FcεRI

protein
Name=Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide
caption=


width=
HGNCid=3609
Symbol=FCER1A
AltSymbols=FCE1A
EntrezGene=2205
OMIM=147140
RefSeq=NM_002001
UniProt=P12319
PDB=
ECnumber=
Chromosome=1
Arm=q
Band=23
LocusSupplementaryData=protein
Name= membrane-spanning 4-domains, subfamily A, member 2 (Fc fragment of IgE, high affinity I, receptor for; beta polypeptide)
caption=


width=
HGNCid=7316
Symbol=MS4A2
AltSymbols=FCER1B, IGER, APY
EntrezGene=2206
OMIM=147138
RefSeq=NM_000139
UniProt=Q01362
PDB=
ECnumber=
Chromosome=1
Arm=q
Band=23
LocusSupplementaryData=protein
Name=Fc fragment of IgE, high affinity I, receptor for; gamma polypeptide
caption=


width=
HGNCid=3611
Symbol=FCER1G
AltSymbols=
EntrezGene=2207
OMIM=147139
RefSeq=NM_004106
UniProt=P30273
PDB=
ECnumber=
Chromosome=1
Arm=q
Band=23
LocusSupplementaryData=

FcεRI, or Fc epsilon RI, is the high-affinity receptor for immunoglobulin E (IgE), an antibody isotype involved in allergy and resistance to parasites. FcεRI is a tetrameric receptor complex consisting of one alpha (FcεRIα), one beta (FcεRIβ), and two gamma chains (FcεRIγ). It is expressed predominantly on mast cells and basophils.

Crosslinking of the FcεRI via IgE-allergen complexes leads to degranulation of mast cells or basophils and release of inflammatory mediators. At laboratory conditions degranulation of isolated basophils can also be induced with antibodies to the FcεRIα which crosslink the receptor. Such crosslinking and potentially pathogenic autoantibodies to the FcεRIα have been isolated from human cord blood, which suggest that they occur naturally and are present already at birth. However, their epitope on FcεRIα was masked by IgE and the affinity of the corresponding autoantibodies found in healthy adults appeared lowered. [The Journal of Immunology 2005, 175: 6589-6596. (Bobrzynski et al., 2005, PMID: 16272313, [http://www.jimmunol.org/cgi/content/full/175/10/6589 Full text] )]

References

External links

*