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Osteoarthritis (OA) is a complex, progressive, and age-associated disease characterized by aberrant epigenetic expression. Epigenetic analysis has helped clarify the role of histone post-translational modifications (PTMs) in OA. PTMs affect histone structure and function and, therefore, regulate the expression of genes implicated in various biological processes. The roles of histone methylation and acetylation in OA progression-including extracellular collagen degradation and matrix destruction-have been thoroughly analyzed. Though several studies have shown that histone PTMs are related to OA, summative investigations in this area are lacking. The present literature review examines the relationships between histone PTMs and OA. It focuses mainly on methylation, acetylation, phosphorylation, lactylation, ubiquitination, and the roles of the histone methyltransferase (HMT)/histone demethylase (HDMT) and histone acetyltransferase (HAT)/histone deacetylase (HDAC) families in OA development. We used epigenetic tools for discovering new OA treatments. This review offers new perspectives for future studies on OA pathogenesis and treatment.
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http://dx.doi.org/10.2147/JIR.S514599 | DOI Listing |
Front Immunol
September 2025
Precision Pharmacy and Drug Development Center, Department of Pharmacy, Tangdu Hospital, Fourth Military Medical University, Xi'an, Shaanxi, China.
Gliomas are the most common primary malignant tumors of the central nervous system (CNS), and despite progress in molecular diagnostics and targeted therapies, their prognosis remains poor. In recent years, immunotherapy has emerged as a promising treatment modality in cancer therapy. However, the inevitable immune evasion by tumor cells is a key barrier affecting therapeutic efficacy.
View Article and Find Full Text PDFFront Endocrinol (Lausanne)
September 2025
Department of Orthopedics I, Second Affiliated Hospital, Anhui University of Traditional Chinese Medicine, Hefei, Anhui, China.
Background: Emerging evidence indicates that lactase-mediated histone lactylation can activate osteogenic gene expression and promote bone formation. However, the role of lactylation-related genes (LRGs) in osteoporosis (OP) remains unclear. This study aims to clarify the key roles of LRGs and the molecular mechanisms of related biomarkers in OP.
View Article and Find Full Text PDFFuture Med Chem
September 2025
Institute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou, P.R. China.
The nuclear receptor binding SET domain (NSD) family of histone methyltransferases, which comprised NSD1, NSD2, and NSD3. They play a pivotal role in catalyzing mono- and dimethylation of histone H3 at lysine 36 (H3K36me1/2), a modification critical for maintaining chromatin structure and transcriptional fidelity. Dysregulation of NSD enzymes, often through overexpression, mutation, or chromosomal translocation, has been implicated in a broad spectrum of malignancies and various diseases.
View Article and Find Full Text PDFNucleus
December 2025
Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
Using an in situ nucleosome stability assay based on salt extraction, we identified distinct stability features of H2A.Z-containing nucleosomes linked to alternative interactions of the histone variant's C-terminal tail (Imre et al., Nat.
View Article and Find Full Text PDFSci China Life Sci
September 2025
State Key Laboratory of Experimental Hematology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Medical University Cancer Institute and Hospital, Tianjin Key Labora
Histone arginine methylation by protein arginine methyltransferases (PRMTs) is crucial for transcriptional regulation and is implicated in cancers. Despite their therapeutic potential, some PRMTs present challenges as drug targets due to their context-dependent activities. Here, we demonstrate that hypoxia triggers the rapid condensation of PRMT2, which is essential for its histone H3R8 asymmetric dimethylation (H3R8me2a) activity.
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