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International Immunology, Vol. 11, No. 12, 1965-1970, December 1999
© 1999 Japanese Society for Immunology

Characterization of the membrane-bound and a soluble form of human IL-4 receptor {alpha} produced by alternative splicing

Susanne Kruse, Johannes Forster, Joachim Kuehr and Klaus A. Deichmann

University Children's Hospital, University of Freiburg, Mathildenstrasse 1, 79106 Freiburg, Germany

Correspondence to: K. A. Deichmann

IL-4 plays a major role in IgE production. Its signal is conferred to effector cells through binding to the {alpha} chain of the membrane-bound human IL-4 receptor (huIL-4R{alpha}). Here we present the genomic structure and organization of huIL-4R{alpha}. The promotor region shows binding sites for several transcription factors involved in inflammatory processes. HuIL-4R{alpha} has been shown to be organized differently to that of mouse IL-4R{alpha}. A soluble form of huIL-4R{alpha} is produced by alternative splicing of the huIL-4R{alpha} gene (shuIL-4R{alpha}/splice). Expression of the corresponding mRNA coding for the extracellular part of the receptor and an additional three amino acids is also shown. A second form of huIL-4R{alpha}, i.e. shuIL-4R{alpha}/prot, is produced by limited proteolysis of the receptor (shedding) and is already known. These results reveal a complex pattern for the regulation of the IL-4 pathway at the receptor level. The patterns of expression of all three receptor proteins as well as their individual meaning in the context of inflammation still have to be elucidated.

Keywords: genomic structure, IL-4 receptor, soluble, splicing

Transmitting editor: A. Radbruch


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