Extracellular forms of IL-37 inhibit innate inflammation in vitro and in vivo but require the IL-1 family decoy receptor IL-1R8
Significance Interleukin-1 family members are highly inflammatory but IL-37 member broadly suppresses inflammation and specific immunity. Initially, the mechanism of this suppression was shown to be via translocation to the nucleus following cleavage of the precursor by intracellular caspase-1. We n...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 112; no. 8; pp. 2497 - 2502 |
|---|---|
| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
24.02.2015
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Significance Interleukin-1 family members are highly inflammatory but IL-37 member broadly suppresses inflammation and specific immunity. Initially, the mechanism of this suppression was shown to be via translocation to the nucleus following cleavage of the precursor by intracellular caspase-1. We now show that recombinant forms of IL-37 limit inflammation by extracellular binding to surface receptors but require the IL-1 family decoy receptor IL-1R8. Unexpectedly, picomolar concentrations of the IL-37 precursor optimally suppress IL-1β, IL-6, and TNFα production from human blood M1 macrophages, suggesting a unique function for a coreceptor function of IL-1R8. Assessment of IL-37 as well as IL-1R8 levels may provide previously unidentified insights into how the host limits inflammation.
Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% ( P < 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti–IL-37 increased LPS-induced IL-6, TNFα and IL-1β ( P < 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFα mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background ( P < 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding α-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFα and IL-6 by 50–55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8–deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. |
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| AbstractList | Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% (P< 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti–IL-37 increased LPS-induced IL-6, TNFα and IL-1β (P< 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFα mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background (P< 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding α-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFα and IL-6 by 50–55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8–deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. Interleukin-1 family members are highly inflammatory but IL-37 member broadly suppresses inflammation and specific immunity. Initially, the mechanism of this suppression was shown to be via translocation to the nucleus following cleavage of the precursor by intracellular caspase-1. We now show that recombinant forms of IL-37 limit inflammation by extracellular binding to surface receptors but require the IL-1 family decoy receptor IL-1R8. Unexpectedly, picomolar concentrations of the IL-37 precursor optimally suppress IL-1β, IL-6, and TNFα production from human blood M1 macrophages, suggesting a unique function for a coreceptor function of IL-1R8. Assessment of IL-37 as well as IL-1R8 levels may provide previously unidentified insights into how the host limits inflammation. Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% ( P < 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti–IL-37 increased LPS-induced IL-6, TNFα and IL-1β ( P < 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFα mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background ( P < 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding α-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFα and IL-6 by 50–55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8–deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% (P < 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti-IL-37 increased LPS-induced IL-6, TNFα and IL-1β (P < 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFα mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background (P < 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding α-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFα and IL-6 by 50-55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8-deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties.Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% (P < 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti-IL-37 increased LPS-induced IL-6, TNFα and IL-1β (P < 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFα mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background (P < 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding α-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFα and IL-6 by 50-55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8-deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. Significance Interleukin-1 family members are highly inflammatory but IL-37 member broadly suppresses inflammation and specific immunity. Initially, the mechanism of this suppression was shown to be via translocation to the nucleus following cleavage of the precursor by intracellular caspase-1. We now show that recombinant forms of IL-37 limit inflammation by extracellular binding to surface receptors but require the IL-1 family decoy receptor IL-1R8. Unexpectedly, picomolar concentrations of the IL-37 precursor optimally suppress IL-1β, IL-6, and TNFα production from human blood M1 macrophages, suggesting a unique function for a coreceptor function of IL-1R8. Assessment of IL-37 as well as IL-1R8 levels may provide previously unidentified insights into how the host limits inflammation. Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% ( P < 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti–IL-37 increased LPS-induced IL-6, TNFα and IL-1β ( P < 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFα mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background ( P < 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding α-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFα and IL-6 by 50–55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8–deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. Similar to IL-1a and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we demonstrate an extracellular function of the IL-37 precursor and a processed form. Recombinant IL-37 precursor reduced LPS-induced IL-6 by 50% (P < 0.001) in highly inflammatory human blood-derived M1 differentiated macrophages derived from selective subjects but not M2 macrophages. In contrast, a neutralizing monoclonal anti-IL-37 increased LPS-induced IL-6, TNFα and IL-1β (P < 0.01). The suppression by IL-37 was consistently observed at low picomolar but not nanomolar concentrations. Whereas LPS induced a 12-fold increase in TNFa mRNA, IL-37 pretreatment decreased the expression to only 3-fold over background (P < 0.01). Mechanistically, LPS-induced p38 and pERK were reduced by IL-37. Recombinant IL-37 bound to the immobilized ligand binding a-chain of the IL-18 receptor as well as to the decoy receptor IL-1R8. In M1 macrophages, LPS increased the surface expression of IL-1R8. Compared with human blood monocytes, resting M1 cells express more surface IL-1R8 as well as total IL-1R8; there was a 16-fold increase in IL-1R8 mRNA levels when pretreated with IL-37. IL-37 reduced LPS-induced TNFa and IL-6 by 50-55% in mouse bone marrow-derived dendritic cells, but not in dendritic cells derived from IL-1R8-deficient mice. In mice subjected to systemic LPS-induced inflammation, pretreatment with IL-37 reduced circulating and organ cytokine levels. Thus, in addition to a nuclear function, IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. |
| Author | Hong, Jaewoo Fujita, Mayumi Barber, Kristina Neff, C. Preston Mantovani, Alberto Li, Suzhao Kim, Soohyun Azam, Tania Palmer, Brent E. Garlanda, Cecilia Luo, Yuchun Dinarello, Charles Anthony |
| Author_xml | – sequence: 1 givenname: Suzhao surname: Li fullname: Li, Suzhao organization: Department of Medicine, University of Colorado Denver, Aurora, CO 80045 – sequence: 2 givenname: C. Preston surname: Neff fullname: Neff, C. Preston organization: Department of Medicine, University of Colorado Denver, Aurora, CO 80045 – sequence: 3 givenname: Kristina surname: Barber fullname: Barber, Kristina organization: Department of Medicine, University of Colorado Denver, Aurora, CO 80045 – sequence: 4 givenname: Jaewoo surname: Hong fullname: Hong, Jaewoo organization: Laboratory of Cytokine Immunology, Konkuk University, 143-701 Seoul, Republic of Korea – sequence: 5 givenname: Yuchun surname: Luo fullname: Luo, Yuchun organization: Department of Dermatology, University of Colorado Denver, Aurora, CO 80045 – sequence: 6 givenname: Tania surname: Azam fullname: Azam, Tania organization: Department of Medicine, University of Colorado Denver, Aurora, CO 80045 – sequence: 7 givenname: Brent E. surname: Palmer fullname: Palmer, Brent E. organization: Department of Medicine, University of Colorado Denver, Aurora, CO 80045 – sequence: 8 givenname: Mayumi surname: Fujita fullname: Fujita, Mayumi organization: Department of Dermatology, University of Colorado Denver, Aurora, CO 80045 – sequence: 9 givenname: Cecilia surname: Garlanda fullname: Garlanda, Cecilia organization: Research Institute Humanitas, 20089 Milan, Italy – sequence: 10 givenname: Alberto surname: Mantovani fullname: Mantovani, Alberto organization: Research Institute Humanitas, 20089 Milan, Italy – sequence: 11 givenname: Soohyun surname: Kim fullname: Kim, Soohyun organization: Laboratory of Cytokine Immunology, Konkuk University, 143-701 Seoul, Republic of Korea – sequence: 12 givenname: Charles Anthony surname: Dinarello fullname: Dinarello, Charles Anthony organization: Department of Medicine, University of Colorado Denver, Aurora, CO 80045 |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25654981$$D View this record in MEDLINE/PubMed |
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| Notes | http://dx.doi.org/10.1073/pnas.1424626112 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 Author contributions: S.L., C.P.N., Y.L., B.E.P., M.F., S.K., and C.A.D. designed research; S.L., C.P.N., K.B., J.H., Y.L., T.A., B.E.P., M.F., C.G., A.M., S.K., and C.A.D. performed research; S.L., J.H., B.E.P., C.G., A.M., S.K., and C.A.D. contributed new reagents/analytic tools; S.L., C.P.N., K.B., Y.L., T.A., B.E.P., M.F., C.G., A.M., and C.A.D. analyzed data; and S.L., C.P.N., B.E.P., M.F., C.G., A.M., S.K., and C.A.D. wrote the paper. Contributed by Charles Anthony Dinarello, January 6, 2015 (sent for review November 12, 2014) |
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| Snippet | Significance Interleukin-1 family members are highly inflammatory but IL-37 member broadly suppresses inflammation and specific immunity. Initially, the... Similar to IL-1α and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we... Interleukin-1 family members are highly inflammatory but IL-37 member broadly suppresses inflammation and specific immunity. Initially, the mechanism of this... Similar to IL-1a and IL-33, IL-1 family member IL-37b translocates to the nucleus and is associated with suppression of innate and adaptive immunity. Here we... |
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| SubjectTerms | Animals Biological Sciences Blood Bone marrow caspase-1 Cell Differentiation - drug effects Cells Cytokines Endotoxemia - metabolism Endotoxemia - pathology Enzyme Activation - drug effects Extracellular Space - chemistry Flow Cytometry Gene expression Gene Expression Regulation - drug effects Humans Immobilized Proteins - metabolism immunity Immunity, Innate inflammation Inflammation - immunology Inflammation - pathology Interleukin-1 - chemistry Interleukin-1 - metabolism interleukin-1beta Interleukin-1beta - metabolism interleukin-6 Interleukin-6 - metabolism Lipopolysaccharides - pharmacology macrophages Macrophages - cytology Macrophages - drug effects Macrophages - enzymology Macrophages - metabolism Mice Neutralization Tests p38 Mitogen-Activated Protein Kinases - metabolism Protein Structure, Tertiary receptors Receptors, Interleukin-1 - chemistry Receptors, Interleukin-1 - metabolism Recombinant Proteins - pharmacology RNA, Messenger - genetics RNA, Messenger - metabolism Rodents tumor necrosis factor-alpha Tumor Necrosis Factor-alpha - metabolism |
| Title | Extracellular forms of IL-37 inhibit innate inflammation in vitro and in vivo but require the IL-1 family decoy receptor IL-1R8 |
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