Impaired dendritic cell function in Crohn’s disease patients with NOD2 3020insC mutation
The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn’s disease (CD), but the mechanism remains controversial. Loss‐of‐function and gain‐of‐function phenotypes have been described as a result of NOD2fs. Here, we show that dendritic cells (DC) der...
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| Published in: | Journal of leukocyte biology Vol. 79; no. 4; pp. 860 - 866 |
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| Abstract | The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn’s disease (CD), but the mechanism remains controversial. Loss‐of‐function and gain‐of‐function phenotypes have been described as a result of NOD2fs. Here, we show that dendritic cells (DC) derived from CD patients homozygous for this mutation respond normally to purified Toll‐like receptor (TLR) ligands but fail to up‐regulate the costimulatory molecules CD80 and CD86 in response to the NOD2 ligand muramyl dipeptide (MDP). Moreover, they lack MDP‐induced enhancement of TLR‐mediated tumor necrosis factor α, interleukin (IL)‐12, and IL‐10 production, which is observed in control DC with intact NOD2. These data indicate that the NOD2fs mutation results in a loss‐of‐function phenotype in human myeloid DC and imply decreased immune regulation by IL‐10 as a possible mechanism for this mutation in CD. |
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| AbstractList | The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn's disease (CD), but the mechanism remains controversial. Loss-of-function and gain-of-function phenotypes have been described as a result of NOD2fs. Here, we show that dendritic cells (DC) derived from CD patients homozygous for this mutation respond normally to purified Toll-like receptor (TLR) ligands but fail to up-regulate the costimulatory molecules CD80 and CD86 in response to the NOD2 ligand muramyl dipeptide (MDP). Moreover, they lack MDP-induced enhancement of TLR-mediated tumor necrosis factor alpha, interleukin (IL)-12, and IL-10 production, which is observed in control DC with intact NOD2. These data indicate that the NOD2fs mutation results in a loss-of-function phenotype in human myeloid DC and imply decreased immune regulation by IL-10 as a possible mechanism for this mutation in CD. The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn’s disease (CD), but the mechanism remains controversial. Loss‐of‐function and gain‐of‐function phenotypes have been described as a result of NOD2fs. Here, we show that dendritic cells (DC) derived from CD patients homozygous for this mutation respond normally to purified Toll‐like receptor (TLR) ligands but fail to up‐regulate the costimulatory molecules CD80 and CD86 in response to the NOD2 ligand muramyl dipeptide (MDP). Moreover, they lack MDP‐induced enhancement of TLR‐mediated tumor necrosis factor α, interleukin (IL)‐12, and IL‐10 production, which is observed in control DC with intact NOD2. These data indicate that the NOD2fs mutation results in a loss‐of‐function phenotype in human myeloid DC and imply decreased immune regulation by IL‐10 as a possible mechanism for this mutation in CD. The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn's disease (CD), but the mechanism remains controversial. Loss-of-function and gain-of-function phenotypes have been described as a result of NOD2fs. Here, we show that dendritic cells (DC) derived from CD patients homozygous for this mutation respond normally to purified Toll-like receptor (TLR) ligands but fail to up-regulate the costimulatory molecules CD80 and CD86 in response to the NOD2 ligand muramyl dipeptide (MDP). Moreover, they lack MDP-induced enhancement of TLR-mediated tumor necrosis factor a, interleukin (IL)-12, and IL-10 production, which is observed in control DC with intact NOD2. These data indicate that the NOD2fs mutation results in a loss-of-function phenotype in human myeloid DC and imply decreased immune regulation by IL-10 as a possible mechanism for this mutation in CD. |
| Author | Matthijs Kramer Dirk J. de Jong Bart Jan Kullberg Gosse J. Adema Mihai G. Netea |
| Author_xml | – sequence: 1 givenname: Matthijs surname: Kramer fullname: Kramer, Matthijs – sequence: 2 givenname: Mihai G. surname: Netea fullname: Netea, Mihai G. – sequence: 3 givenname: Dirk J. surname: Jong fullname: Jong, Dirk J. – sequence: 4 givenname: Bart Jan surname: Kullberg fullname: Kullberg, Bart Jan – sequence: 5 givenname: Gosse J. surname: Adema fullname: Adema, Gosse J. email: g.adema@ncmls.ru.nl |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16461743$$D View this record in MEDLINE/PubMed |
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| Snippet | The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn’s disease (CD), but the mechanism remains... The nucleotide oligomerization domain 2 (NOD2) 3020insC (NOD2fs) mutation increases susceptibility to Crohn's disease (CD), but the mechanism remains... |
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| SubjectTerms | Acetylmuramyl-Alanyl-Isoglutamine - pharmacology Adult Crohn Disease - genetics Crohn Disease - immunology cytokines Cytokines - biosynthesis Dendritic Cells - drug effects Dendritic Cells - immunology Female human Humans Interleukin-10 - pharmacology Intracellular Signaling Peptides and Proteins - genetics Ligands Male Middle Aged Mutation Nod2 Signaling Adaptor Protein Phenotype Toll-Like Receptors - immunology Toll‐like receptor |
| Title | Impaired dendritic cell function in Crohn’s disease patients with NOD2 3020insC mutation |
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