Liu Jiena, Zhao Liuying, Yan Meisi, Jin Shengye, Shang Lingmin, Wang Jianyu, Wang Qin, Zhao Shilu, Shen Zibo, Liu Tong, Wu Hao, Pang Da
Department of Breast Surgery, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang Province, 150081, China.
Department of Pathology, Harbin Medical University, Harbin, Heilongjiang Province, China.
J Exp Clin Cancer Res. 2025 Aug 23;44(1):252. doi: 10.1186/s13046-025-03512-6.
Metabolic reprogramming and epigenetic modification are two hallmarks of cancer. Protein lysine lactylation (Kla) is a novel type of glycolysis lactate-triggered posttranslational modification. However, the role of Kla in breast cancer (BC) remains largely unknown. Here, western blot, and immunohistochemical (IHC) staining of BC tissues revealed that global Kla levels were upregulated in BC tissues, and high levels of Kla were correlated with poor prognosis of patients with BC. A series of in vitro and in vivo assays demonstrated that interruption of glycolysis by lactate dehydrogenase (LDH) inhibitor or silencing LDHA and LDHB repressed the malignant behaviors of BC cells. Moreover, 4D label-free quantitative lactylproteomics analysis of BC tissues and cells revealed that lactylated proteins widely existed in several subcellular compartments and were closely associated with various cancer-related biological processes. Notably, two previously unresearched sites of histone lactylation, H4K79 lactylation (H4K79la) and H4K91 lactylation (H4K91la), were identified to be hyperlactylated in cancer tissues and cells. Glycolytic genes, such as lactate dehydrogenase A (LDHA), phosphoglycerate kinase 1 (PGK1), and hexokinase 1 (HK1) were identified to be the potential candidate genes epigenetically regulated by H4K79la and H4K91la by intersecting through chromatin immunoprecipitation sequencing (ChIP-seq), RNA sequencing (RNA-seq), and TCGA-BRCA database. Pharmacological inhibition of glycolysis downregulated H4K79 and H4K91 lactylation and suppressed the expression of glycolytic genes, whereas treatment with sodium lactate exhibited the opposite effects. Additionally, E1A-binding protein p300 (P300) acted as lysine lactyltransferase to regulate H4K79la and H4K91la, and control the transcription and expression of downstream glycolytic genes in BC cells. The results revealed an intriguing positive feedback loop formed by glycolysis/H4K79la/H4K91la/glycolytic genes in BC, highlighting the relationship between metabolic reprogramming and epigenetic regulation. These findings provide new therapeutic targets for patients with BC.
代谢重编程和表观遗传修饰是癌症的两个标志。蛋白质赖氨酸乳酰化(Kla)是一种新型的糖酵解乳酸触发的翻译后修饰。然而,Kla在乳腺癌(BC)中的作用仍 largely未知。在这里,对BC组织进行的蛋白质印迹和免疫组织化学(IHC)染色显示,BC组织中整体Kla水平上调,高水平的Kla与BC患者的不良预后相关。一系列体外和体内试验表明,乳酸脱氢酶(LDH)抑制剂或沉默LDHA和LDHB中断糖酵解可抑制BC细胞的恶性行为。此外,对BC组织和细胞进行的4D无标记定量乳酰蛋白质组学分析表明,乳酰化蛋白广泛存在于几个亚细胞区室中,并与各种癌症相关的生物学过程密切相关。值得注意的是,在癌症组织和细胞中发现了两个以前未研究过的组蛋白乳酰化位点,即H4K79乳酰化(H4K79la)和H4K91乳酰化(H4K91la),它们高度乳酰化。通过染色质免疫沉淀测序(ChIP-seq)、RNA测序(RNA-seq)和TCGA-BRCA数据库交叉分析,发现糖酵解基因,如乳酸脱氢酶A(LDHA)、磷酸甘油酸激酶1(PGK1)和己糖激酶1(HK1)是受H4K79la和H4K91la表观遗传调控的潜在候选基因。糖酵解的药理学抑制下调了H4K79和H4K91乳酰化,并抑制了糖酵解基因的表达,而乳酸钠处理则表现出相反的效果。此外,E1A结合蛋白p300(P300)作为赖氨酸乳酰转移酶来调节H4K79la和H4K91la,并控制BC细胞中下游糖酵解基因的转录和表达。结果揭示了BC中由糖酵解/H4K79la/H4K91la/糖酵解基因形成的一个有趣的正反馈环,突出了代谢重编程与表观遗传调控之间的关系。这些发现为BC患者提供了新的治疗靶点。