MANNOSE-BINDING PROTEIN (MBP) ENHANCES MONONUCLEAR PHAGOCYTE FUNCTION VIA A RECEPTOR THAT CONTAINS THE 126,000 M(R) COMPONENT OF THE C1Q RECEPTOR

被引:136
作者
TENNER, AJ
ROBINSON, SL
EZEKOWITZ, RAB
机构
[1] AMER RED CROSS,JEROME H HOLLAND LAB,ROCKVILLE,MD 20855
[2] HARVARD UNIV,CHILDRENS HOSP,SCH MED,DANA FARBER CANC INST,DEPT PEDIAT,DIV HEMATOL ONCOL,BOSTON,MA 02115
关键词
D O I
10.1016/1074-7613(95)90177-9
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Mannose-binding protein (MBP), Clq, the recognition component of the classical complement pathway, and pulmonary surfactant protein A (SP-A) are members of a family 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 CR1-mediated phagocytosis, suggesting that the common structural features of the collagen-like domains may provide a basis for this immunologically important function. Results presented here demonstrate that MBP also enhanced FcR-mediated phagocytosis by both monocytes and macrophages, and stimulated CR1-mediated phagocytosis in human culture-derived macrophages and in phorbol ester-activated monocytes. Furthermore, a monoclonal antibody that recognizes a 126,000 M(r) 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(r) ClqRp.
引用
收藏
页码:485 / 493
页数:9
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