MFR, a putative receptor mediating the fusion of macrophages
MFR, a putative receptor mediating the fusion of macrophages
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DOI：
10.1128/mcb.18.11.6213
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发表时间：
1998-11-01
影响因子：
5.3
通讯作者：
Vignery, A
中科院分区：
文献类型：
--
作者：
Saginario, C;Sterling, H;Vignery, A
我们之前已经鉴定出一种巨噬细胞表面蛋白，其表达是高度诱导的、瞬时的和特异性的，因为它仅限于在体外和体内主动融合巨噬细胞。这种蛋白质被阻断巨噬细胞融合的单克隆抗体识别。现在我们已经纯化了该蛋白并克隆了其相应的 cDNA。该蛋白属于免疫球蛋白超家族，与 T 细胞受体、B 细胞受体等免疫抗原受体和 CD4 等病毒受体相似。因此我们将这种蛋白命名为巨噬细胞融合受体（MFR）。我们发现MFR的胞外结构域在体外阻止巨噬细胞的融合，因此提出MFR属于巨噬细胞的融合机制，MFR与SHPS-1和BIT相同，并且是P84、SIRP α和MyD-1的同源物，所有这些最近都已被克隆并与细胞信号传导和细胞-细胞相互作用事件有关。
We had previously identified a macrophage surface protein whose expression is highly induced, transient, and specific, as it is restricted to actively fusing macrophages in vitro and in vivo. This protein is recognized by monoclonal antibodies that block macrophage fusion. We have now purified this protein and cloned its corresponding cDNA. This protein belongs to the superfamily of immunoglobulins and is similar to immune antigen receptors such as the T-cell receptor, B-cell receptor, and viral receptors such as CD4. We have therefore named this protein macrophage fusion receptor (MFR). We show that the extracellular domain of MFR prevents fusion of macrophages in vitro and therefore propose that MFR belongs to the fusion machinery of macrophages, MFR is identical to SHPS-1 and BIT and is a homologue of P84, SIRP alpha, and MyD-1, all of which have been recently cloned and implicated in cell signaling and cell-cell interaction events.