The Patatin-like Phospholipase Domain Containing Protein 7 (PNPLA7) Facilitates M2 Polarization of Macrophages Through a PPARγ-Dependent Mechanism
10.13865/j.cnki.cjbmb.2022.07.1093
- Author:
Yu WANG
1
;
Fei-Fei HUANG
1
;
Xiao-Hong HE
1
;
Quan SUN
1
;
Ping-An CHANG
1
Author Information
1. Chongqing Key Laboratory of Big Data for Bio-intelligence, College of Bio-information, Chongqing University of Posts and Telecommunications
- Publication Type:Journal Article
- Keywords:
lysophosphatidylcholine (LPC);
M2 macrophage;
patatin-like phospholipase domain containing protein7;
peroxisome proliferator activated receptor-γ (PPARγ)
- From:
Chinese Journal of Biochemistry and Molecular Biology
2022;38(9):1193-1201
- CountryChina
- Language:Chinese
-
Abstract:
Lysophosphatidylcholine (LPC) modulates the dynamic and integral process of macrophage polarization in immune responses, tissue inflammation and remodeling. Patatin-like phospholipase domain containing protein 7 (PNPLA7) was identified as an LPC-preferring lysophospholipase recently. However, the expression and role of PNPLA7 in macrophage polarization remained unknown. In the present study, PNPLA7 was found to be upregulated in the process of macrophage polarization toward an alternatively activated (M2) phenotype stimulated with interleukin 4 (IL-4) (P<0.05). We found that knockdown and overexpression of PNPLA1 decreased and increased the expression of M2 marker genes, including arginase 1 (Argl) and chitinase-like 3 (Ym\ ), respectively (P<0.05). Further studies showed that PNPLA7 regulated the expression of peroxisome proliferator activated receptor-γ (P P A R γ) at the mRNA and protein levels during M2 polarization (P < 0.05). However, the phosphorylation of signal transducer and activator of transcription 6 (STAT6) was not influenced by PNPLA7. These findings suggest that PNPLA7 favors macrophage anti-inflammatory M2 polarization through a PPAR^-dependent mechanism.
