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NAT10 promotes glycolysis and cell stemness of ovarian cancer cells via ac4C acetylation of PGAM1 mRNA
by
Shen, Yuan
, Zhang, Qian
in
631/67
/ 631/80
/ ac4C acetylation modification
/ Acetylation
/ Acetyltransferase
/ Acidification
/ Animals
/ Antibodies
/ Cancer therapies
/ Cell Line, Tumor
/ Cells
/ Female
/ Gene Expression Regulation, Neoplastic
/ Glucose
/ Glycolysis
/ Glycolysis - genetics
/ Growth factors
/ Humanities and Social Sciences
/ Humans
/ Immunoprecipitation
/ Malignancy
/ Mice
/ Mice, Nude
/ Molecular modelling
/ mRNA stability
/ multidisciplinary
/ N-Acetyltransferase
/ N-Terminal Acetyltransferase E - genetics
/ N-Terminal Acetyltransferase E - metabolism
/ N-Terminal Acetyltransferases
/ NAT10
/ Neoplastic Stem Cells - metabolism
/ Neoplastic Stem Cells - pathology
/ Ovarian cancer
/ Ovarian Neoplasms - genetics
/ Ovarian Neoplasms - metabolism
/ Ovarian Neoplasms - pathology
/ Pathogenesis
/ PGAM1
/ Phosphoglycerate mutase
/ Phosphoglycerate Mutase - genetics
/ Phosphoglycerate Mutase - metabolism
/ Plasmids
/ Proteins
/ Reagents
/ RNA modification
/ RNA, Messenger - genetics
/ RNA, Messenger - metabolism
/ Science
/ Science (multidisciplinary)
/ Therapeutic targets
/ Tumorigenesis
2025
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NAT10 promotes glycolysis and cell stemness of ovarian cancer cells via ac4C acetylation of PGAM1 mRNA
by
Shen, Yuan
, Zhang, Qian
in
631/67
/ 631/80
/ ac4C acetylation modification
/ Acetylation
/ Acetyltransferase
/ Acidification
/ Animals
/ Antibodies
/ Cancer therapies
/ Cell Line, Tumor
/ Cells
/ Female
/ Gene Expression Regulation, Neoplastic
/ Glucose
/ Glycolysis
/ Glycolysis - genetics
/ Growth factors
/ Humanities and Social Sciences
/ Humans
/ Immunoprecipitation
/ Malignancy
/ Mice
/ Mice, Nude
/ Molecular modelling
/ mRNA stability
/ multidisciplinary
/ N-Acetyltransferase
/ N-Terminal Acetyltransferase E - genetics
/ N-Terminal Acetyltransferase E - metabolism
/ N-Terminal Acetyltransferases
/ NAT10
/ Neoplastic Stem Cells - metabolism
/ Neoplastic Stem Cells - pathology
/ Ovarian cancer
/ Ovarian Neoplasms - genetics
/ Ovarian Neoplasms - metabolism
/ Ovarian Neoplasms - pathology
/ Pathogenesis
/ PGAM1
/ Phosphoglycerate mutase
/ Phosphoglycerate Mutase - genetics
/ Phosphoglycerate Mutase - metabolism
/ Plasmids
/ Proteins
/ Reagents
/ RNA modification
/ RNA, Messenger - genetics
/ RNA, Messenger - metabolism
/ Science
/ Science (multidisciplinary)
/ Therapeutic targets
/ Tumorigenesis
2025
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NAT10 promotes glycolysis and cell stemness of ovarian cancer cells via ac4C acetylation of PGAM1 mRNA
by
Shen, Yuan
, Zhang, Qian
in
631/67
/ 631/80
/ ac4C acetylation modification
/ Acetylation
/ Acetyltransferase
/ Acidification
/ Animals
/ Antibodies
/ Cancer therapies
/ Cell Line, Tumor
/ Cells
/ Female
/ Gene Expression Regulation, Neoplastic
/ Glucose
/ Glycolysis
/ Glycolysis - genetics
/ Growth factors
/ Humanities and Social Sciences
/ Humans
/ Immunoprecipitation
/ Malignancy
/ Mice
/ Mice, Nude
/ Molecular modelling
/ mRNA stability
/ multidisciplinary
/ N-Acetyltransferase
/ N-Terminal Acetyltransferase E - genetics
/ N-Terminal Acetyltransferase E - metabolism
/ N-Terminal Acetyltransferases
/ NAT10
/ Neoplastic Stem Cells - metabolism
/ Neoplastic Stem Cells - pathology
/ Ovarian cancer
/ Ovarian Neoplasms - genetics
/ Ovarian Neoplasms - metabolism
/ Ovarian Neoplasms - pathology
/ Pathogenesis
/ PGAM1
/ Phosphoglycerate mutase
/ Phosphoglycerate Mutase - genetics
/ Phosphoglycerate Mutase - metabolism
/ Plasmids
/ Proteins
/ Reagents
/ RNA modification
/ RNA, Messenger - genetics
/ RNA, Messenger - metabolism
/ Science
/ Science (multidisciplinary)
/ Therapeutic targets
/ Tumorigenesis
2025
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NAT10 promotes glycolysis and cell stemness of ovarian cancer cells via ac4C acetylation of PGAM1 mRNA
Journal Article
NAT10 promotes glycolysis and cell stemness of ovarian cancer cells via ac4C acetylation of PGAM1 mRNA
2025
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Overview
Ovarian cancer represents one of the most prevalent gynecological malignancies with a poor prognosis. Targeting glycolytic pathways has emerged as a novel cancer therapeutic strategy. N-acetyltransferase 10 (NAT10)-mediated N4-acetylcytidine (ac4C) modification plays a regulatory role in cancer glycolysis. Phosphoglycerate mutase 1 (PGAM1) functions as a critical glycolytic enzyme and potential therapeutic target in oncology. This study investigated the functional role and underlying mechanisms of NAT10 in ovarian cancer progression. Cellular glycolysis was assessed through glucose uptake measurements, lactate production quantification, and extracellular acidification rate analysis. Cell stemness characteristics were evaluated using sphere formation assays and western blot analysis. Molecular mechanisms were explored via quantitative real-time PCR, RNA immunoprecipitation (RIP), ac4C-specific RIP, dot blot analysis, and dual-luciferase reporter assays. Elevated NAT10 expression and ac4C modification levels were observed in ovarian cancer cells. NAT10 silencing significantly inhibited both cell stemness properties and glycolytic activity. Mechanistically, NAT10 enhanced PGAM1 mRNA stability through ac4C modification. Re-expression of PGAM1 reversed the functional effects induced by NAT10 depletion in ovarian cancer cells. Furthermore, in vivo tumor growth experiments demonstrated that NAT10 promotes tumorigenesis. Our findings demonstrate that NAT10 facilitates ovarian cancer progression by mediating ac4C modification of PGAM1. This study identifies a novel and potentially effective therapeutic target for ovarian cancer treatment.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/80
/ ac4C acetylation modification
/ Animals
/ Cells
/ Female
/ Gene Expression Regulation, Neoplastic
/ Glucose
/ Humanities and Social Sciences
/ Humans
/ Mice
/ N-Terminal Acetyltransferase E - genetics
/ N-Terminal Acetyltransferase E - metabolism
/ N-Terminal Acetyltransferases
/ NAT10
/ Neoplastic Stem Cells - metabolism
/ Neoplastic Stem Cells - pathology
/ Ovarian Neoplasms - genetics
/ Ovarian Neoplasms - metabolism
/ Ovarian Neoplasms - pathology
/ PGAM1
/ Phosphoglycerate Mutase - genetics
/ Phosphoglycerate Mutase - metabolism
/ Plasmids
/ Proteins
/ Reagents
/ Science
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