Kang JH, Liu JJ, Liang PP, Liu HL, Qu FY, Nie PF, Long WJ. Protein acylation and heart failure: A review of novel lysine modifications in cardiac pathology. World J Cardiol 2026; 18(10): 124339 [DOI: 10.4330/wjc.124339]
Corresponding Author of This Article
Wen-Jie Long, Department of Geriatrics, The First Affiliated Hospital of Guangzhou University of Chinese Medicine, No. 12 Jichang Road, Guangzhou 510405, Guangdong Province, China. lwj5699@gzucm.edu.cn
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Cardiac & Cardiovascular Systems
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review-article
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Kang JH, Liu JJ, Liang PP, Liu HL, Qu FY, Nie PF, Long WJ. Protein acylation and heart failure: A review of novel lysine modifications in cardiac pathology. World J Cardiol 2026; 18(10): 124339 [DOI: 10.4330/wjc.124339]
World J Cardiol. Oct 26, 2026; 18(10): 124339 Published online Oct 26, 2026. doi: 10.4330/wjc.124339
Protein acylation and heart failure: A review of novel lysine modifications in cardiac pathology
Jin-Hua Kang, Jia-Jun Liu, Peng-Peng Liang, Hui-Lin Liu, Fang-Yuan Qu, Peng-Fei Nie, Wen-Jie Long
Jin-Hua Kang, Peng-Fei Nie, Guangzhou Hospital of Integrated Chinese and Western Medicine, Guangzhou 518000, Guangdong Province, China
Jin-Hua Kang, Jia-Jun Liu, Peng-Peng Liang, Luohu District Hospital of Traditional Chinese Medicine, Shenzhen 518000, Guangdong Province, China
Hui-Lin Liu, State Key Laboratory of Traditional Chinese Medicine Syndrome, The First Affiliated Hospital of Guangzhou University of Chinese Medicine, Guangzhou 510405, Guangdong Province, China
Fang-Yuan Qu, The First Affiliated Hospital of Guangzhou University of Chinese Medicine, Guangzhou 510405, Guangdong Province, China
Wen-Jie Long, Department of Geriatrics, The First Affiliated Hospital of Guangzhou University of Chinese Medicine, Guangzhou 510405, Guangdong Province, China
Co-corresponding authors: Peng-Fei Nie and Wen-Jie Long.
Author contributions: Kang JH, Liu JJ, Liang PP, and Liu HL contributed equally to this work; Kang JH, Nie PF, and Long WJ conceived and designed the review; Kang JH, Liang PP, Liu JJ, and Liu HL performed the literature search, data collection, and manuscript drafting; Qu FY contributed to literature organization, figure/table preparation, and manuscript revision; Nie PF and Long WJ supervised the review, provided critical intellectual input, revised the manuscript critically for important intellectual content, and were responsible for project administration and funding acquisition as co-corresponding authors. All authors read and approved the final manuscript.
AI contribution statement: Not applicable.
Supported by National Natural Science Foundation of China, No. 82505398; and Basic Research Project of Natural Science Foundation of Shenzhen Municipality, No. JCYJ20240813163011015.
Conflict-of-interest statement: All the authors report no relevant conflicts of interest for this article.
Corresponding author: Wen-Jie Long, Department of Geriatrics, The First Affiliated Hospital of Guangzhou University of Chinese Medicine, No. 12 Jichang Road, Guangzhou 510405, Guangdong Province, China. lwj5699@gzucm.edu.cn
Received: June 12, 2026 Revised: August 11, 2026 Accepted: October 8, 2026 Published online: October 26, 2026 Processing time: 133 Days and 16.6 Hours
Abstract
Pathological cardiac hypertrophy is a primary contributor to heart failure (HF). Protein acylation, particularly acetylation, plays a crucial role in this process. Advances in mass spectrometry and proteomics have identified an increasing number of novel lysine acylation modifications, including crotonylation, lactylation, succinylation, β-hydroxybutyrylation, 2-hydroxyisobutyrylation, propionylation and malonylation. These novel acylations are implicated in key physiological processes and disease-related cellular functions, as they modify the physicochemical properties of proteins and closely link substrate metabolism to gene regulation. Research on these novel lysine acylations associated with cardiac hypertrophy and HF has been steadily increasing in recent years. This review aims to summarize the progress and significance of these novel lysine acylations in cardiac hypertrophy and HF, providing references for a deeper understanding of the pathogenesis of HF and development of innovative therapeutic strategies.
Core Tip: This review highlights novel lysine acylations that link substrate metabolism to gene regulation by altering protein properties and play key roles in pathological cardiac hypertrophy and heart failure. It summarizes their emerging roles and significance in these conditions, providing insights into the pathogenesis of heart failure and potential therapeutic strategies.
