Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2

Ulcerative colitis is an idiopathic, chronic inflammatory bowel disease. Its pathogenesis is multifactorial involving inflammation and immune dysregulation. Proinflammatory TNFα/NFκB signaling is believed to play a cardinal role in ulcerative colitis. Growing evidence indicates the molecular interac...

Full description

Saved in:
Bibliographic Details
Main Authors: Sadaf Hasan, Nabil Ghani, Xiangli Zhao, Julia Good, Chuan-ju Liu
Format: Article
Language:English
Published: KeAi Communications Co., Ltd. 2025-09-01
Series:Genes and Diseases
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2352304225000601
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1849710160753197056
author Sadaf Hasan
Nabil Ghani
Xiangli Zhao
Julia Good
Chuan-ju Liu
author_facet Sadaf Hasan
Nabil Ghani
Xiangli Zhao
Julia Good
Chuan-ju Liu
author_sort Sadaf Hasan
collection DOAJ
description Ulcerative colitis is an idiopathic, chronic inflammatory bowel disease. Its pathogenesis is multifactorial involving inflammation and immune dysregulation. Proinflammatory TNFα/NFκB signaling is believed to play a cardinal role in ulcerative colitis. Growing evidence indicates the molecular interactions between the cellular metabolites and different phases of inflammation. This study aims to identify the metabolites that can inhibit TNFα/NFκB signaling and are potentially therapeutic against various TNFα-associated inflammatory diseases, particularly inflammatory bowel diseases. We performed in vitro and in vivo screening of cellular metabolites to inhibit TNFα/NFκB signaling. Multiple confirmation assays, including NFκB translocation, quantitative real-time PCR, ELISA, immunofluorescence staining, and RNA sequencing analysis were executed. Drug affinity-responsive target stability assay with proteomics was utilized for target identification. cPLA2 ablated mice with dextran sodium sulfate-induced colitis were employed to assess pyruvate's dependence on its molecular target in attenuating ulcerative colitis pathogenesis. Metabolite screening and subsequent validation with multiple approaches led to the isolation of pyruvate, a glycolytic metabolite, and a critical node in several metabolic pathways, as a novel inhibitor of TNFα/NFκB signaling. Importantly, pyruvate suppressed inflammation, preserved colonic histology, maintained tight junction proteins, and regulated permeability in the ulcerative colitis model. Additionally, cPLA2 was identified as a previously unknown target of pyruvate and pyruvate largely lost its therapeutic effects against ulcerative colitis in cPLA2-deficient mice. Conclusively, this study not only unveils pyruvate as an antagonist of TNFα/NFκB signaling and therapeutic intervention against colitis but also provides mechanistic insight into the mode of action of pyruvate.
format Article
id doaj-art-81bbbb51bd1842f58e217b7704ce7291
institution DOAJ
issn 2352-3042
language English
publishDate 2025-09-01
publisher KeAi Communications Co., Ltd.
record_format Article
series Genes and Diseases
spelling doaj-art-81bbbb51bd1842f58e217b7704ce72912025-08-20T03:15:02ZengKeAi Communications Co., Ltd.Genes and Diseases2352-30422025-09-0112510157110.1016/j.gendis.2025.101571Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2Sadaf Hasan0Nabil Ghani1Xiangli Zhao2Julia Good3Chuan-ju Liu4Department of Orthopedic Surgery, New York University Grossman School of Medicine, New York, NY 10010, USADepartment of Medicine, Division of Internal Medicine, Saint Peter's University Hospital, Rutgers University, New Brunswick, NJ 08901, USADepartment of Orthopedic Surgery, New York University Grossman School of Medicine, New York, NY 10010, USA; Department of Orthopedics & Rehabilitation, Yale School of Medicine, New Haven, CT 06510, USADepartment of Orthopedic Surgery, New York University Grossman School of Medicine, New York, NY 10010, USADepartment of Orthopedic Surgery, New York University Grossman School of Medicine, New York, NY 10010, USA; Department of Cell Biology, New York University Grossman School of Medicine, New York, NY 10010, USA; Department of Orthopedics & Rehabilitation, Yale School of Medicine, New Haven, CT 06510, USA; Corresponding author. Department of Orthopedics & Rehabilitation, Yale School of Medicine, New Haven, CT06510, USA. Tel.: 203-785-5968.Ulcerative colitis is an idiopathic, chronic inflammatory bowel disease. Its pathogenesis is multifactorial involving inflammation and immune dysregulation. Proinflammatory TNFα/NFκB signaling is believed to play a cardinal role in ulcerative colitis. Growing evidence indicates the molecular interactions between the cellular metabolites and different phases of inflammation. This study aims to identify the metabolites that can inhibit TNFα/NFκB signaling and are potentially therapeutic against various TNFα-associated inflammatory diseases, particularly inflammatory bowel diseases. We performed in vitro and in vivo screening of cellular metabolites to inhibit TNFα/NFκB signaling. Multiple confirmation assays, including NFκB translocation, quantitative real-time PCR, ELISA, immunofluorescence staining, and RNA sequencing analysis were executed. Drug affinity-responsive target stability assay with proteomics was utilized for target identification. cPLA2 ablated mice with dextran sodium sulfate-induced colitis were employed to assess pyruvate's dependence on its molecular target in attenuating ulcerative colitis pathogenesis. Metabolite screening and subsequent validation with multiple approaches led to the isolation of pyruvate, a glycolytic metabolite, and a critical node in several metabolic pathways, as a novel inhibitor of TNFα/NFκB signaling. Importantly, pyruvate suppressed inflammation, preserved colonic histology, maintained tight junction proteins, and regulated permeability in the ulcerative colitis model. Additionally, cPLA2 was identified as a previously unknown target of pyruvate and pyruvate largely lost its therapeutic effects against ulcerative colitis in cPLA2-deficient mice. Conclusively, this study not only unveils pyruvate as an antagonist of TNFα/NFκB signaling and therapeutic intervention against colitis but also provides mechanistic insight into the mode of action of pyruvate.http://www.sciencedirect.com/science/article/pii/S2352304225000601ColitisCytosolic phospholipase A2Drug affinity-responsive target stability assayInflammationPyruvateTNFα/NFκB signaling
spellingShingle Sadaf Hasan
Nabil Ghani
Xiangli Zhao
Julia Good
Chuan-ju Liu
Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2
Genes and Diseases
Colitis
Cytosolic phospholipase A2
Drug affinity-responsive target stability assay
Inflammation
Pyruvate
TNFα/NFκB signaling
title Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2
title_full Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2
title_fullStr Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2
title_full_unstemmed Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2
title_short Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2
title_sort exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase a2
topic Colitis
Cytosolic phospholipase A2
Drug affinity-responsive target stability assay
Inflammation
Pyruvate
TNFα/NFκB signaling
url http://www.sciencedirect.com/science/article/pii/S2352304225000601
work_keys_str_mv AT sadafhasan exogenouspyruvateistherapeuticagainstcolitisbytargetingcytosolicphospholipasea2
AT nabilghani exogenouspyruvateistherapeuticagainstcolitisbytargetingcytosolicphospholipasea2
AT xianglizhao exogenouspyruvateistherapeuticagainstcolitisbytargetingcytosolicphospholipasea2
AT juliagood exogenouspyruvateistherapeuticagainstcolitisbytargetingcytosolicphospholipasea2
AT chuanjuliu exogenouspyruvateistherapeuticagainstcolitisbytargetingcytosolicphospholipasea2