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The Patatin-Like Phospholipase Domain Containing Protein 7 Regulates Macrophage Classical Activation through SIRT1/NF-κB and p38 MAPK Pathways.
Zhao, Zheng; Heier, Christoph; Pang, Huimin; Wang, Yu; Huang, Feifei; Chang, Pingan.
Affiliation
  • Zhao Z; Chongqing Key Laboratory of Big Data for Bio-Intelligence, School of Bio-Information, Chongqing University of Posts and Telecommunications, Chongqing 400065, China.
  • Heier C; Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria.
  • Pang H; Chongqing Key Laboratory of Big Data for Bio-Intelligence, School of Bio-Information, Chongqing University of Posts and Telecommunications, Chongqing 400065, China.
  • Wang Y; Chongqing Key Laboratory of Big Data for Bio-Intelligence, School of Bio-Information, Chongqing University of Posts and Telecommunications, Chongqing 400065, China.
  • Huang F; Chongqing Key Laboratory of Big Data for Bio-Intelligence, School of Bio-Information, Chongqing University of Posts and Telecommunications, Chongqing 400065, China.
  • Chang P; Chongqing Key Laboratory of Big Data for Bio-Intelligence, School of Bio-Information, Chongqing University of Posts and Telecommunications, Chongqing 400065, China.
Int J Mol Sci ; 23(23)2022 Nov 29.
Article in En | MEDLINE | ID: mdl-36499308
ABSTRACT
Lysophosphatidylcholine (LPC) is a bioactive lipid that modulates macrophage polarization during immune responses, inflammation, and tissue remodeling. Patatin-like phospholipase domain containing protein 7 (PNPLA7) is a lysophospholipase with a preference for LPC. However, the role of PNPLA7 in macrophage polarization as an LPC hydrolase has not been explored. In the current study, we found that PNPLA7 is highly expressed in naïve macrophages and downregulated upon lipopolysaccharide (LPS)-induced polarization towards the classically activated (M1) phenotype. Consistently, overexpression of PNPLA7 suppressed the expression of proinflammatory M1 marker genes, including interleukin 1ß (IL-1ß), IL-6, inducible nitric oxide synthase (iNOS), and tumor necrosis factor α (TNF-α), whereas knockdown of PNPLA7 augmented the inflammatory gene expression in LPS-challenged macrophages. PNPLA7 overexpression and knockdown increased and decreased Sirtuin1 (SIRT1) mRNA and protein levels, respectively, and affected the acetylation of the nuclear factor-kappa B (NF-κB) p65 subunit, a key transcription factor in M1 polarization. In addition, the levels of phosphorylated p38 mitogen-activated protein kinase (MAPK) were suppressed and enhanced by PNPLA7 overexpression and knockdown, respectively. Taken together, these findings suggest that PNPLA7 suppresses M1 polarization of LPS-challenged macrophages by modulating SIRT1/NF-κB- and p38 MAPK-dependent pathways.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: NF-kappa B / P38 Mitogen-Activated Protein Kinases / Sirtuin 1 / Lysophospholipase / Macrophage Activation Limits: Humans Language: En Journal: Int J Mol Sci Year: 2022 Document type: Article Affiliation country: China

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: NF-kappa B / P38 Mitogen-Activated Protein Kinases / Sirtuin 1 / Lysophospholipase / Macrophage Activation Limits: Humans Language: En Journal: Int J Mol Sci Year: 2022 Document type: Article Affiliation country: China