Human and rat mast cell high-affinity immunoglobulin E receptors: characterization of putative alpha-chain gene products.

作者：Akira Shimizu, I Tepler, Philip N. Benfey, Elsa H. Berenstein, R P Siraganian, Philip Leder · 发表于：Proceedings of the National Academy of Sciences · 年份：1988 · DOI：10.1073/pnas.85.6.1907 · 被引用次数：112 · 研究领域：Monoclonal and Polyclonal Antibodies Research、Glycosylation and Glycoproteins Research、RNA and protein synthesis mechanisms

We have cloned and determined the entire nucleotide sequence of cDNAs corresponding to the putative alpha subunits of the human and rat mast cell high-affinity IgE receptors. Both human and rat cDNAs encode an NH2-terminal signal peptide, two immunoglobulin-like extracellular domains (encoded by discrete exons), a hydrophobic transmembrane region, and a positively charged cytoplasmic tail. The human and rat alpha subunits share an overall homology with one another and the immunoglobulin gene family, suggesting that they arose from a common ancestral gene and continue to share structural homology with their ligands. In addition, the rat gene is transcribed into at least three distinct forms, each of which yields a somewhat different coding sequence.