ArticleMolecular medicine (Cambridge, Mass.)
Phosphorylation of extracellular signal-regulated kinase (ERK)-1/2 Is associated with the downregulation of peroxisome proliferator-activated receptor (PPAR)-γ during polymicrobial sepsis.
Article in Molecular medicine (Cambridge, Mass.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Dual host and pathogen targeting by MEK1/2 inhibitors.Infection and immunity · 2026Review
- Hyaluronan induces ERK activation with minimal transcriptomic changes in pancreatic α-cells.Biochemistry and biophysics reports · 2026Article
- Pioglitazone Reverses Alcohol-induced Human Immunodeficiency Virus (HIV) Replication and IL-1β Expression in Alveolar Macrophages.American journal of respiratory cell and molecular biology · 2025Article
- Unburned Tobacco Smoke Affects Neuroinflammation-Related Pathways in the Rat Mesolimbic System.International journal of molecular sciences · 2024Article
- Curcumin and saroglitazar attenuate diet-induced nonalcoholic steatohepatitis by activating the Nrf2 pathway and suppressing ERK1/2 signaling.Iranian journal of basic medical sciences · 2024Article
- Article
- Acetylated-PPARγ expression is regulated by differentCancer biology & medicine · 2023Article
- Article
- Antidepressant-like Effects of BDNF and NGF Individual Loop Dipeptide Mimetics Depend on the Signal Transmission Patterns Associated with Trk.Pharmaceuticals (Basel, Switzerland) · 2022Article
- PPAR Gamma: From Definition to Molecular Targets and Therapy of Lung Diseases.International journal of molecular sciences · 2021Review
- Peroxisome proliferator-activated receptor gamma as a theragnostic target for mesenchymal-type glioblastoma patients.Experimental & molecular medicine · 2020Article
- Article
- Peroxisome Proliferator Activated Receptor gamma (PPARγ) Agonist Rosiglitazone Ameliorate Airway Inflammation by Inhibiting Toll-Like Receptor 2 (TLR2)/Nod-Like Receptor with Pyrin Domain Containing 3 (NLRP3) Inflammatory Corpuscle Activation in Asthmatic Mice.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- DHA increases adiponectin expression more effectively than EPA at relative low concentrations by regulating PPARγ and its phosphorylation at Ser273 in 3T3-L1 adipocytes.Nutrition & metabolism · 2017Article
- Pharmacologic inhibition of MEK1/2 reduces lung inflammation without impairing bacterial clearance in experimentalPneumonia (Nathan Qld.) · 2017Article
- Activation of the peroxisome proliferator-activated receptor γ counteracts sepsis-induced T cell cytotoxicity toward alloantigenic target cells.Journal of molecular medicine (Berlin, Germany) · 2015Article
- Sesamol ameliorates hypotension by modulating cytokines and PPAR-gamma in systemic inflammatory response.EXCLI journal · 2015Article
- Rosiglitazone attenuates the metalloprotease/anti-metalloprotease imbalance in emphysema induced by cigarette smoke: involvement of extracellular signal-regulated kinase and NFκB signaling.International journal of chronic obstructive pulmonary disease · 2015Article
- Combined zinc supplementation with proinsulin C-peptide treatment decreases the inflammatory response and mortality in murine polymicrobial sepsis.Shock (Augusta, Ga.) · 2014Article
- Hypoxia downregulates PPARγ via an ERK1/2-NF-κB-Nox4-dependent mechanism in human pulmonary artery smooth muscle cells.Free radical biology & medicine · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Peroxisome proliferator-activated receptor (PPAR)-γ is a ligand-activated transcription factor and regulates inflammation. Posttranslational modifications regulate the function of PPARγ, potentially affecting inflammation. PPARγ contains a mitogen-activated protein kinase (MAPK) site, and phosphorylation by extracellular signal-regulated kinase (ERK)-1/2 leads to inhibition of PPARγ. This study investigated the kinetics of PPARγ expression and activation in parenchymal and immune cells in sepsis using the MAPK/ERK kinase (MEK)-1 inhibitor, an upstream kinase of ERK1/2. Adult male Sprague Dawley rats were subjected to polymicrobial sepsis by cecal ligation and puncture. Rats received intraperitoneal injection of vehicle or the MEK1 inhibitor PD98059 (5 mg/kg) 30 min before cecal ligation and puncture. Rats were euthanized at 0, 1, 3, 6 and 18 h after cecal ligation and puncture. Control animals used were animals at time 0 h. Lung, plasma and peripheral blood mononuclear cells (PBMCs) were collected for biochemical assays. In vehicle-treated rats, polymicrobial sepsis resulted in significant lung injury. In the lung and PBMCs, nuclear levels of PPARγ were decreased and associated with an increase in phosphorylated PPARγ and phosphorylated ERK1/2 levels. Treatment with the MEK1 inhibitor increased the antiinflammatory plasma adipokine adiponectin, restored PPARγ expression in PBMCs and lung, and decreased lung injury. The inflammatory effects of sepsis cause changes in PPARγ expression and activation, in part, because of phosphorylation of PPARγ by ERK1/2. This phosphorylation can be reversed by ERK1/2 inhibition, thereby improving lung injury.
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