ArticleGastroenterology research2025
Histone Lactylation-Driven Ubiquitin-Specific Protease 34 Promotes Cisplatin Resistance in Hepatocellular Carcinoma.
Article in Gastroenterology research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Clinical implications of lactylation modification in digestive system tumors (Review).Oncology letters · 2026Review
- Lactylation as a metabolic-epigenetic switch: Mechanisms and roles in cancer, sepsis, trauma, inflammation, and tissue repair.Biochemistry and biophysics reports · 2026Review
- Beyond metabolism: exploring the regulatory and therapeutic implications of lactate and lactylation in cancer-regulated cell death.Cell death & disease · 2026Review
- A novel dual histone mark reader ZCWPW2 regulates meiotic recombination through lactylation and transcriptional regulation in humans and mice.Nucleic acids research · 2026Article
- Targeting Lactylation for Cancer: Mechanisms, Effects, and Therapeutic Prospects.International journal of molecular sciences · 2025Review
- Targeting Lactylation: From Metabolic Reprogramming to Precision Therapeutics in Liver Diseases.Biomolecules · 2025Review
- Protein lactylation and immunotherapy in gliomas: A novel regulatory axis in tumor metabolism (Review).International journal of oncology · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
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Abstract
Background: Ubiquitin-specific protease 34 (USP34) is a deubiquitinase that has been shown to play a critical role in the process of tumor drug-resistance. The objective of this study was to investigate the role of USP34 in cisplatin resistance in hepatocellular carcinoma (HCC). Methods: Firstly, we analyzed the USP34 levels in cisplatin-sensitive and -resistant patients using The Cancer Genomic Atlas (TCGA) data from Gene Expression Profiling Interactive Analysis (GEPIA2). The cell viability and half-maximal inhibitory concentration (IC Results: USP34 was significantly upregulated in cisplatin-resistant HCC tissues and cells. Functional studies found that knockdown of USP34 inhibited HepG2 and HepG2/DDP cell proliferation and survival. Importantly, knockdown of USP34 enhanced cisplatin sensitivity in HepG2 and HepG2/DDP cells. Mechanistically, lactylation of histones promoted the expression level of USP34 in HepG2/DDP cells. Conclusion: USP34 promotes the progression of HCC by regulating histone lactylation levels and cisplatin resistance in HCC.
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Registered trials
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