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

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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
Volume163
Issue number12
Publication statusPublished - Dec 28 1999

Fingerprint

Granulocyte Colony-Stimulating Factor Receptors
Granulocyte Precursor Cells
Granulocyte Colony-Stimulating Factor
Protein Isoforms
Myeloid Cells
Monocytes
Neutrophils
Myelopoiesis
Messenger RNA
Serum
Cell Line
Polymerase Chain Reaction
Membranes
Population

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

Cite this

Iwasaki, H., Shimoda, K., Okamura, S., Otsuka, T., Nagafuji, K., Harada, N., ... Niho, Y. (1999). Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells. Journal of Immunology, 163(12), 6907-6911.

Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells. / Iwasaki, Hiromi; Shimoda, Kazuya; Okamura, Seiichi; Otsuka, Teruhisa; Nagafuji, Koji; Harada, Naoki; Ohno, Yuju; Miyamoto, Toshihiro; Akashi, Koichi; Harada, Mine; Niho, Yoshiyuki.

In: Journal of Immunology, Vol. 163, No. 12, 28.12.1999, p. 6907-6911.

Research output: Contribution to journalArticle

Iwasaki, H, Shimoda, K, Okamura, S, Otsuka, T, Nagafuji, K, Harada, N, Ohno, Y, Miyamoto, T, Akashi, K, Harada, M & Niho, Y 1999, 'Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells', Journal of Immunology, vol. 163, no. 12, pp. 6907-6911.
Iwasaki H, Shimoda K, Okamura S, Otsuka T, Nagafuji K, Harada N et al. Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells. Journal of Immunology. 1999 Dec 28;163(12):6907-6911.
Iwasaki, Hiromi ; Shimoda, Kazuya ; Okamura, Seiichi ; Otsuka, Teruhisa ; Nagafuji, Koji ; Harada, Naoki ; Ohno, Yuju ; Miyamoto, Toshihiro ; Akashi, Koichi ; Harada, Mine ; Niho, Yoshiyuki. / Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells. In: Journal of Immunology. 1999 ; Vol. 163, No. 12. pp. 6907-6911.
@article{2832dfa3264945c99e3081de56491806,
title = "Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells",
abstract = "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.",
author = "Hiromi Iwasaki and Kazuya Shimoda and Seiichi Okamura and Teruhisa Otsuka and Koji Nagafuji and Naoki Harada and Yuju Ohno and Toshihiro Miyamoto and Koichi Akashi and Mine Harada and Yoshiyuki Niho",
year = "1999",
month = "12",
day = "28",
language = "English",
volume = "163",
pages = "6907--6911",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "12",

}

TY - JOUR

T1 - Production of soluble granulocyte colony-stimulating factor receptors from myelomonocytic cells

AU - Iwasaki, Hiromi

AU - Shimoda, Kazuya

AU - Okamura, Seiichi

AU - Otsuka, Teruhisa

AU - Nagafuji, Koji

AU - Harada, Naoki

AU - Ohno, Yuju

AU - Miyamoto, Toshihiro

AU - Akashi, Koichi

AU - Harada, Mine

AU - Niho, Yoshiyuki

PY - 1999/12/28

Y1 - 1999/12/28

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0032715667&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032715667&partnerID=8YFLogxK

M3 - Article

C2 - 10586093

AN - SCOPUS:0032715667

VL - 163

SP - 6907

EP - 6911

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 12

ER -