| First Author | Sanjay | Year | 2022 |
| Journal | Mol Neurobiol | Volume | 59 |
| Issue | 8 | Pages | 5135-5148 |
| PubMed ID | 35670898 | Mgi Jnum | J:350957 |
| Mgi Id | MGI:7663128 | Doi | 10.1007/s12035-022-02873-9 |
| Citation | Sanjay, et al. (2022) Cyanidin-3-O-Glucoside Regulates the M1/M2 Polarization of Microglia via PPARgamma and Abeta42 Phagocytosis Through TREM2 in an Alzheimer's Disease Model. Mol Neurobiol 59(8):5135-5148 |
| abstractText | Microglial polarization plays an essential role in the progression and regression of neurodegenerative disorders. Cyanidin-3-O-glucoside (C3G), a dietary anthocyanin found in many fruits and vegetables, has been reported as an antioxidant, anti-inflammatory, and antitumor agent. However, there have been no reports on whether C3G can regulate the M1/M2 shift in an Alzheimer's disease model. We attempted to investigate the effects of C3G on M1/M2 polarization and the mechanism to regulate anti-inflammation and phagocytosis, both in vitro and in vivo. HMC3 cells were treated with beta-amyloid (Abeta42) in the presence or absence of 50 muM C3G for different time intervals, and APPswe/PS1DeltaE9 mice were orally administered 30 mg/kg/day of C3G for 38 weeks. The in vitro data revealed that C3G could shift the M1 phenotype of microglia to M2 by reducing the expression of M1-specific markers (CD86 and CD80), inflammatory cytokines (IL-Ibeta, IL-6, TNF-alpha), reactive oxygen species, and enhancing the expression of M2-specific markers (CD206 and CD163). The APPswe/PS1DeltaE9 mice results were consistent with the in vitro data, indicating a significant reduction in inflammatory cytokines and higher expression of M2-specific markers such as CD206 and Arg1 in C3G-treated Alzheimer's disease model mice. Additionally, C3G was found to upregulate PPARgamma expression levels both in vitro and in vivo, whereas a PPARgamma antagonist (GW9662) was found to block C3G-mediated effects in vitro. In this study, we confirmed that C3G could regulate microglial polarization by activating PPARgamma and eliminating accumulated beta-amyloid by enhancing Abeta42 phagocytosis through the upregulation of TREM2. |
