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. 1987 Jan;6(1):109–114. doi: 10.1002/j.1460-2075.1987.tb04726.x

Cloning and expression of the cDNA coding for a human lymphocyte IgE receptor.

C Lüdin, H Hofstetter, M Sarfati, C A Levy, U Suter, D Alaimo, E Kilchherr, H Frost, G Delespesse
PMCID: PMC553364  PMID: 3034567

Abstract

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.

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Selected References

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