INHIBITION OF PHAGOCYTOSIS OF COMPLEMENT-C3-COATED OR IMMUNOGLOBULIN-G-COATED PARTICLES AND OF C3BI BINDING BY MONOCLONAL-ANTIBODIES TO A MONOCYTE-GRANULOCYTE MEMBRANE GLYCOPROTEIN (MOL)
INHIBITION OF PHAGOCYTOSIS OF COMPLEMENT-C3-COATED OR IMMUNOGLOBULIN-G-COATED PARTICLES AND OF C3BI BINDING BY MONOCLONAL-ANTIBODIES TO A MONOCYTE-GRANULOCYTE MEMBRANE GLYCOPROTEIN (MOL)
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DOI：
10.1172/jci110955
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发表时间：
1983-01-01
影响因子：
15.9
通讯作者：
COLTEN, HR
中科院分区：
文献类型：
--
作者：
ARNAOUT, MA;TODD, RF;COLTEN, HR
补体 (C3) 或 IgG 包被颗粒与特定细胞表面受体相互作用后导致其被吞噬的事件尚不清楚。针对人粒细胞-单核细胞表面膜分化抗原 (Mo1) 的两种小鼠单克隆抗体（IgM 和 IgG2a）抑制粒细胞对用正常人血清或用 IgG 调理的油红 O 颗粒和用 IgG 致敏的绵羊红细胞的摄取。它们特异性地抑制被C3bi包被的吞噬细胞和绵羊红细胞之间的玫瑰花结，C3bi是补体成分C3的片段，通过用C3b灭活剂和βIH蛋白裂解C3b而产生。这些单克隆抗 Mo1 抗体不会抑制 IgG Fc、C3b 或 C3d 受体介导的涂有相应蛋白质的红细胞的结合。当用 C3bi 包被的酵母聚糖刺激粒细胞时，IgG2a 单克隆抗体的 Fab 片段抑制粒细胞释放非细胞毒性酶。将多形核白细胞去污剂裂解物电泳转移到硝酸纤维素上，然后用单克隆抗体进行免疫固定，结果表明这些抗体针对 155,000 MW 糖蛋白。这种表面膜结构似乎参与 Fc 和 C3 受体依赖性吞噬作用，并与 C3bi 受体密切相关。
Events that lead to phagocytosis of complement (C3)- or IgG-coated particles after their interaction with specific cell surface receptors are poorly understood. Two mouse monoclonal antibodies (an IgM and an IgG2a) to a human granulocyte-monocyte surface membrane differentiation antigen (Mo1) inhibited ingestion by granulocytes both of oil Red O particles opsonized with normal human serum or with IgG and of sheep erythrocytes sensitized with IgG. They specifically inhibited rosetting between phagocytes and sheep erythrocytes coated with C3bi, a fragment of the complement component C3, generated by cleaving C3b with C3b inactivator and .beta.IH protein. These monoclonal anti-Mo1 antibodies did not inhibit IgG Fc, C3b or C3d receptor-mediated binding of erythrocytes coated with the respective proteins. The Fab fragment of the IgG2a monoclonal antibody inhibited noncytotoxic enzyme release from granulocytes when these cells were stimulated with zymosan coated with C3bi. Electrophoretic transfer of polymorphonuclear leukocyte detergent lysates to nitrocellulose, followed by immunofixation with monoclonal antibody, showed that these antibodies were directed to a 155,000-MW glycoprotein. This surface membrane structure appears to be involved in Fc and C3 receptor-dependent phagocytosis and closely associated with the C3bi receptor.