[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"doc-detail-332379-en":3,"doc-seo-332379-105":31,"detail-sidebar-cat-0-en-105":99},{"code":4,"msg":5,"data":6},0,"success",{"doc_id":7,"user_id":8,"nickname":9,"user_avatar":10,"doc_module":4,"category_id":11,"category_name":12,"doc_title":13,"doc_description":14,"doc_content":15,"file_id":16,"file_url":17,"file_type":18,"file_size":19,"view_count":20,"is_deleted":4,"is_public":21,"is_downloadable":21,"audit_status":21,"page_count":22,"language":23,"language_code":24,"site_id":25,"html_lang":24,"table_of_contents":26,"faqs":27,"seo_title":28,"seo_description":14,"update_tm":29,"read_time":30,"preview_page_count":4},332379,1099514068035,"Ezra","https://ap-avatar.wpscdn.com/davatar_276721f389ce27ea32af1340a28f341c",8,"Research & Report","Acetylation of PGK1 at lysine 323 promotes glycolysis, cell proliferation, and metastasis in luminal A breast cancer cells","This study investigates how protein acetylation contributes to luminal A breast cancer biology, focusing on acetylated targets previously detected by iTRAQ. Bioinformatics identified acetylation sites, followed by proteomic and experimental validation of acetyltransferases and deacetylases. Functional assays tested metabolic output (glucose consumption, ATP, lactate) and cellular behavior (proliferation and metastasis) via viability, cell-cycle analysis, clonogenic growth, migration/invasion tests, and EMT/MMP markers. Results show that PGK1 lysine 323 acetylation enhances glycolysis and the TCA contribution while driving proliferation and metastasis, regulated by p300 and Sirtuin3.","Gao et al. BMC Cancer (2024) 24:1054 [https://doi.org/10.1186/s12885-024-12792-8](https://doi.org/10.1186/s12885-024-12792-8)  \nBMC Cancer  \n RESEARCH Open Access  \nAcetylation of PGK1 at lysine 323 promotes   glycolysis, cell proliferation, and metastasis in luminal A breast cancer cells  \nXiuli Gao1, Ting Pan2, Yu Gao3, Wenbin Zhu1, Likun Liu1, Wenbo Duan2, Cuicui Han4, Bo Feng5, Wenjing Yan4, Qiuhang Song6, Yunlong Liu7* and Liling Yue1*  \nAbstract  \nBackground In prior research employing iTRAQ (Isobaric Tags for Relative and Absolute Quantitation) technology, we identified a range of proteins in breast cancer tissues exhibiting high levels of acetylation. Despite this advancement, the specific functions and implications of these acetylated proteins in the context of cancer biology have yet to be elucidated. This study aims to systematically investigate the functional roles of these acetylated proteins with the objective of identifying potential therapeutic targets within breast cancer pathophysiology.  \nMethods Acetylated targets were identified through bioinformatics, with their expression and acetylation subsequently confirmed. Proteomic analysis and validation studies identified potential acetyltransferases and deacetylases. We evaluated metabolic functions via assays for catalytic activity, glucose consumption, ATP levels, and lactate production. Cell proliferation and metastasis were assessed through viability, cycle analysis, clonogenic assays, PCNA uptake, wound healing, Transwell assays, and MMP/EMT marker detection.  \nResults Acetylated proteins in breast cancer were primarily involved in metabolism, significantly impacting glycolysis and the tricarboxylic acid cycle. Notably, PGK1 showed the highest acetylation at lysine 323 and exhibited increased expression and acetylation across breast cancer tissues, particularly inT47D and MCF-7 cells. Notably,  \n18 varieties acetyltransferases or deacetylases were identified inT47D cells, among which p300 and Sirtuin3 were validated for their interaction with PGK1 . Acetylation at 323 K enhanced PGK1’s metabolic role by boosting its activity, glucose uptake, ATP production, and lactate output. This modification also promoted cell proliferation, as evidenced by increased viability, S phase ratio, clonality, and PCNA levels. Furthermore, PGK1-323 K acetylation facilitated metastasis, improving wound healing, cell invasion, and upregulating MMP2, MMP9, N-cadherin, and Vimentin while downregulating E-cadherin.  \nConclusion PGK1-323 K acetylation was significantly elevated inT47D and MCF-7 luminal A breast cancer cells and this acetylation could be regulated by p300 and Sirtuin3 . PGK1-323 K acetylation promoted cell glycolysis, proliferation, and metastasis, highlighting novel epigenetic targets for breast cancer therapy.  \nKeywords Breast cancer, PGK1 acetylation, Glycolysis, Cell proliferation and metastasis, Acetyltransferase and deacetylase  \n*Correspondence: Yunlong Liu [38396193@qq.com](38396193@qq.com)[ ](38396193@qq.com)Liling Yue [yuell1025@126.com](yuell1025@126.com)  \nFull list of author information is available at the end of the article  \n© The Author(s) 2024. Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory","cbCaioNPCImVr9s2","https://ap.wps.com/l/cbCaioNPCImVr9s2","pdf",5980408,15,1,17,"English","en",105,"# Abstract\n## Background\n## Methods\n## Results\n## Conclusion\n# Introduction\n## Epidemiology and unmet needs\n## Epigenetic regulation and protein acetylation","[{\"question\":\"What is the main focus of the study on luminal A breast cancer cells?\",\"answer\":\"The study examines how acetylation of PGK1 at lysine 323 affects glycolysis, cell proliferation, and metastasis.\"},{\"question\":\"How were acetylated targets and modifying enzymes identified and validated?\",\"answer\":\"Acetylated targets were identified using bioinformatics, then confirmed by proteomic analysis and validation studies, including identifying acetyltransferases and deacetylases.\"},{\"question\":\"What functional effects does PGK1 lysine 323 acetylation produce?\",\"answer\":\"It increases PGK1 activity and enhances glucose uptake, ATP production, and lactate output, leading to higher proliferation and improved metastatic behaviors with changes in EMT and MMP markers.\"}]","Acetylation of PGK1 at lysine 323 promotes glycolysis, cell proliferation, and metastasis in luminal A breast cancer cells | 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is the main focus of the study on luminal A breast cancer cells?","Question",{"text":82,"@type":83},"The study examines how acetylation of PGK1 at lysine 323 affects glycolysis, cell proliferation, and metastasis.","Answer",{"name":85,"@type":80,"acceptedAnswer":86},"How were acetylated targets and modifying enzymes identified and validated?",{"text":87,"@type":83},"Acetylated targets were identified using bioinformatics, then confirmed by proteomic analysis and validation studies, including identifying acetyltransferases and deacetylases.",{"name":89,"@type":80,"acceptedAnswer":90},"What functional effects does PGK1 lysine 323 acetylation produce?",{"text":91,"@type":83},"It increases PGK1 activity and enhances glucose uptake, ATP production, and lactate output, leading to higher proliferation and improved metastatic behaviors with changes in EMT and MMP 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