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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Kubagawa, Yoshiki Honjo, Kazuhito Kearney, John F. Kubagawa, Hiromi |
Description | Author Affiliation: Honjo K ( Division of Laboratory Medicine, Department of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294); Kubagawa Y ( Division of Laboratory Medicine, Department of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294); Kearney JF ( Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294.); Kubagawa H ( Division of Laboratory Medicine, Department of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294) |
Abstract | The IgM Fc receptor (FcµR) is the newest FcR, and coligation of FcµR and Fas/CD95 on Jurkat cells with agonistic IgM anti-Fas mAb was shown to inhibit Fas-induced apoptosis. The ligand-binding activity of human FcµR was further examined. FcµR-mediated protection from apoptosis was partially blocked by addition of 10(4) molar excess of IgM or its soluble immune complexes, but it could be inhibited by addition of 10-fold excess of IgM anti-CD2 mAb. This suggests that FcµR binds more efficiently to the Fc portion of IgM reactive with plasma-membrane proteins than to the Fc portion of IgM in solution. The former interaction occurred in cis on the same cell surface, but not in trans between neighboring cells. This cis engagement of FcµR resulted in modulation of Ca(2+) mobilization via CD2 on Jurkat cells or BCRs on blood B cells upon cross-linkage with the corresponding IgM mAbs. Several functional changes were observed with FcµR mutants: 1) significant increase in IgM ligand binding in the cytoplasmic tail-deletion mutant, 2) enhanced cap formation in FcµR upon IgM binding at 4°C with a point mutation of the transmembrane His to Phe, and 3) less protective activity of FcµR in IgM anti-Fas mAb-mediated apoptosis assays with a point mutation of the membrane-proximal Tyr to Phe. These findings show the importance of the cis engagement of FcµR and its critical role in receptor function. Hence, FcµR on B, T, and NK cells may modulate the function of surface proteins recognized by natural or immune IgM Abs on the shared membrane cell surface. |
ISSN | 00221767 |
e-ISSN | 15506606 |
DOI | 10.4049/jimmunol.1401866 |
Journal | The Journal of Immunology |
Issue Number | 4 |
Volume Number | 194 |
Language | English |
Publisher | The American Association of Immunologists |
Publisher Date | 2015-02-15 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Immunoglobulin Fc Fragments Immunology Lymphocyte Activation Receptors, Fc Signal Transduction Animals Antigen-antibody Complex Apoptosis B-lymphocytes Cell Line Fluorescent Antibody Technique Jurkat Cells Killer Cells, Natural Ligands Mice Mutagenesis, Site-directed Research Support, N.i.h., Extramural Discipline Immunology |
Content Type | Text |
Resource Type | Article |
Subject | Immunology and Allergy Immunology |
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