Novel histone post-translational modifications in Alzheimer's disease: current advances and implications

• Published in: Clinical epigenetics 2024-03, Vol.16 (1), p.39-39, Article 39
• Main Authors: Qin, Yuanyuan, Yang, Ping, He, Wanhong, Li, Dongze, Zeng, Lisha, Li, Junle, Zhou, Tingting, Peng, Juan, Cao, Ling, Huang, Wei
• Format: Article
• Language: English
• Subjects: Acetylation; Advertising executives; Alzheimer Disease - genetics; Alzheimer's disease; Amino acids; Cognitive ability; Development and progression; Disease; DNA Methylation; Drug development; Drugs; Enzymes; Epigenetics; FDA approval; Gene expression; Gene regulation; Genes; Genetic aspects; Histone; Histones; Histones - metabolism; Humans; Mass spectrometry; Mass spectroscopy; Medical research; Memory; Metabolism; Metabolites; Neurodegeneration; Neurodegenerative diseases; Novel histone post-translational modifications; Pathogenesis; Pathology; Peptides; Phosphorylation; Physiological aspects; Post-translation; Protein Processing, Post-Translational; Proteins; Proteomics; Translation
• ISSN: 1868-7083; 1868-7075; 1868-7083; 1868-7075
• DOI: 10.1186/s13148-024-01650-w

Alzheimer's disease (AD) has a complex pathogenesis, and multiple studies have indicated that histone post-translational modifications, especially acetylation, play a significant role in it. With the development of mass spectrometry and proteomics, an increasing number of novel HPTMs, including lactoylation, crotonylation, β-hydroxybutyrylation, 2-hydroxyisobutyrylation, succinylation, and malonylation, have been identified. These novel HPTMs closely link substance metabolism to gene regulation, and an increasing number of relevant studies on the relationship between novel HPTMs and AD have become available. This review summarizes the current advances and implications of novel HPTMs in AD, providing insight into the deeper pathogenesis of AD and the development of novel drugs.