Open AccessHuman lymphocyte Fc receptor for IgE: sequence homology of its cloned cDNA with animal lectins.
Author(s) -
Koichi Ikuta,
Masaaki Takami,
Choong Won Kim,
Tasuku Honjo,
Takashi Miyoshi,
Yutaka Tagaya,
Takumi Kawabe,
Junji Yodoi
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.3.819
Subject(s) - receptor , biology , complementary dna , microbiology and biotechnology , asialoglycoprotein receptor , fc receptor , peptide sequence , immunoglobulin e , fragment crystallizable region , biochemistry , transmembrane domain , antibody , gene , immunology , in vitro , hepatocyte
We have purified the human lymphocyte Fc receptor specific for IgE (Fc epsilon receptor) and its soluble form by using the anti-Fc epsilon receptor monoclonal antibody H107. Using an oligonucleotide probe corresponding to the partial amino acid sequence of the soluble Fc epsilon receptor related to IgE binding factor, we cloned, sequenced, and expressed a cDNA for the receptor. The Fc epsilon receptor has 321 amino acid residues with no NH2-terminal signal sequence. The receptor was separated into two domains by a putative 24-amino acid residue transmembrane region located near the NH2-terminal end. The Fc epsilon receptor showed a marked homology with animal lectins including human and rat asialoglycoprotein receptors, chicken hepatic lectin, and rat mannose binding proteins.