PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation

Abstract Sepsis, severe sepsis and septic shock are the main cause of mortality in non-cardiac intensive care units. Immunometabolism has been linked to sepsis; however, the precise mechanism by which metabolic reprogramming regulates the inflammatory response is unclear. Here we show that aerobic g...

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Main Authors: Min Xie, Yan Yu, Rui Kang, Shan Zhu, Liangchun Yang, Ling Zeng, Xiaofang Sun, Minghua Yang, Timothy R. Billiar, Haichao Wang, Lizhi Cao, Jianxin Jiang, Daolin Tang
Format: Article
Language:English
Published: Nature Portfolio 2016-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms13280
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author Min Xie
Yan Yu
Rui Kang
Shan Zhu
Liangchun Yang
Ling Zeng
Xiaofang Sun
Minghua Yang
Timothy R. Billiar
Haichao Wang
Lizhi Cao
Jianxin Jiang
Daolin Tang
author_facet Min Xie
Yan Yu
Rui Kang
Shan Zhu
Liangchun Yang
Ling Zeng
Xiaofang Sun
Minghua Yang
Timothy R. Billiar
Haichao Wang
Lizhi Cao
Jianxin Jiang
Daolin Tang
author_sort Min Xie
collection DOAJ
description Abstract Sepsis, severe sepsis and septic shock are the main cause of mortality in non-cardiac intensive care units. Immunometabolism has been linked to sepsis; however, the precise mechanism by which metabolic reprogramming regulates the inflammatory response is unclear. Here we show that aerobic glycolysis contributes to sepsis by modulating inflammasome activation in macrophages. PKM2-mediated glycolysis promotes inflammasome activation by modulating EIF2AK2 phosphorylation in macrophages. Pharmacological and genetic inhibition of PKM2 or EIF2AK2 attenuates NLRP3 and AIM2 inflammasomes activation, and consequently suppresses the release of IL-1β, IL-18 and HMGB1 by macrophages. Pharmacological inhibition of the PKM2–EIF2AK2 pathway protects mice from lethal endotoxemia and polymicrobial sepsis. Moreover, conditional knockout of PKM2 in myeloid cells protects mice from septic death induced by NLRP3 and AIM2 inflammasome activation. These findings define an important role of PKM2 in immunometabolism and guide future development of therapeutic strategies to treat sepsis.
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institution Kabale University
issn 2041-1723
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series Nature Communications
spelling doaj-art-44e902eea61c43bbab9d4975480e57e92025-08-20T03:38:18ZengNature PortfolioNature Communications2041-17232016-10-017111310.1038/ncomms13280PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activationMin Xie0Yan Yu1Rui Kang2Shan Zhu3Liangchun Yang4Ling Zeng5Xiaofang Sun6Minghua Yang7Timothy R. Billiar8Haichao Wang9Lizhi Cao10Jianxin Jiang11Daolin Tang12Department of Pediatrics, Xiangya Hospital, Central South UniversityDepartment of Pediatrics, Xiangya Hospital, Central South UniversityDepartment of Surgery, University of PittsburghCenter of DAMP Biology, The Third Affiliated Hospital of Guangzhou Medical UniversityDepartment of Pediatrics, Xiangya Hospital, Central South UniversityDepartment of Surgery, University of PittsburghCenter of DAMP Biology, The Third Affiliated Hospital of Guangzhou Medical UniversityDepartment of Pediatrics, Xiangya Hospital, Central South UniversityDepartment of Surgery, University of PittsburghLaboratory of Emergency Medicine, The Feinstein Institute for Medical ResearchDepartment of Pediatrics, Xiangya Hospital, Central South UniversityState Key Laboratory of Trauma, Burns and Combined Injury, Research Institute of Surgery, Research institute for Traffic Medicine of People’s Liberation Army, Daping Hospital, Third Military Medical UniversityDepartment of Surgery, University of PittsburghAbstract Sepsis, severe sepsis and septic shock are the main cause of mortality in non-cardiac intensive care units. Immunometabolism has been linked to sepsis; however, the precise mechanism by which metabolic reprogramming regulates the inflammatory response is unclear. Here we show that aerobic glycolysis contributes to sepsis by modulating inflammasome activation in macrophages. PKM2-mediated glycolysis promotes inflammasome activation by modulating EIF2AK2 phosphorylation in macrophages. Pharmacological and genetic inhibition of PKM2 or EIF2AK2 attenuates NLRP3 and AIM2 inflammasomes activation, and consequently suppresses the release of IL-1β, IL-18 and HMGB1 by macrophages. Pharmacological inhibition of the PKM2–EIF2AK2 pathway protects mice from lethal endotoxemia and polymicrobial sepsis. Moreover, conditional knockout of PKM2 in myeloid cells protects mice from septic death induced by NLRP3 and AIM2 inflammasome activation. These findings define an important role of PKM2 in immunometabolism and guide future development of therapeutic strategies to treat sepsis.https://doi.org/10.1038/ncomms13280
spellingShingle Min Xie
Yan Yu
Rui Kang
Shan Zhu
Liangchun Yang
Ling Zeng
Xiaofang Sun
Minghua Yang
Timothy R. Billiar
Haichao Wang
Lizhi Cao
Jianxin Jiang
Daolin Tang
PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
Nature Communications
title PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
title_full PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
title_fullStr PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
title_full_unstemmed PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
title_short PKM2-dependent glycolysis promotes NLRP3 and AIM2 inflammasome activation
title_sort pkm2 dependent glycolysis promotes nlrp3 and aim2 inflammasome activation
url https://doi.org/10.1038/ncomms13280
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