Ppars are a unique set of fatty acid regulated transcription factors controlling both lipid metabolism and inflammation

Varga, Tamas; Czimmerer, Zsolt; Nagy, Laszlo

doi:10.1016/j.bbadis.2011.02.014

Cited by 933Peroxisome Proliferator-Activated ReceptorsFatty Acid Research and HealthCholesterol and Lipid Metabolism

Ppars are a unique set of fatty acid regulated transcription factors controlling both lipid metabolism and inflammation

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Varga, Tamas, Czimmerer, Zsolt, Nagy, Laszlo·2011·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

DOI 10.1016/j.bbadis.2011.02.014PMC PMC3117990

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Abstract

Cells are constantly exposed to a large variety of lipids. Traditionally, these molecules were thought to serve as simple energy storing molecules. More recently it has been realized that they can also initiate and regulate signaling events that will decisively influence development, cellular differentiation, metabolism and related functions through the regulation of gene expression. Multicellular organisms dedicate a large family of nuclear receptors to these tasks. These proteins combine the defining features of both transcription factors and receptor molecules, and therefore have the unique ability of being able to bind lipid signaling molecules and transduce the appropriate signals derived from lipid environment to the level of gene expression. Intriguingly, the members of a subfamily of the nuclear receptors, the peroxisome proliferator-activated receptors (PPARs) are able to sense and interpret fatty acid signals derived from dietary lipids, pathogenic lipoproteins or essential fatty acid metabolites. Not surprisingly, Peroxisome proliferator-activated receptors were found to be key regulators of lipid and carbohydrate metabolism. Unexpectedly, later studies revealed that Peroxisome proliferator-activated receptors are also able to modulate inflammatory responses. Here we summarize our understanding on how these transcription factors/receptors connect lipid metabolism to inflammation and some of the novel regulatory mechanisms by which they contribute to homeostasis and certain pathological conditions. This article is part of a Special Issue entitled: Translating nuclear receptors from health to disease.

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Upon ligand binding, the corepressor complex is replaced by coactivators, resulting in transcription of PPAR target genes.
“Upon ligand binding, the corepressor complex is replaced by coactivators, resulting in the transcription of PPAR target genes.”
From The Peroxisome Proliferator–Activated Receptor (PPAR)-γ Antagonist 2-Chloro-5-Nitro-N-Phenylbenzamide (GW9662) Triggers Perilipin 2 Expression via PPARδ and Induces Lipogenesis and Triglyceride Accumulation in Human THP-1 Macrophages (2020) · cites this paper as Varga et al., 2011
In “Mechanisms of PPARγ mediated gene regulation” (page unavailable), the paper describes liganded PPARγ/RXR recruiting coactivators and usually upregulating target genes. It does not say that ligand binding replaces a corepressor complex with those coactivators; the corepressor-replacement step is unsupported. (LLM, conf=0.86)
Experimental — accuracy not yet measured
In the absence of ligands, the PPAR-RXR heterodimer binds to the PPAR response element in the promoter of target genes, binds a corepressor complex, and represses transcription.
“In the absence of ligands, the heterodimer is bound to the so-called PPAR response element in the promoter of target genes.In this state, the heterodimer binds a corepressor complex and represses the transcription of target genes.”
From The Peroxisome Proliferator–Activated Receptor (PPAR)-γ Antagonist 2-Chloro-5-Nitro-N-Phenylbenzamide (GW9662) Triggers Perilipin 2 Expression via PPARδ and Induces Lipogenesis and Triglyceride Accumulation in Human THP-1 Macrophages (2020) · cites this paper as Varga et al., 2011
The Introduction’s “DNA recognition by PPARs” section says PPAR–RXR heterodimers bind PPAR response elements, but describes binding in its simplified model as occurring upon ligand binding. The “Mechanisms of PPARγ mediated gene regulation” section discusses a repressor complex in a different mechanism involving ligand-bound PPARγ, not an unliganded PPAR–RXR heterodimer bound to a PPRE. Our copy therefore does not support the claimed ligand-free corepressor mechanism. (LLM, conf=0.86)
Experimental — accuracy not yet measured
As transcription factors, PPARs regulate various genes implicated in lipid and glucose metabolism, inflammation, proliferation, and differentiation.
“As transcription factors, PPARs regulate various genes implicated in lipid and glucose metabolism, inflammation, proliferation, and differentiation (Varga et al., 2011;Vrablík and Ce ska, 2015).”
From The Peroxisome Proliferator–Activated Receptor (PPAR)-γ Antagonist 2-Chloro-5-Nitro-N-Phenylbenzamide (GW9662) Triggers Perilipin 2 Expression via PPARδ and Induces Lipogenesis and Triglyceride Accumulation in Human THP-1 Macrophages (2020) · cites this paper as Varga et al., 2011
The most common model for PPAR-dependent gene regulation is direct transcriptional regulation by heterodimerization of a PPAR isoform with retinoid X receptors.
“The most common model for PPAR-dependent gene regulation is the direct transcriptional regulation by heterodimerization of a PPAR isoform with retinoid X receptors.”
From The Peroxisome Proliferator–Activated Receptor (PPAR)-γ Antagonist 2-Chloro-5-Nitro-N-Phenylbenzamide (GW9662) Triggers Perilipin 2 Expression via PPARδ and Induces Lipogenesis and Triglyceride Accumulation in Human THP-1 Macrophages (2020) · cites this paper as Varga et al., 2011
PPARs are critical regulators of genes involved in development, lipid and carbohydrate metabolism, and inflammation.
“PPARs are also critical regulators of genes that are involved in development, metabolism of lipids and carbohydrates, as well as inflammation [85].”
From Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration (2018) · cites this paper as [85]

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Alternative activation is an innate response to injury that requires CD4+ T cells to be sustained during chronic infection
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Peroxisome proliferator–activated receptor (PPAR)α expression in T cells mediates gender differences in development of T cell–mediated autoimmunity
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PPARδ-mediated antiinflammatory mechanisms inhibit angiotensin II-accelerated atherosclerosis
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Peroxisome proliferator activated receptor γ in colonic epithelial cells protects against experimental inflammatory bowel disease
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Peroxisome Proliferator-Activated Receptor α Agonists as Therapy for Autoimmune Disease
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Dendritic Cell Immunogenicity Is Regulated by Peroxisome Proliferator-Activated Receptor γ
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PPARδ regulates multiple proinflammatory pathways to suppress atherosclerosis
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Non-DNA binding, dominant-negative, human PPARγ mutations cause lipodystrophic insulin resistance
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Peroxisome Proliferator-activated Receptor γ-regulated ABCG2 Expression Confers Cytoprotection to Human Dendritic Cells
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Conditional Knockout of Macrophage PPARγIncreases Atherosclerosis in C57BL/6 and Low-Density Lipoprotein Receptor–Deficient Mice
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Hypotension, lipodystrophy, and insulin resistance in generalized PPARγ-deficient mice rescued from embryonic lethality
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Nuclear Receptor Peroxisome Proliferator-activated Receptor α (PPARα) Is Expressed in Resting Murine Lymphocytes
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Identification of Two mPPAR Related Receptors and Evidence for the Existence of Five Subfamily Members
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Activation of PPARγ Specifies a Dendritic Cell Subtype Capable of Enhanced Induction of iNKT Cell Expansion
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Arginase I Induction by Modified Lipoproteins in Macrophages: A Peroxisome Proliferator-Activated Receptor-γ/δ-Mediated Effect that Links Lipid Metabolism and Immunity
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Induction of oral tolerance to cellular immune responses in the absence of Peyer's patches
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Targeted Elimination of Peroxisome Proliferator-Activated Receptor γ in β Cells Leads to Abnormalities in Islet Mass without Compromising Glucose Homeostasis
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Acute Intracerebroventricular Administration of Palmitoylethanolamide, an Endogenous Peroxisome Proliferator-Activated Receptor-α Agonist, Modulates Carrageenan-Induced Paw Edema in Mice
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Evaluation of Selected Hypolipidemic Agents for the Induction of Peroxisomal Enzymes and Peroxisome Proliferation in the Rat Liver
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Peroxisome proliferator-activated receptor-γ haploinsufficiency enhances B cell proliferative responses and exacerbates experimentally induced arthritis
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Fenofibrate Represses Interleukin-17 and Interferon-γ Expression and Improves Colitis in Interleukin-10–Deficient Mice
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Human B Lymphocytes and B Lymphomas Express PPAR-γ and Are Killed by PPAR-γ Agonists
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F4/80+ Alternatively Activated Macrophages Control CD4+ T Cell Hyporesponsiveness at Sites Peripheral to Filarial Infection
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PPARα blocks glucocorticoid receptor α-mediated transactivation but cooperates with the activated glucocorticoid receptor α for transrepression on NF-κB
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PPARγ in Placental Angiogenesis
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Peroxisome Proliferator-Activated Receptor-γ-Deficient Heterozygous Mice Develop an Exacerbated Neural Antigen-Induced Th1 Response and Experimental Allergic Encephalomyelitis
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The role of the peroxisome proliferator-activated receptor-α (PPAR-α) in the regulation of acute inflammation
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The Protein Kinase C Signaling Pathway Regulates a Molecular Switch between Transactivation and Transrepression Activity of the Peroxisome Proliferator-Activated Receptor α
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Development of hepatocellular carcinomas and increased peroxisomal fatty acid β-oxidation in rats fed [4-chloro-6-(2, 3-xylidino)-2-pyrimidinylthio] acetic acid (Wy-14, 643) in the semipurified diet
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Peroxisome proliferator-activated receptor-α and retinoid X receptor agonists inhibit inflammatory responses of astrocytes
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Peroxisome proliferator–activated receptor δ limits the expansion of pathogenic Th cells during central nervous system autoimmunity
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PPARα downregulates airway inflammation induced by lipopolysaccharide in the mouse
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Lipoxins: regulators of resolution
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Peroxisome Proliferator-Activated Receptor γ Inhibits the Migration of Dendritic Cells: Consequences for the Immune Response
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Authors: Varga, T., Czimmerer, Z., & Nagy, L.
Affiliations: University of Debrecen (HU)
ORCID: Czimmerer, Zsolt
Venue: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Publisher: Elsevier BV
Published: 2011-08
Volume: 1812
Issue: 8
Pages: 1007-1022
ISSN: 0925-4439 (ISSN-L)
DOI: 10.1016/j.bbadis.2011.02.014
PMC: PMC3117990
OpenAlex: W2129205142
Cited by: 933
References: 164
Citations by year: 2026: 43 · 2025: 81 · 2024: 69 · 2023: 69 · 2022: 74 · 2021: 103 · 2020: 90 · 2019: 87 · 2018: 60 · 2017: 52 · 2016: 43 · 2015: 44 · 2014: 38 · 2013: 40 · 2012: 36
FWCI: 3.49
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1207 d)
Locations: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
Funders: Hungarian Scientific Research Fund (NK72730)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Health Sciences › Nursing › Nutrition and Dietetics › Fatty Acid Research and Health
Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
Keywords: peroxisome proliferator-activated receptors, nuclear receptors, fatty acid signaling, lipid metabolism, inflammation, transcriptional regulation, gene expression regulation, homeostasis, lipoproteins
MeSH terms: Animals, Fatty Acids, Humans, Inflammation, Transcription Factors, Receptors, Cytoplasmic and Nuclear, Peroxisome Proliferator-Activated Receptors, Lipid Metabolism

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Ppars are a unique set of fatty acid regulated transcription factors controlling both lipid metabolism and inflammation

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