Acetylsalicylic acid decreases tau phosphorylation at serine 422.
Tau protein pathology in Alzheimer's disease is characterized by the hyperphosphorylation of tau at some specific sites. One of these sites is serine 422 which modification has been correlated with a possible toxic effect of phosphotau in neural cells. In this work, we have found that in the presence of acetylsalicylic acid, at a concentration like that used for anti-inflammatory treatments, tau phosphorylation at serine 422 decreases.
Tortosa
E
E
Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Avila
J
J
Pérez
M
M
D000544:Alzheimer Disease / Q000188:drug therapy / Q000378:metabolism / Q000503:physiopathology; D000595:Amino Acid Sequence / Q000502:physiology; D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry / Q000494:pharmacology; D001241:Aspirin / Q000737:chemistry / Q000494:pharmacology*; D001921:Brain / Q000187:drug effects / Q000378:metabolism / Q000503:physiopathology; D045744:Cell Line, Tumor; D015536:Down-Regulation / Q000187:drug effects / Q000502:physiology; D006801:Humans; D009474:Neurons / Q000187:drug effects / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D012694:Serine / Q000378:metabolism*; D016875:tau Proteins / Q000037:antagonists & inhibitors* / Q000187:drug effects* / Q000378:metabolism
D000894:Anti-Inflammatory Agents, Non-Steroidal; D016875:tau Proteins; D012694:Serine; D001241:Aspirin