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Molecular cloning of two isoforms of a receptor for the human hematopoietic
cytokine interleukin-11
M Cherel, M Sorel, B Lebeau, S Dubois, JF Moreau, R Bataille, S Minvielle and Y Jacques
Institut National de la Sante et de la Recherche Medicale (INSERM U211),
Nantes, France.
Interleukin-11 (IL-11) is a stromal cell-derived cytokine with multiple
biologic activities on lymphohematopoietic cells. It belongs to a family of
pleiotropic and redundant cytokines that use the gp 130 transducing subunit
in their high affinity receptors. By amplifying human cDNA libraries with
oligonucleotide primers corresponding to the conserved WSXWS motif found in
the hematopoietic cytokine receptor family, a novel cytokine receptor cDNA
was identified that, based on high (82%) sequence homology with the
recently cloned murine IL-11 receptor, appears to encode the human IL-11
receptor. This receptor is a 422-amino acid protein containing a signal
peptide followed by extracellular, transmembrane, and cytoplasmic domains.
The extracellular region has a two-domain structure homologous to those of
the IL-6 and ciliary neurotrophic factor (CNTF) receptors: an
immunoglobulin-like domain and a cytokine receptor-like domain. In
addition, an isoform of the human IL-11 receptor that lacks the cytoplasmic
domain was also identified. In agreement with the pleiotropic effects of
IL-11 on different hematopoietic lineages and bone cells, IL-11 receptor
transcripts were found to be expressed by the myelogenous leukemia cell
line K562, the megakaryocytic leukemia cell line Mo7E, the erythroleukemia
cell line TF1, and the osteosarcoma cell lines MG-63 and Saos-2.
Volume 86,
Issue 7,
pp. 2534-2540,
10/01/1995
Copyright © 1995 by The American Society of Hematology
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