Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells

Hiromi Iwasaki, Kazuya Shimoda, Seiichi Okamura, Teruhisa Otsuka, Koji Nagafuji, Naoki Harada, Yuju Ohno, Toshihiro Miyamoto, Koichi Akashi, Mine Harada, Yoshiyuki Niho

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11 Citations (Scopus)


It has been speculated that a soluble form of G-CSFR might be physiologically present in humans, since G-CSFR mRNA that lacks a transmembrane domain has been identified from a human myelomonocytic cell line. Here, we demonstrate human soluble G-CSFR (sG-CSFR) of two different molecular sizes (80 and 85 kDa) on an immunoblot analysis using Abs generated against the amino-terminal, extracellular domain of the full-length G-CSFR. Both isoforms of sG-CSFR were able to bind recombinant human G-CSF (rhG-CSF). RT-PCR analysis with primers targeted outside of the transmembrane region revealed that membrane-anchored G-CSFR is expressed at all maturation stages of purified myeloid cells, including CD34+CD13+ cells (blasts), CD11b- CD15+ cells (promyelocytes or myelocytes), CD11b+CD15+ cells (metamyelocytes and mature neutrophils), and CD14+ cells (monocytes). On the other hand, sG-CSFR mRNA was detectable in CD11b-CD15+, CD11b+CD15+, and CD14+ cells, but not in the CD34+CD13+ blast population. The serum concentration of both isoforms of sG-CSFR appeared to be correlated with the numbers of neutrophils/monocytes before and after rhG-CSF treatment in normal individuals. Thus, two isoforms of SG-CSFR are physiologically secreted from relatively mature myeloid cells and might play an important role in myelopoiesis through their binding to serum G-CSF.

Original languageEnglish
Pages (from-to)6907-6911
Number of pages5
JournalJournal of Immunology
Issue number12
Publication statusPublished - 1999

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology


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