PADI4 mediates autophagy and participates in the role of ganoderic acid A monomers in delaying the senescence of Alzheimer's cells through the Akt/mTOR pathway
Autor: | Xiaoming Wang, Hang Lv, Lu-Wei Xiao, Yuan Shi, Shu-Hua Shen |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
Senescence congenital hereditary and neonatal diseases and abnormalities Applied Microbiology and Biotechnology Biochemistry Cell Line Analytical Chemistry Lanosterol 03 medical and health sciences 0302 clinical medicine Protein-Arginine Deiminase Type 4 Alzheimer Disease Autophagy Humans Viability assay Molecular Biology Protein kinase B Cellular Senescence PI3K/AKT/mTOR pathway Reverse Transcriptase Polymerase Chain Reaction Chemistry TOR Serine-Threonine Kinases Organic Chemistry nutritional and metabolic diseases General Medicine Transfection Cell biology 030104 developmental biology Heptanoic Acids Apoptosis Phosphorylation Proto-Oncogene Proteins c-akt 030217 neurology & neurosurgery Biotechnology |
Zdroj: | Bioscience, Biotechnology, and Biochemistry. 85:1818-1829 |
ISSN: | 1347-6947 |
Popis: | The effects of PADI4 and GAA on the senescence of Alzheimer's cells were explored in the present work. HT22 cells were treated with Aβ25-35 to establish an Alzheimer's model and were then treated with different concentrations of GAA and transfected with a siPADI4 lentiviral vector. GAA could reverse the effects of Aβ25-35 on inhibiting cell viability and promoting apoptosis and senescence. siPADI4 reduced Aβ25-35-induced cell viability and upregulated Aβ25-35-induced cell apoptosis and senescence, as well as partially reversed the effect of GAA on cells, and these results were confirmed by detecting the expressions of senescence- and apoptosis-related proteins. In addition, siPADI4 was found to promote the phosphorylation of Akt and mTOR, which was partially reversed by GAA. In conclusion, PADI4 mediates autophagy and participates in the role of GAA monomers in delaying the senescence of Alzheimer's cells through the Akt/mTOR pathway. |
Databáze: | OpenAIRE |
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