MARCH1 E3 Ubiquitin Ligase Dampens the Innate Inflammatory Response by Modulating Monocyte Functions in Mice

Ubiquitination was recently identified as a central process in the pathogenesis and development of numerous inflammatory diseases, such as obesity, atherosclerosis, and asthma. Treatment with proteasomal inhibitors led to severe side effects because ubiquitination is heavily involved in a plethora o...

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Veröffentlicht in:The Journal of immunology (1950) 2017-01, Vol.198 (2), p.852-861
Hauptverfasser: Galbas, Tristan, Raymond, Maxime, Sabourin, Antoine, Bourgeois-Daigneault, Marie-Claude, Guimont-Desrochers, Fanny, Yun, Tae Jin, Cailhier, Jean-François, Ishido, Satoshi, Lesage, Sylvie, Cheong, Cheolho, Thibodeau, Jacques
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container_title The Journal of immunology (1950)
container_volume 198
creator Galbas, Tristan
Raymond, Maxime
Sabourin, Antoine
Bourgeois-Daigneault, Marie-Claude
Guimont-Desrochers, Fanny
Yun, Tae Jin
Cailhier, Jean-François
Ishido, Satoshi
Lesage, Sylvie
Cheong, Cheolho
Thibodeau, Jacques
description Ubiquitination was recently identified as a central process in the pathogenesis and development of numerous inflammatory diseases, such as obesity, atherosclerosis, and asthma. Treatment with proteasomal inhibitors led to severe side effects because ubiquitination is heavily involved in a plethora of cellular functions. Thus, new players regulating ubiquitination processes must be identified to improve therapies for inflammatory diseases. In addition to their role in adaptive immunity, endosomal MHC class II (MHCII) molecules were shown to modulate innate immune responses by fine tuning the TLR4 signaling pathway. However, the role of MHCII ubiquitination by membrane associated ring-CH-type finger 1 (MARCH1) E3 ubiquitin ligase in this process remains to be assessed. In this article, we demonstrate that MARCH1 is a key inhibitor of innate inflammation in response to bacterial endotoxins. The higher mortality of March1 mice challenged with a lethal dose of LPS was associated with significantly stronger systemic production of proinflammatory cytokines and splenic NK cell activation; however, we did not find evidence that MARCH1 modulates LPS or IL-10 signaling pathways. Instead, the mechanism by which MARCH1 protects against endotoxic shock rests on its capacity to promote the transition of monocytes from Ly6C to Ly6C Moreover, in competitive bone marrow chimeras, March1 monocytes and polymorphonuclear neutrophils outcompeted wild-type cells with regard to bone marrow egress and homing to peripheral organs. We conclude that MARCH1 exerts MHCII-independent effects that regulate the innate arm of immunity. Thus, MARCH1 might represent a potential new target for emerging therapies based on ubiquitination reactions in inflammatory diseases.
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Treatment with proteasomal inhibitors led to severe side effects because ubiquitination is heavily involved in a plethora of cellular functions. Thus, new players regulating ubiquitination processes must be identified to improve therapies for inflammatory diseases. In addition to their role in adaptive immunity, endosomal MHC class II (MHCII) molecules were shown to modulate innate immune responses by fine tuning the TLR4 signaling pathway. However, the role of MHCII ubiquitination by membrane associated ring-CH-type finger 1 (MARCH1) E3 ubiquitin ligase in this process remains to be assessed. In this article, we demonstrate that MARCH1 is a key inhibitor of innate inflammation in response to bacterial endotoxins. 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Raymond, Maxime ; Sabourin, Antoine ; Bourgeois-Daigneault, Marie-Claude ; Guimont-Desrochers, Fanny ; Yun, Tae Jin ; Cailhier, Jean-François ; Ishido, Satoshi ; Lesage, Sylvie ; Cheong, Cheolho ; Thibodeau, Jacques</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c468t-b2717a4fdbb7e1b94030dd6ee3355a9e6a4419c0950917e7261a49b1c8321f953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Adaptive immunity</topic><topic>Animals</topic><topic>Arteriosclerosis</topic><topic>Asthma</topic><topic>Bacteria</topic><topic>Bone marrow</topic><topic>Cell activation</topic><topic>Chimeras</topic><topic>Disease Models, Animal</topic><topic>Egress</topic><topic>Endotoxemia</topic><topic>Endotoxemia - immunology</topic><topic>Endotoxins</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Flow Cytometry</topic><topic>Histocompatibility Antigens Class II - immunology</topic><topic>Homing</topic><topic>Immune response</topic><topic>Immunity, Innate - immunology</topic><topic>Inflammation - immunology</topic><topic>Inflammatory diseases</topic><topic>Inflammatory response</topic><topic>Innate immunity</topic><topic>Interleukin 10</topic><topic>Lethal dose</topic><topic>Leukocytes (neutrophilic)</topic><topic>Leukocytes (polymorphonuclear)</topic><topic>Lipopolysaccharides</topic><topic>Lipopolysaccharides - immunology</topic><topic>Lymphocyte Activation - immunology</topic><topic>Major histocompatibility complex</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Monocytes</topic><topic>Monocytes - immunology</topic><topic>Natural killer cells</topic><topic>Organs</topic><topic>Proteasomes</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>Rodents</topic><topic>Shock</topic><topic>Signal transduction</topic><topic>Spleen</topic><topic>TLR4 protein</topic><topic>Toll-like receptors</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitin-Protein Ligases - immunology</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Galbas, Tristan</creatorcontrib><creatorcontrib>Raymond, Maxime</creatorcontrib><creatorcontrib>Sabourin, Antoine</creatorcontrib><creatorcontrib>Bourgeois-Daigneault, Marie-Claude</creatorcontrib><creatorcontrib>Guimont-Desrochers, Fanny</creatorcontrib><creatorcontrib>Yun, Tae Jin</creatorcontrib><creatorcontrib>Cailhier, Jean-François</creatorcontrib><creatorcontrib>Ishido, Satoshi</creatorcontrib><creatorcontrib>Lesage, Sylvie</creatorcontrib><creatorcontrib>Cheong, Cheolho</creatorcontrib><creatorcontrib>Thibodeau, Jacques</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium &amp; 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subjects Adaptive immunity
Animals
Arteriosclerosis
Asthma
Bacteria
Bone marrow
Cell activation
Chimeras
Disease Models, Animal
Egress
Endotoxemia
Endotoxemia - immunology
Endotoxins
Enzyme-Linked Immunosorbent Assay
Flow Cytometry
Histocompatibility Antigens Class II - immunology
Homing
Immune response
Immunity, Innate - immunology
Inflammation - immunology
Inflammatory diseases
Inflammatory response
Innate immunity
Interleukin 10
Lethal dose
Leukocytes (neutrophilic)
Leukocytes (polymorphonuclear)
Lipopolysaccharides
Lipopolysaccharides - immunology
Lymphocyte Activation - immunology
Major histocompatibility complex
Mice
Mice, Inbred C57BL
Mice, Knockout
Monocytes
Monocytes - immunology
Natural killer cells
Organs
Proteasomes
Real-Time Polymerase Chain Reaction
Rodents
Shock
Signal transduction
Spleen
TLR4 protein
Toll-like receptors
Ubiquitin-protein ligase
Ubiquitin-Protein Ligases - immunology
Ubiquitination
title MARCH1 E3 Ubiquitin Ligase Dampens the Innate Inflammatory Response by Modulating Monocyte Functions in Mice
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