Open AccessAssociation of the high-affinity receptor for IgG (Fc gamma RI) with the gamma subunit of the IgE receptor.
Author(s) -
Л. К. Эрнст,
AnneMarie Duchemin,
Clark L. Anderson
Publication year - 1993
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.13.6023
Subject(s) - gamma subunit , receptor , antibody , immunoglobulin e , microbiology and biotechnology , protein subunit , fc receptor , fragment crystallizable region , interleukin 10 receptor, alpha subunit , cd64 , chemistry , interleukin 5 receptor alpha subunit , common gamma chain , biology , biochemistry , g alpha subunit , immunology , interleukin 21 receptor , gene
How receptors for the Fc portion of IgG antibodies (Fc gamma R) trigger a variety of immune functions by clustering upon engagement of ligand is largely unknown. Of the three distinct classes of human Fc gamma R, only Fc gamma RIIIA has been shown to associate with a potential signal-generating subunit, either the gamma chain or the zeta chain. With these studies we show that Fc gamma RI, the high-affinity receptor for IgG, also is found in association with gamma chain. This association can be demonstrated by using anti-Fc gamma RI antibodies, Fc gamma RI ligand, and anti-gamma-chain antibodies that coadsorb the proteins from detergent lysates of Fc gamma RI-expressing cells. The association of Fc gamma RI and gamma chain can be reconstituted by cotransfection of cDNAs for both proteins into COS cells.