Title |
Identification of multiple isoforms of the low-affinity human IgG Fc receptor
|
---|---|
Published in |
Immunogenetics, July 1989
|
DOI | 10.1007/bf02421463 |
Pubmed ID | |
Authors |
Tetsunori Seki |
Abstract |
Two varieties of similar, but structurally distinct, cDNA clones for the human low-affinity receptors for the Fc portion of immunoglobulin G (Fc gamma RII) have been isolated. One type of clone was obtained from human B lymphocytes, and the other from PHA-activated peripheral T cells and monocytes. Transfection of both prototype clones into Cos-7 cells and subsequent specific staining with monoclonal antibodies of the CDw32 group confirmed the identification of the gene products. The nucleotide sequence of the cDNA clone from B lymphocytes contains an open reading frame that encodes a protein of relative mass (Mr) 27,000 with an extracellular domain of 179 amino acids containing three potential N-glycosylation sites, a 26 amino acid transmembrane domain, and a 44 amino acid cytoplasmic domain. The clones from peripheral T cells and monocytes both encoded a protein of Mr 31,000 with a 179 amino acid extracellular domain containing two potential N-glycosylation sites and a 26 amino acid transmembrane domain. The two types of clones had similar sequences in their immunoglobulin-like extracellular and transmembrane domain, but differed in their leader sequences and 3'untranslated regions. The most notable difference between the clones was the presence of a distinctive 76 amino acid cytoplasmic domain in those isolated from T cells and monocytes. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 2 | 40% |
Student > Ph. D. Student | 1 | 20% |
Student > Master | 1 | 20% |
Unknown | 1 | 20% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 4 | 80% |
Unknown | 1 | 20% |