FcεRI

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Fc fragment of IgE, high affinity I, receptor for; alpha polypeptide
Identifiers
SymbolFCER1A
Alt. symbolsFCE1A
Entrez2205
HUGO3609
OMIM147140
RefSeqNM_002001
UniProtP12319
Other data
LocusChr. 1 q23
membrane-spanning 4-domains, subfamily A, member 2 (Fc fragment of IgE, high affinity I, receptor for; beta polypeptide)
Identifiers
SymbolMS4A2
Alt. symbolsFCER1B, IGER, APY
Entrez2206
HUGO7316
OMIM147138
RefSeqNM_000139
UniProtQ01362
Other data
LocusChr. 1 q23
Fc fragment of IgE, high affinity I, receptor for; gamma polypeptide
Identifiers
SymbolFCER1G
Entrez2207
HUGO3611
OMIM147139
RefSeqNM_004106
UniProtP30273
Other data
LocusChr. 1 q23

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.[1]

References

  1. The Journal of Immunology 2005, 175: 6589-6596. (Bobrzynski et al., 2005, PMID: 16272313, Full text)

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