We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Cloning and sequencing of the equine and ovine high-affinity IgE receptor β-and γ-chain cDNA.
- Authors
McAleese, S. M.; Miller, H. R. P.
- Abstract
The high-affinity receptor for IgE is expressed on the surface of mast cells and basophils. It is a transmembrane protein with one α, one β and two γ subunits. The cDNA sequences for the α subunit have already been determined. We report here the cDNA sequences for the β and γ subunits. The cytoplasmic domains of these subunits are important for intracellular signalling and the deduced amino acid sequences show the expected immunoreceptor tyrosine-based activation motifs. The γ subunit is highly conserved between species but more variation is seen with the β subunit. Near the C terminus of the equine β chain there is a two-base deletion, which changes the reading frame: residue 237 (human numbering) becomes Asp instead of Glu and the chain is three amino acids shorter than the other known mammalian and rodent sequences.
- Subjects
CLONING; GENETIC engineering; IMMUNOGLOBULIN E; BASOPHILS; PROTEIN analysis; AMINO acid sequence; GRANULOCYTES
- Publication
Immunogenetics, 2003, Vol 55, Issue 2, p122
- ISSN
0093-7711
- Publication type
Article
- DOI
10.1007/s00251-003-0564-y