MFR，一种介导巨噬细胞融合的假定受体。
MFR, a putative receptor mediating the fusion of macrophages.
作者信息
Saginario C, Sterling H, Beckers C, Kobayashi R, Solimena M, Ullu E, Vignery A
机构信息
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut, USA.
出版信息
Mol Cell Biol. 1998 Nov;18(11):6213-23. doi: 10.1128/MCB.18.11.6213.
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, SIRPalpha, and MyD-1, all of which have been recently cloned and implicated in cell signaling and cell-cell interaction events.
我们之前鉴定出一种巨噬细胞表面蛋白，其表达受到高度诱导，具有瞬时性和特异性，因为它在体外和体内均局限于正在积极融合的巨噬细胞。这种蛋白可被阻断巨噬细胞融合的单克隆抗体识别。我们现已纯化该蛋白并克隆了其相应的cDNA。这种蛋白属于免疫球蛋白超家族，与免疫抗原受体如T细胞受体、B细胞受体以及病毒受体如CD4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可阻止巨噬细胞融合，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、SIRPα和MyD-1的同源物，所有这些蛋白最近都已被克隆，并与细胞信号传导和细胞间相互作用事件有关。
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