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Molecular cloning of a human immunoglobulin G Fc receptor.

Hibbs ML, Bonadonna L, Scott BM, McKenzie IF, Hogarth PM

  • Journal Proceedings of the National Academy of Sciences of the United States of America

  • Published 12 May 1988

  • Volume 85

  • ISSUE 7

  • Pagination 2240-4

  • DOI 10.1073/pnas.85.7.2240


Human IgG Fc receptor (Fc gamma R) cDNA clones were isolated by cross-species hybridization by probing cDNA libraries with the low-affinity Fc gamma R beta 1 cDNA clone from mouse as well as a pool of oligonucleotides constructed from the nucleotide sequence of this Fc gamma R. Three cDNA clones were isolated and analysis of the predicted amino acid sequence indicated that the human Fc gamma R protein is synthesized with a 34-amino acid leader and the mature protein is composed of 281 amino acids. The extracellular region of this Fc gamma R was divided into two domains, which were very similar to each other and to the corresponding regions of both mouse alpha and beta Fc gamma Rs and showed a clear relationship to immunoglobulin variable regions. One possible N-linked glycosylation site was found in each of the extracellular domains. The human Fc gamma R leader sequence was shown to be similar to the mouse alpha Fc gamma R leader sequence, but the transmembrane region was most similar to the mouse beta 1 Fc gamma R. The intracellular domain of the human Fc gamma R was surprisingly different from both mouse Fc gamma Rs. RNA blot analysis of human cells demonstrated two transcripts (2.5 and 1.5 kilobases) that arise by use of different adenylylation signals. The cellular expression of these transcripts suggest that they encode the low-affinity p40 Fc gamma R protein.