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J Biol Chem, Vol. 275, Issue 13, 9178-9185, March 31, 2000
From INSERM, Unité 349, affiliated to CNRS, Hôpital
Lariboisière, 75475 Paris Cedex 10 and § Laboratoire
d'Histologie-Embryologie, Université d'Angers, 49045 Angers,
France
We previously showed that granulocyte-macrophage
colony-stimulating factor (GM-CSF) binds to heparan sulfate
proteoglycans expressed at the surface of osteoblastic cells and that
the mitogenic activity of this cytokine is dependent on the presence of
fully sulfated proteoglycans. In this study, we determined if GM-CSF interacts with syndecans, a family of cell surface heparan sulfate proteoglycans. Human primary osteoblasts were found to express syndecan-2 and -4 but few syndecan-1 transcripts and proteins. Recombinant human GM-CSF coupled to biotin was found to bind to syndecan-2. Immunocytochemical transmission electron microscope analysis showed co-localization of syndecan-2 and GM-CSF at the cell
membrane surface. Syndecan-2 also co-localized at the cell surface and
co-immunoprecipitated with the GM-CSF receptor
Syndecan-2 Is Involved in the Mitogenic Activity and Signaling of
Granulocyte-Macrophage Colony-stimulating Factor in Osteoblasts*
,
chain, suggesting a
strong interaction between the cytokine, its receptor, and syndecan-2.
Phosphorylation of tyrosine residues in syndecan-2 associated with the
chain of the GM-CSF receptor was increased after cell stimulation
by GM-CSF. Antisense oligonucleotides that reduced specifically the
expression of syndecan-2 inhibited the mitogenic activity of GM-CSF and
the activation of extracellular signal-regulated kinase-1 induced by
the cytokine. Our results indicate functional interactions between
syndecan-2 and GM-CSF in osteoblasts, and we propose that syndecan-2
plays a role as a co-receptor for this cytokine.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: U349 INSERM, 2 rue
Ambroise Paré, 75475 Paris Cedex 10, France. Tel.: 33-1-49 95 63 58; Fax: 33-1-49 95 84 52; E-mail:
dominique.modrowski@inserm.lrb.ap-hop-paris.fr.
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