Cathelicidin‐related antimicrobial peptide alleviates alcoholic liver disease through inhibiting inflammasome activation
Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol‐induced inflammasome activation...
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| Published in | The Journal of pathology Vol. 252; no. 4; pp. 371 - 383 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
01.12.2020
Wiley Subscription Services, Inc |
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| Abstract | Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol‐induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin‐related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout (Camp−/−) and wild‐type (WT) mice were subjected to binge‐on‐chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)‐1β levels. Although Camp−/− mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL‐1β in alcohol use disorder patients with ALD and were increased in Camp−/− mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL‐1β concentrations and rescued the liver from alcohol‐induced damage in both WT and Camp−/− mice. In summary, CRAMP exhibited a protective role against binge‐on‐chronic alcohol‐induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. © 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. |
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| AbstractList | Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol-induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin-related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout (Camp
) and wild-type (WT) mice were subjected to binge-on-chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)-1β levels. Although Camp
mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL-1β in alcohol use disorder patients with ALD and were increased in Camp
mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL-1β concentrations and rescued the liver from alcohol-induced damage in both WT and Camp
mice. In summary, CRAMP exhibited a protective role against binge-on-chronic alcohol-induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. © 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol‐induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin‐related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout ( Camp −/− ) and wild‐type (WT) mice were subjected to binge‐on‐chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)‐1β levels. Although Camp −/− mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL‐1β in alcohol use disorder patients with ALD and were increased in Camp −/− mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL‐1β concentrations and rescued the liver from alcohol‐induced damage in both WT and Camp −/− mice. In summary, CRAMP exhibited a protective role against binge‐on‐chronic alcohol‐induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. © 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol‐induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin‐related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout (Camp−/−) and wild‐type (WT) mice were subjected to binge‐on‐chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)‐1β levels. Although Camp−/− mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL‐1β in alcohol use disorder patients with ALD and were increased in Camp−/− mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL‐1β concentrations and rescued the liver from alcohol‐induced damage in both WT and Camp−/− mice. In summary, CRAMP exhibited a protective role against binge‐on‐chronic alcohol‐induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. © 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol-induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin-related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout ( Camp −/− ) and wild-type (WT) mice were subjected to binge-on-chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)-1β levels. Although Camp −/− mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL-1β in alcohol use disorder patients with ALD and were increased in Camp −/− mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL-1β concentrations and rescued the liver from alcohol-induced damage in both WT and Camp −/− mice. In summary, CRAMP exhibited a protective role against binge-on-chronic alcohol-induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol-induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin-related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout (Camp-/-) and wild-type (WT) mice were subjected to binge-on-chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)-1β levels. Although Camp-/- mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL-1β in alcohol use disorder patients with ALD and were increased in Camp-/- mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL-1β concentrations and rescued the liver from alcohol-induced damage in both WT and Camp-/- mice. In summary, CRAMP exhibited a protective role against binge-on-chronic alcohol-induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. © 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a critical role in the regulation of bacterial homeostasis in ALD, the functional role of AMPs in the alcohol-induced inflammasome activation is unclear. The aim of this study was to determine the effects of cathelicidin-related antimicrobial peptide (CRAMP) on inflammasome activation in ALD. CRAMP knockout (Camp-/-) and wild-type (WT) mice were subjected to binge-on-chronic alcohol feeding and synthetic CRAMP peptide was administered. Serum/plasma and hepatic tissue samples from human subjects with alcohol use disorder and/or alcoholic hepatitis were analyzed. CRAMP deficiency exacerbated ALD with enhanced inflammasome activation as shown by elevated serum interleukin (IL)-1β levels. Although Camp-/- mice had comparable serum endotoxin levels compared to WT mice after alcohol feeding, hepatic lipopolysaccharide (LPS) binding protein (LBP) and cluster of differentiation (CD) 14 were increased. Serum levels of uric acid (UA), a Signal 2 molecule in inflammasome activation, were positively correlated with serum levels of IL-1β in alcohol use disorder patients with ALD and were increased in Camp-/- mice fed alcohol. In vitro studies showed that CRAMP peptide inhibited LPS binding to macrophages and inflammasome activation stimulated by a combination of LPS and UA. Synthetic CRAMP peptide administration decreased serum UA and IL-1β concentrations and rescued the liver from alcohol-induced damage in both WT and Camp-/- mice. In summary, CRAMP exhibited a protective role against binge-on-chronic alcohol-induced liver damage via regulation of inflammasome activation by decreasing LPS binding and UA production. CRAMP administration may represent a novel strategy for treating ALD. © 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. |
| Author | Jiang, Mengwei Chen, Shao‐Yu Feng, Wenke Zhang, Lihua Puri, Puneet Li, Fengyuan McClain, Craig J Gillevet, Patrick M Zhao, Cuiqing Gu, Zelin Liu, Yunhuan Vatsalya, Vatsalya Shao, Tuo Barve, Shirish Gobejishvili, Leila Li, Huimin Deng, Zhong‐Bin |
| AuthorAffiliation | 1 Department of Pharmacology and Toxicology, University of Louisville, Louisville, KY, USA 5 Department of Biology, George Mason University, Manassas, VA, USA 7 McGuire VA Medical Center, Richmond, VA, USA 8 Alcohol Research Center, University of Louisville, Louisville, KY, USA 2 Department of Medicine, University of Louisville, Louisville, KY, USA 9 Hepatobiology & Toxicology Center, University of Louisville, Louisville, KY, USA 3 College of Animal Science and Technology, Key Lab of Preventive Veterinary Medicine in Jilin Province, Jilin Agricultural Science and Technology University, Jilin, PR China 6 Section of Gastroenterology, Hepatology and Nutrition, Virginia Commonwealth University, Richmond, VA, USA 4 School of Pharmaceutical Sciences, Jiujiang University, Jiujiang, PR China 10 Robley Rex VA Medical Center, Louisville, KY, USA |
| AuthorAffiliation_xml | – name: 5 Department of Biology, George Mason University, Manassas, VA, USA – name: 8 Alcohol Research Center, University of Louisville, Louisville, KY, USA – name: 10 Robley Rex VA Medical Center, Louisville, KY, USA – name: 6 Section of Gastroenterology, Hepatology and Nutrition, Virginia Commonwealth University, Richmond, VA, USA – name: 2 Department of Medicine, University of Louisville, Louisville, KY, USA – name: 7 McGuire VA Medical Center, Richmond, VA, USA – name: 4 School of Pharmaceutical Sciences, Jiujiang University, Jiujiang, PR China – name: 9 Hepatobiology & Toxicology Center, University of Louisville, Louisville, KY, USA – name: 1 Department of Pharmacology and Toxicology, University of Louisville, Louisville, KY, USA – name: 3 College of Animal Science and Technology, Key Lab of Preventive Veterinary Medicine in Jilin Province, Jilin Agricultural Science and Technology University, Jilin, PR China |
| Author_xml | – sequence: 1 givenname: Fengyuan surname: Li fullname: Li, Fengyuan organization: University of Louisville – sequence: 2 givenname: Cuiqing surname: Zhao fullname: Zhao, Cuiqing organization: Key Lab of Preventive Veterinary Medicine in Jilin Province, Jilin Agricultural Science and Technology University – sequence: 3 givenname: Tuo surname: Shao fullname: Shao, Tuo organization: University of Louisville – sequence: 4 givenname: Yunhuan surname: Liu fullname: Liu, Yunhuan organization: University of Louisville – sequence: 5 givenname: Zelin surname: Gu fullname: Gu, Zelin organization: University of Louisville – sequence: 6 givenname: Mengwei surname: Jiang fullname: Jiang, Mengwei organization: University of Louisville – sequence: 7 givenname: Huimin surname: Li fullname: Li, Huimin organization: Jiujiang University – sequence: 8 givenname: Lihua surname: Zhang fullname: Zhang, Lihua organization: University of Louisville – sequence: 9 givenname: Patrick M surname: Gillevet fullname: Gillevet, Patrick M organization: George Mason University – sequence: 10 givenname: Puneet surname: Puri fullname: Puri, Puneet organization: McGuire VA Medical Center – sequence: 11 givenname: Zhong‐Bin surname: Deng fullname: Deng, Zhong‐Bin organization: University of Louisville – sequence: 12 givenname: Shao‐Yu surname: Chen fullname: Chen, Shao‐Yu organization: University of Louisville – sequence: 13 givenname: Shirish surname: Barve fullname: Barve, Shirish organization: University of Louisville – sequence: 14 givenname: Leila surname: Gobejishvili fullname: Gobejishvili, Leila organization: University of Louisville – sequence: 15 givenname: Vatsalya surname: Vatsalya fullname: Vatsalya, Vatsalya organization: University of Louisville – sequence: 16 givenname: Craig J surname: McClain fullname: McClain, Craig J organization: Robley Rex VA Medical Center – sequence: 17 givenname: Wenke orcidid: 0000-0001-5456-5347 surname: Feng fullname: Feng, Wenke email: wenke.feng@louisville.edu organization: University of Louisville |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33245573$$D View this record in MEDLINE/PubMed |
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| Copyright | 2020 The Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd. Copyright © 2020 Pathological Society of Great Britain and Ireland |
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| Keywords | IL‐1β ALD CRAMP uric acid LPS |
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| Notes | No conflicts of interest were declared. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Author contributions statement FL performed the experiments, analyzed and interpreted data, and drafted the manuscript. CZ, TS, YL, ZG, MJ, HL and LZ provided technical support and performed the experiments. PMG and PP helped with fecal microbiota analysis. LG and VV provided patient data and performed analyses. Z-BD, S-YC and SB contributed to the critical discussion of the study. CJM contributed to conceiving the study and critical revision of the manuscript. WF conceived, designed, and supervised the study, and wrote and critically revised the manuscript. |
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| Snippet | Alcoholic liver disease (ALD) is associated with gut dysbiosis and hepatic inflammasome activation. While it is known that antimicrobial peptides (AMPs) play a... |
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| SubjectTerms | Alcohol use ALD Animals Antimicrobial agents Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - metabolism Antimicrobial peptides Biomarkers - blood Cell activation CRAMP Dysbacteriosis Dysbiosis - genetics Dysbiosis - metabolism Dysbiosis - pathology Hepatitis Homeostasis Humans IL‐1β Inflammasomes Inflammasomes - genetics Inflammasomes - metabolism Interleukin-1beta - blood Lipopolysaccharides Liver - metabolism Liver - pathology Liver diseases Liver Diseases, Alcoholic - genetics Liver Diseases, Alcoholic - metabolism Liver Diseases, Alcoholic - pathology LPS Macrophages Male Mice Mice, Knockout Oxidative Stress - genetics Peptides Serum levels Uric acid Uric Acid - blood |
| Title | Cathelicidin‐related antimicrobial peptide alleviates alcoholic liver disease through inhibiting inflammasome activation |
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