期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：3
页码：1400-1404
DOI：10.1073/pnas.76.3.1400
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Variants of the J774 mouse macrophage cell line that lack immunologically important membrane receptors were isolated. After mutagenesis, variants were selected in a metrizamide gradient that separated cells heavily rosetted with sheep erythrocytes (E) coated with rabbit anti-E IgG (EIgG) from poorly rosetted cells. Stable variants that exhibited altered binding were found with a frequency of <10-7, and five clones were studied in detail. The variants failed to bind E opsonized with a monoclonal mouse IgG2b anti-E antibody but bound monomeric IgG2a normally when compared to the parental J774 line (Ka 4{degrees}C={approx}1x108 M-1; {approx}2x105 sites per cell). This demonstrates the independence of the receptor for mouse IgG2b complexes (FcRII) from the trypsin-sensitive receptor for mouse IgG2a monomer (FcRI). The variants bound an average of 10-15 EIgG per cell, compared to >20 per cell for J774. After trypsinization, three variants bound only three to five EIgG per cell; the J774 line was not affected by this treatment. Monomeric IgG2a could inhibit the binding of soluble rabbit IgG--antigen complexes to the variants but not to the parent line. Finally, E coated with IgM and complement (EIgMC) were bound poorly by all the variants, relative to the J774 parent. These results show that rabbit IgG complexes are bound by both FcRI and FcRII on mouse macrophages. The impairment of EIgMC rosetting in the variants suggests that the C3b receptor and FcRII are related.
