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巨噬细胞吞噬识别位点。通过异种和同种抗血清证明其选择性。

Macrophage phagocytic recognition sites. Demonstration of selectivity by hetero- and alloantisera.

作者信息

Schroit A J, Gallily R

出版信息

Immunology. 1977 Jul;33(1):121-7.

Abstract

Separate and independent phagocytic recognition sites have been identified on mouse peritoneal macrophages through the use of xenogeneic antimacrophage serum (AMS) and allogeneic anti H-2 antisera. Anti H-2d and anti H-2b antisera inhibit the binding and ingestion of opsonized erythrocytes (EA) by macrophages bearing H-2 haplotypes d and b, respectively. AMS and its F(ab')2 and Fab fragments inhibit the binding and ingestion of EA, and the ingestion but not the binding of 125I-labelled Shigella by macrophages. Neither antiserum inhibited the binding or ingestion of latex particles by macrophages. The results suggest that particulate binding to macrophages can be inhibited by two different mechanisms: a non-specific one where antibody bound to certain cell-surface antigens can mediate either directly or indirectly, and a specific interaction with Fc receptors. The possible mechanisms of non-specific antibody mediated phagocytic inhibition are discussed.

摘要

通过使用异种抗巨噬细胞血清(AMS)和同种异体抗H-2抗血清,在小鼠腹腔巨噬细胞上已鉴定出独立且不同的吞噬识别位点。抗H-2d和抗H-2b抗血清分别抑制携带H-2单倍型d和b的巨噬细胞对调理红细胞(EA)的结合和摄取。AMS及其F(ab')2和Fab片段抑制巨噬细胞对EA的结合和摄取,以及对125I标记的志贺氏菌的摄取,但不抑制其结合。两种抗血清均不抑制巨噬细胞对乳胶颗粒的结合或摄取。结果表明,颗粒与巨噬细胞的结合可通过两种不同机制被抑制:一种是非特异性机制,即与某些细胞表面抗原结合的抗体可直接或间接介导;另一种是与Fc受体的特异性相互作用。文中讨论了非特异性抗体介导的吞噬抑制的可能机制。

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