Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 M(r) component of the C1q receptor.
Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 M(r) component of the C1q receptor.
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甘露糖结合蛋白 (MBP) 通过含有 C1q 受体 126,000 M(r) 成分的受体增强单核吞噬细胞功能。
DOI：
10.1016/1074-7613(95)90177-9
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发表时间：
1995
期刊：
影响因子：
32.4
通讯作者：
Ezekowitz,RA
中科院分区：
文献类型：
--
作者：
Tenner,AJ;Robinson,SL;Ezekowitz,RA
甘露糖结合蛋白（MBP）、Clq（经典补体途径的识别组分）和肺表面活性蛋白A（SP-A）是一类分子的成员，所述分子含有与非胶原样序列邻接的胶原样序列，并且通常具有凝集素的性质。Clq和SP-A已被证明能增强单核细胞FcR和CRl介导的吞噬作用，这表明胶原样结构域的共同结构特征可能为这种免疫学重要功能提供了基础。本文呈现的结果表明，MBP还增强了单核细胞和巨噬细胞的FcR介导的吞噬作用，并刺激了人培养衍生的巨噬细胞和佛波酯活化的单核细胞中的CRl介导的吞噬作用。此外，识别126，000 M细胞表面蛋白并抑制Clq增强的吞噬作用的单克隆抗体抑制MBP介导的吞噬作用增强。因此，介导MBP和Clq增强吞噬作用的受体共享至少一个关键功能组分，126，000 M，ClqRp。
Mannose-binding protein (MBP), Clq, the recognition component of the classical complement pathway, and pulmonary surfactant protein A (SP-A) are members of a faniily of molecules containing a collagen-like sequence contiguous with a noncollagen-like sequence, and usually having the properties of a lectin. Clq and SP-A have been shown to enhance monocyte FcR-and CRl-mediated phagocytosis, suggesting that thecommon structural features of the collagen-like domains may provide a basisforthis immunologically important function. Results presented here demonstrate that MBP also enhanced FcR-mediated phagocytosis by both monocytes and macrophages, and stimulated CRl-mediated phagocytosis in human culture-derived macrophages and in phorbol ester-activated monocytes. Furthermore, a monoclonal antibody that recognizes a 126,000 M, cell surface protein and inhibits Clq-enhanced phagocytosis, inhibited the MBP-mediated enhancement of phagocytosis. Thus, the receptors that mediate the enhancement of phagocytosis by MBP and Clq share at least one critical functional component, the 126,000 M, ClqRp.