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J. Exp. Med.,
Volume 189, Number 2, January 18, 1999 309-318
By
§¶
From the Division of Developmental and Clinical Immunology, * Department of Pathology, PIR-A and PIR-B, paired immunoglobulin-like receptors encoded, respectively, by multiple
Pira genes and a single Pirb gene in mice, are relatives of the human natural killer (NK) and Fc receptors. Monoclonal and polyclonal antibodies produced against a recombinant PIR protein
identified cell surface glycoproteins of ~85 and ~120 kD on B cells, granulocytes, and macrophages. A disulfide-linked homodimer associated with the cell surface PIR molecules was
identified as the Fc receptor common Department of Microbiology, § Department of Pediatrics, and Department of Medicine, University of
Alabama at Birmingham, and the ¶ Howard Hughes Medical Institute, Birmingham, Alabama
35294; and the ** Laboratory of Molecular Genetics and Immunology, The Rockefeller University,
New York 10021
(FcRc) chain. Whereas PIR-B fibroblast transfectants
expressed cell surface molecules of ~120 kD, PIR-A transfectants expressed the ~85-kD molecules exclusively intracellularly; PIR-A and FcRc cotransfectants expressed the PIR-A/
FcRc complex on their cell surface. Correspondingly, PIR-B was normally expressed on the
cell surface of splenocytes from FcRc
/ mice whereas PIR-A was not. Cell surface levels of
PIR molecules on myeloid and B lineage cells increased with cellular differentiation and activation. Dendritic cells, monocytes/macrophages, and mast cells expressed the PIR molecules in
varying levels, but T cells and NK cells did not. These experiments define the coordinate cellular expression of PIR-B, an inhibitory receptor, and PIR-A, an activating receptor; demonstrate the requirement of FcRc chain association for cell surface PIR-A expression; and suggest that the level of FcRc chain expression could differentially affect the PIR-A/PIR-B
equilibrium in different cell lineages.
chain;
activating receptor;
inhibitory receptor;
dendritic cells;
innate immunity
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