Phagocytic cells of the immune system express specific receptors for the Fc
region of immunoglobulins (FcRs). In humans, most FcRs for IgG (Fc gammaR)
, IgA (Fc alphaR) and IgE (Fc epsilonR) consist of an immunoglobulin (Ig) -
binding subunit associated with a specialized signaling molecule, the FcR g
amma chain. The FeR gamma chain is crucial for the transmission of intracel
lular signals following receptor ligation. In cattle, however, although fou
r distinct complimentary DNAs (cDNAs) encoding IgG-binding subunits have be
en described (corresponding to bovine Fc gamma RI, Fc gamma RII, Fc gamma R
III, and Fc gamma 2R), virtually, nothing is known about signal transductio
n via bovine FcRs. Therefore, in this study, a cDNA encoding the bovine FcR
gamma chain was cloned. The cDNA is 258 base pairs long and encodes a prot
ein of 85 amino-acids. The mature protein shows high homology with the FcR
gamma chains from several other species. Interestingly, the cytoplasmic dom
ain of the bovine FeR gamma chain is one amino-acid shorter than those prev
iously described. Cloning of a cDNA encoding, the bovine FcR gamma chain wi
ll allow for a better understanding of signal transduction processes trigge
red by bovine FcRs. (C) 2001 Elsevier Science B.V. All rights reserved.