Anakinra restores cellular proteostasis by coupling mitochondrial redox balance to autophagy
Autophagy selectively degrades aggregation-prone misfolded proteins caused by defective cellular proteostasis. However, the complexity of autophagy may prevent the full appreciation of how its modulation could be used as a therapeutic strategy in disease management. Here, we define a molecular pathw...
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| Veröffentlicht in: | The Journal of clinical investigation 2022-01, Vol.132 (2), p.0_1-16 |
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| creator | van de Veerdonk, Frank L Renga, Giorgia Pariano, Marilena Bellet, Marina M Servillo, Giuseppe Fallarino, Francesca De Luca, Antonella Iannitti, Rossana G Piobbico, Danilo Gargaro, Marco Manni, Giorgia D'Onofrio, Fiorella Stincardini, Claudia Sforna, Luigi Borghi, Monica Castelli, Marilena Pieroni, Stefania Oikonomou, Vasileios Villella, Valeria R Puccetti, Matteo Giovagnoli, Stefano Galarini, Roberta Barola, Carolina Maiuri, Luigi Fazia, Maria Agnese Della Cellini, Barbara Talesa, Vincenzo Nicola Dinarello, Charles A Costantini, Claudio Romani, Luigina |
| description | Autophagy selectively degrades aggregation-prone misfolded proteins caused by defective cellular proteostasis. However, the complexity of autophagy may prevent the full appreciation of how its modulation could be used as a therapeutic strategy in disease management. Here, we define a molecular pathway through which recombinant IL-1 receptor antagonist (IL-1Ra, anakinra) affects cellular proteostasis independently from the IL-1 receptor (IL-1R1). Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activated NADPH oxidase 4 independent of the IL-1R1. By coupling the mitochondrial redox balance to autophagy, anakinra improved the dysregulated proteostasis network in murine and human cystic fibrosis. We anticipate that anakinra may represent a therapeutic option in addition to its IL-1R1-dependent antiinflammatory properties by acting at the intersection of mitochondrial oxidative stress and autophagy with the capacity to restore conditions in which defective proteostasis leads to human disease. |
| doi_str_mv | 10.1172/JCM44983 |
| format | Article |
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However, the complexity of autophagy may prevent the full appreciation of how its modulation could be used as a therapeutic strategy in disease management. Here, we define a molecular pathway through which recombinant IL-1 receptor antagonist (IL-1Ra, anakinra) affects cellular proteostasis independently from the IL-1 receptor (IL-1R1). Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activated NADPH oxidase 4 independent of the IL-1R1. By coupling the mitochondrial redox balance to autophagy, anakinra improved the dysregulated proteostasis network in murine and human cystic fibrosis. We anticipate that anakinra may represent a therapeutic option in addition to its IL-1R1-dependent antiinflammatory properties by acting at the intersection of mitochondrial oxidative stress and autophagy with the capacity to restore conditions in which defective proteostasis leads to human disease.</description><identifier>ISSN: 0021-9738</identifier><identifier>EISSN: 1558-8238</identifier><identifier>DOI: 10.1172/JCM44983</identifier><language>eng</language><publisher>Ann Arbor: American Society for Clinical Investigation</publisher><subject>Anti-inflammatory agents ; Autophagy ; Binding sites ; Biomedical research ; Cystic fibrosis ; Disease management ; Gene expression ; Hydrocarbons ; Hydrogen peroxide ; Inflammation ; Interleukin 1 ; Interleukin 1 receptor antagonist ; Lung diseases ; Mitochondria ; Mutation ; NAD(P)H oxidase ; Oxidative stress ; Pathogenesis ; Protein folding ; Proteins ; Transcription ; Tryptophan 2,3-dioxygenase</subject><ispartof>The Journal of clinical investigation, 2022-01, Vol.132 (2), p.0_1-16</ispartof><rights>Copyright American Society for Clinical Investigation Jan 2022</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,864,27924,27925</link.rule.ids></links><search><creatorcontrib>van de Veerdonk, Frank L</creatorcontrib><creatorcontrib>Renga, Giorgia</creatorcontrib><creatorcontrib>Pariano, Marilena</creatorcontrib><creatorcontrib>Bellet, Marina M</creatorcontrib><creatorcontrib>Servillo, Giuseppe</creatorcontrib><creatorcontrib>Fallarino, Francesca</creatorcontrib><creatorcontrib>De Luca, Antonella</creatorcontrib><creatorcontrib>Iannitti, Rossana G</creatorcontrib><creatorcontrib>Piobbico, Danilo</creatorcontrib><creatorcontrib>Gargaro, Marco</creatorcontrib><creatorcontrib>Manni, Giorgia</creatorcontrib><creatorcontrib>D'Onofrio, Fiorella</creatorcontrib><creatorcontrib>Stincardini, Claudia</creatorcontrib><creatorcontrib>Sforna, Luigi</creatorcontrib><creatorcontrib>Borghi, Monica</creatorcontrib><creatorcontrib>Castelli, Marilena</creatorcontrib><creatorcontrib>Pieroni, Stefania</creatorcontrib><creatorcontrib>Oikonomou, Vasileios</creatorcontrib><creatorcontrib>Villella, Valeria R</creatorcontrib><creatorcontrib>Puccetti, Matteo</creatorcontrib><creatorcontrib>Giovagnoli, Stefano</creatorcontrib><creatorcontrib>Galarini, Roberta</creatorcontrib><creatorcontrib>Barola, Carolina</creatorcontrib><creatorcontrib>Maiuri, Luigi</creatorcontrib><creatorcontrib>Fazia, Maria Agnese Della</creatorcontrib><creatorcontrib>Cellini, Barbara</creatorcontrib><creatorcontrib>Talesa, Vincenzo Nicola</creatorcontrib><creatorcontrib>Dinarello, Charles A</creatorcontrib><creatorcontrib>Costantini, Claudio</creatorcontrib><creatorcontrib>Romani, Luigina</creatorcontrib><title>Anakinra restores cellular proteostasis by coupling mitochondrial redox balance to autophagy</title><title>The Journal of clinical investigation</title><description>Autophagy selectively degrades aggregation-prone misfolded proteins caused by defective cellular proteostasis. However, the complexity of autophagy may prevent the full appreciation of how its modulation could be used as a therapeutic strategy in disease management. Here, we define a molecular pathway through which recombinant IL-1 receptor antagonist (IL-1Ra, anakinra) affects cellular proteostasis independently from the IL-1 receptor (IL-1R1). Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activated NADPH oxidase 4 independent of the IL-1R1. By coupling the mitochondrial redox balance to autophagy, anakinra improved the dysregulated proteostasis network in murine and human cystic fibrosis. We anticipate that anakinra may represent a therapeutic option in addition to its IL-1R1-dependent antiinflammatory properties by acting at the intersection of mitochondrial oxidative stress and autophagy with the capacity to restore conditions in which defective proteostasis leads to human disease.</description><subject>Anti-inflammatory agents</subject><subject>Autophagy</subject><subject>Binding sites</subject><subject>Biomedical research</subject><subject>Cystic fibrosis</subject><subject>Disease management</subject><subject>Gene expression</subject><subject>Hydrocarbons</subject><subject>Hydrogen peroxide</subject><subject>Inflammation</subject><subject>Interleukin 1</subject><subject>Interleukin 1 receptor antagonist</subject><subject>Lung diseases</subject><subject>Mitochondria</subject><subject>Mutation</subject><subject>NAD(P)H oxidase</subject><subject>Oxidative stress</subject><subject>Pathogenesis</subject><subject>Protein 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Carolina</au><au>Maiuri, Luigi</au><au>Fazia, Maria Agnese Della</au><au>Cellini, Barbara</au><au>Talesa, Vincenzo Nicola</au><au>Dinarello, Charles A</au><au>Costantini, Claudio</au><au>Romani, Luigina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anakinra restores cellular proteostasis by coupling mitochondrial redox balance to autophagy</atitle><jtitle>The Journal of clinical investigation</jtitle><date>2022-01-01</date><risdate>2022</risdate><volume>132</volume><issue>2</issue><spage>0_1</spage><epage>16</epage><pages>0_1-16</pages><issn>0021-9738</issn><eissn>1558-8238</eissn><abstract>Autophagy selectively degrades aggregation-prone misfolded proteins caused by defective cellular proteostasis. However, the complexity of autophagy may prevent the full appreciation of how its modulation could be used as a therapeutic strategy in disease management. Here, we define a molecular pathway through which recombinant IL-1 receptor antagonist (IL-1Ra, anakinra) affects cellular proteostasis independently from the IL-1 receptor (IL-1R1). Anakinra promoted H2O2-driven autophagy through a xenobiotic sensing pathway involving the aryl hydrocarbon receptor that, activated through the indoleamine 2,3-dioxygenase 1-kynurenine pathway, transcriptionally activated NADPH oxidase 4 independent of the IL-1R1. By coupling the mitochondrial redox balance to autophagy, anakinra improved the dysregulated proteostasis network in murine and human cystic fibrosis. We anticipate that anakinra may represent a therapeutic option in addition to its IL-1R1-dependent antiinflammatory properties by acting at the intersection of mitochondrial oxidative stress and autophagy with the capacity to restore conditions in which defective proteostasis leads to human disease.</abstract><cop>Ann Arbor</cop><pub>American Society for Clinical Investigation</pub><doi>10.1172/JCM44983</doi></addata></record> |
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| subjects | Anti-inflammatory agents Autophagy Binding sites Biomedical research Cystic fibrosis Disease management Gene expression Hydrocarbons Hydrogen peroxide Inflammation Interleukin 1 Interleukin 1 receptor antagonist Lung diseases Mitochondria Mutation NAD(P)H oxidase Oxidative stress Pathogenesis Protein folding Proteins Transcription Tryptophan 2,3-dioxygenase |
| title | Anakinra restores cellular proteostasis by coupling mitochondrial redox balance to autophagy |
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