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                <term xml:lang="en">Co-receptor chondroitin sulphate</term>
                <term xml:lang="en">Cytokine bioavailability</term>
                <term xml:lang="en">Interleukin-34</term>
                <term xml:lang="en">M-CSFR</term>
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              <classCode scheme="mesh">Cell Line ; Cell Movement/drug effects ; Chondroitin Sulfates/metabolism ; Humans ; Interleukins/metabolism* ; Interleukins/pharmacology ; Macrophage Colony-Stimulating Factor/metabolism ; Models, Biological ; Myeloid Cells/cytology ; Myeloid Cells/drug effects ; Phosphorylation/drug effects ; Protein Binding/drug effects ; RNA, Small Interfering/metabolism ; Receptor, Macrophage Colony-Stimulating Factor/metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 5/metabolism ; Syndecan-1/metabolism*</classCode>
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              <p>IL-34 is a challenging cytokine sharing functional similarities with M-CSF through M-CSFR activation. It also plays a singular role that has recently been explained in the brain, through a binding to the receptor protein tyrosine phosphatase RPTPβ/ζ. The aim of this paper was to look for alternative binding of IL-34 on other cell types. Myeloid cells (HL-60, U-937, THP-1) were used as cells intrinsically expressing M-CSFR, and M-CSFR was expressed in TF-1 and HEK293 cells. IL-34 binding was studied by Scatchard and binding inhibition assays, using 125I-radiolabelled cytokines, and surface plasmon resonance. M-CSFR activation was analysed by Western blot after glycosaminoglycans abrasion, syndecan-1 overexpression or repression and addition of a blocking anti-syndecan antibody. M-CSF and IL-34 induced different patterns of M-CSFR phosphorylations, suggesting the existence of alternative binding for IL-34. Binding experiments and chondroitinase treatment confirmed low affinity binding to chondroitin sulphate chains on cells lacking both M-CSFR and RPTPβ/ζ. Amongst the proteoglycans with chondroitin sulphate chains, syndecan-1 was able to modulate the IL-34-induced M-CSFR signalling pathways. Interestingly, IL-34 induced the migration of syndecan-1 expressing cells. Indeed, IL-34 significantly increased the migration of THP-1 and M2a macrophages that was inhibited by addition of a blocking anti-syndecan-1 antibody. This paper provides evidence of alternative binding of IL-34 to chondroitin sulphates and syndecan-1 at the cell surface that modulates M-CSFR activation. In addition, IL-34-induced myeloid cell migration is a syndecan-1 dependent mechanism.</p>
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