ArticleCell death and differentiation2026
AARS1-mediated lactylation of H3K18 and STAT1 promotes ferroptosis in diabetic nephropathy.
Article in Cell death and differentiation, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The lactate-lactylation axis in acute kidney injury: mechanisms from metabolic reprogramming to epigenetic regulation and clinical therapeutic prospects.International urology and nephrology · 2026Review
- LRRC8A deficiency in vascular smooth muscle cells promotes STAT1/Calcrl/Ramp1 signaling to decrease blood pressure.Acta pharmacologica Sinica · 2026Article
- Lactate-Mediated Lysine Lactylation in Renal Fibrosis: Current Progress and Challenges.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- Lactate-dependent regulation of ferroptosis: redox homeostasis, lactylation, and translational perspectives.Apoptosis : an international journal on programmed cell death · 2026Review
- The Lactate-lactylation circuitry in kidney fibrosis: cellular crosstalk from tubular metabolic reprogramming to macrophage effector functions.Seminars in immunopathology · 2026Review
- p300-Mediated H3K18 Lactylation Drives Radiation-Induced Pulmonary Fibrosis via VIRMA-Dependent m6A Modification of GATA3.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Lysine l-Lactylation: Bridging Metabolism, Chromatin and Disease.Cell proliferation · 2026Review
- Keratin 18 functions as a lactyltransferase to trigger necroptosis in diabetic kidney disease by modulating Fas transcription.Experimental & molecular medicine · 2026Article
- Unveiling lactylation: A novel frontier in the pathogenesis of diabetic nephropathy (Review).International journal of molecular medicine · 2026Review
- AARS1 promotes diabetic kidney disease through rewiring Akt and NF-κB signaling to suppress autophagy and sustain inflammation.Cellular & molecular biology letters · 2026Article
- Epigenetic regulation in a high-sugar environment (Review).International journal of molecular medicine · 2026Review
- Lactylation-regulated ferroptosis: mechanisms, disease associations, and therapeutic strategies.Archives of pharmacal research · 2026Review
- Post‑translational modifications in diabetic kidney disease (Review).International journal of molecular medicine · 2026Review
- Lactylation in kidney diseases: a review of regulatory mechanisms and therapeutic prospects.Frontiers in cell and developmental biology · 2026Review
- Role of metabolic reprogramming and lactylation in diabetic nephropathy: molecular mechanisms and therapeutic prospects - a narrative review.Frontiers in endocrinology · 2026Review
- Lactylation in sepsis-associated acute kidney injury: regulatory mechanisms and therapeutic prospects.Frontiers in molecular biosciences · 2026Review
- Tubular injury in diabetic kidney disease: a focus on regulated cell death.Frontiers in endocrinology · 2026Review
- When metabolic enzymes meet lactylation: a bidirectional dialogue in health and disease.Frontiers in cell and developmental biology · 2026Review
- Progress on novel compounds for the treatment of bone metabolism-related disorders: focus on osteoporosis and beyond.Frontiers in chemistry · 2026Review
- Lactate Metabolism and Protein Lactylation in Diabetic Kidney Disease: A Narrative Review.Diabetes, metabolic syndrome and obesity : targets and therapy · 2026Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diabetic nephropathy (DN) is the primary cause of end-stage renal disease worldwide. Recent studies have revealed that lactate-mediated histone lactylation, which functions as a novel epigenetic modification, is involved in the occurrence and development of diabetes-related complications. However, little is known about the role of lactyltransferase in DN. Alanyl-tRNA synthetase 1 (AARS1) was identified as a novel lactyltransferase that modulates histone H3-lysine-18 lactylation (H3K18la). In the present study, we determined whether AARS1-mediated H3K18la participates in the pathogenesis of DN. More importantly, we explored the potential mechanism involved. A mouse DN model consisting of both wild-type and alanyl-tRNA synthetase (AARS1) heterozygote (AARS1
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