Abstract
Hematopoietic growth factor receptors, in general, are integral membrane proteins composed of an extracellular ligand-binding domain, a transmembrane domain, and an intracellular signal-transducing domain. Soluble receptors that lack the transmembrane domain have been shown to be potent immunomodulators of their respective ligands [1–6]. Since IL-6 has been shown to be a central growth factor for myeloma cells [7], an sIL-6R may modulate myeloma cell growth. A novel IL-6R mRNA was isolated from human myeloma cells that exhibits a deletion of the entire transmembrane domain [8]. The corresponding cDNA was sequenced, expressed in fibroblasts, and the functional activity of the protein product was determined using an IL-6 dependent cell line.
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© 1995 Springer-Verlag Berlin Heidelberg
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Lust, J.A. et al. (1995). Sequence, Expression and Function of an mRNA Encoding a Soluble Form of the Human Interleukin-6 Receptor (sIL-6R). In: Potter, M., Melchers, F. (eds) Mechanisms in B-Cell Neoplasia 1994. Current Topics in Microbiology and Immunology, vol 194. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79275-5_24
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DOI: https://doi.org/10.1007/978-3-642-79275-5_24
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