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• W4375955209 abstract "There are multiple theories of Alzheimer's disease pathogenesis. One major theory is that oxidation of amyloid beta (Aβ) promotes plaque deposition that directly contributes to pathology. A competing theory is that hypomethylation of DNA (due to altered one carbon metabolism) results in pathology through altered gene regulation. Herein, we propose a novel hypothesis involving L-isoaspartyl methyltransferase (PIMT) that unifies the Aβ and DNA hypomethylation hypotheses into a single model. Importantly, the proposed model allows bidirectional regulation of Aβ oxidation and DNA hypomethylation. The proposed hypothesis does not exclude simultaneous contributions by other mechanisms (e.g., neurofibrillary tangles). The new hypothesis is formulated to encompass oxidative stress, fibrillation, DNA hypomethylation, and metabolic perturbations in one carbon metabolism (i.e., methionine and folate cycles). In addition, deductive predictions of the hypothesis are presented both to guide empirical testing of the hypothesis and to provide candidate strategies for therapeutic intervention and/or nutritional modification. HIGHLIGHTS: PIMT repairs L-isoaspartyl groups on amyloid beta and decreases fibrillation. SAM is a common methyl donor for PIMT and DNA methyltransferases. Increased PIMT activity competes with DNA methylation and vice versa. The PIMT hypothesis bridges a gap between plaque and DNA methylation hypotheses." @default.
• W4375955209 created "2023-05-10" @default.
• W4375955209 creator A5041867277 @default.
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• W4375955209 date "2023-05-08" @default.
• W4375955209 modified "2023-10-12" @default.
• W4375955209 title "The role of PIMT in Alzheimer's disease pathogenesis: A novel hypothesis" @default.
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• W4375955209 doi "https://doi.org/10.1002/alz.13115" @default.
• W4375955209 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37157118" @default.
• W4375955209 hasPublicationYear "2023" @default.
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