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Isolation of an mRNA encoding a soluble form of the human interleukin-6 receptor

Lust, John A., Donovan, Kathleen A., Kline, Michael P., Greipp, Philip R., Kyle, Robert A., Maihle, Nita J.·1992·Cytokine
DOI 10.1016/1043-4666(92)90043-q
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Abstract

Soluble forms of the interleukin (IL)-2, IL-4 and IL-7 receptors which lack the transmembrane domain have been described. IL-6 is a growth factor important in the final differentiation of B-cells into plasma cells and in the pathogenesis of multiple myeloma. To determine whether the receptor for IL-6 may exist as a soluble molecule, RNA was analysed from the transformed B-cell lines U266, CESS and Daudi, from bone marrow from two myeloma patients, and from normal leukocytes. Using polymerase chain reaction, oligonucleotide primers which flank the transmembrane domain were selected to generate a 339 bp fragment. All samples produced equivalent amounts of the expected 339 bp fragment plus a smaller 245 bp fragment except Daudi which exhibited virtual absence of both. Sequence analysis of the smaller fragments from each of the five samples demonstrated the deletion of the entire transmembrane region from codons 356 (G-TG) to 387 (AG-G). The boundaries of this deletion were identical in all cases. Partial sequence analysis of the ligand-binding domain for U266 demonstrated identical sequences for the membrane-bound and soluble forms of the IL-6 receptor cDNAs. In summary, an mRNA which encodes a soluble form of the IL-6 receptor is expressed in both normal and myeloma cells.

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Metadata

Authors
Lust, J. A., Donovan, K. A., Kline, M. P., Greipp, P. R., Kyle, R. A., & Maihle, N. J.
Venue
Cytokine
Publisher
Elsevier BV
Published
1992-03
Volume
4
Issue
2
Pages
96-100
ISSN
1043-4666
DOI
10.1016/1043-4666(92)90043-q
Cited by
316
References
0
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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