Adherence influences monocyte responsiveness to interleukin-10.
We studied the effects of adherence on the properties of interleukin (IL)-10 on monocyte-enriched peripheral blood mononuclear cells. We found that the decrease of CD11b expression induced by IL-10 was enhanced by adherence. Toll-like receptor (TLR)2 and TLR4 mRNA, as well as TLR4 surface expression, were significantly up-regulated by IL-10 in adherent cells. The absence of adherence prevented the inhibitory effects of IL-10 on lipopolysaccharide-induced tumor necrosis factor (TNF) and granulocyte-colony stimulating factor production and increased IL-1beta production and soluble TNF receptor II release in IL-10-pretreated cells. Similarly, the absence of adherence amplified the enhancement of phagocytosis induced by IL-10. Tyk2 and signal transducer and activator of transcription 3 (STAT3) phosphorylation and suppressor of cytokine signaling 3 (SOCS3) expression were induced by IL-10 in both conditions, but a longer activation and/or expression were observed in adherent monocytes. Finally, heme oxygenase-1, an anti-inflammatory molecule, was induced by IL-10 in adherent monocytes, whereas its expression remained low in nonadherent cells. Altogether, these data illustrate that adherence modulates the properties and the anti-inflammatory effects of IL-10.
Petit-Bertron
Anne-France
AF
UP Cytokines & Inflammation, Institut Pasteur, 28 rue Dr Roux, 75015 Paris, France.
Fitting
Catherine
C
Cavaillon
Jean-Marc
JM
Adib-Conquy
Minou
M
D015703:Antigens, CD / Q000187:drug effects; D002448:Cell Adhesion / Q000502:physiology*; D016207:Cytokines / Q000187:drug effects / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000187:drug effects; D029721:Drosophila Proteins; D006419:Heme Oxygenase (Decyclizing) / Q000187:drug effects; D051547:Heme Oxygenase-1; D006801:Humans; D016753:Interleukin-10 / Q000494:pharmacology*; D008562:Membrane Glycoproteins / Q000187:drug effects / Q000378:metabolism; D008565:Membrane Proteins; D009000:Monocytes / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D010587:Phagocytosis / Q000187:drug effects; D011505:Protein-Tyrosine Kinases; D011506:Proteins / Q000187:drug effects; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000378:metabolism; D012097:Repressor Proteins; D050796:STAT3 Transcription Factor; D015398:Signal Transduction / Q000187:drug effects; D000071223:Suppressor of Cytokine Signaling 3 Protein; D050826:Suppressor of Cytokine Signaling Proteins; D053634:TYK2 Kinase; D051195:Toll-Like Receptor 2; D051197:Toll-Like Receptor 4; D051193:Toll-Like Receptors; D015534:Trans-Activators / Q000187:drug effects; D014157:Transcription Factors
D015703:Antigens, CD; D016207:Cytokines; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D011506:Proteins; D011956:Receptors, Cell Surface; D012097:Repressor Proteins; C106644:SOCS3 protein, human; D050796:STAT3 Transcription Factor; C494086:STAT3 protein, human; D000071223:Suppressor of Cytokine Signaling 3 Protein; D050826:Suppressor of Cytokine Signaling Proteins; C495342:TLR2 protein, human; C495345:TLR4 protein, human; D051195:Toll-Like Receptor 2; D051197:Toll-Like Receptor 4; D051193:Toll-Like Receptors; D015534:Trans-Activators; D014157:Transcription Factors; D016753:Interleukin-10; C496541:HMOX1 protein, human; D006419:Heme Oxygenase (Decyclizing); D051547:Heme Oxygenase-1; D011505:Protein-Tyrosine Kinases; D053634:TYK2 Kinase; C070139:TYK2 protein, human