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Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor.
Author(s) -
Lüdin C.,
Hofstetter H.,
Sarfati M.,
Levy C.A.,
Suter U.,
Alaimo D.,
Kilchherr E.,
Frost H.,
Delespesse G.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb04726.x
Subject(s) - biology , complementary dna , cloning (programming) , immunoglobulin e , expression cloning , coding region , molecular cloning , genetics , microbiology and biotechnology , gene , antibody , programming language , computer science
Low‐affinity receptors (Fc epsilon R) and secreted factors (IgE‐BF) which bind to immunoglobulins of the IgE isotype play a key role in the regulation of human IgE synthesis. We report here the cloning of a cDNA coding for the Fc epsilon R of the human B‐lymphoblast cell line RPMI 8866. The nucleotide sequence of this cDNA predicts a polypeptide with 321 amino acids and a mol. wt of 36,281 daltons. A functional Fc epsilon R capable of binding IgE was expressed in Chinese hamster ovary cells after stable transformation with the cDNA which had been cloned into a mammalian expression vector. Amino acid sequence analysis of IgE‐BF purified from RPMI 8866 cells revealed an amino‐terminal sequence of 19 residues which coincides with the predicted amino acid sequence of the Fc epsilon R, starting at residues 148 and 150. A computer search with the translated amino acid sequence of the Fc epsilon R revealed a domain of 120 amino acids having striking homology to the human asialoglycoprotein receptors.