与脂筏标记物GM 1共定位。在抗IgM处理之前交联PS隔离该脂质并改变通过IgM的信号传导。因此，暴露于体内大多数B细胞上的PS不反映早期凋亡，而是在受体介导的信号传导事件中起作用。
Recombinant annexin V (rAnV) has been used to identify apoptotic cells based on its ability to bind phosphatidylserine (PS), a lipid normally restricted to the cytoplasmic face of the plasma membrane, but externalized early during apoptosis, However, this association of rAnV binding and apoptosis is not an obligatory one, We demonstrate that rAnV binds to a large fraction of murine B cells bearing selectable Ag receptors despite the fact that these cells are not apoptotic, Phosphatidylserine, which is uniformly distributed on resting B cells, is mobilized to co-cap with IgM on anti-IgM-treated B cells and to colocalize with GM1, a marker of lipid rafts. Cross-linking PS before anti-IgM treatment sequesters this lipid and alters signaling through IgM, Thus, PS exposed on the majority of B cells in vivo does not reflect early apoptosis, but, instead, plays a role in receptor-mediated signaling events.