Scholarlink

<p>Research indicates that patients with salt-sensitive (SS) hypertension experience higher morbidity and target organ damage than in patients with non-SS hypertension. Dysregulated macrophage activation has been implicated in SS hypertension development, with lysine acetylation playing a role in modulating macrophage function. However, the role of macrophage acetylation patterns in SS hypertension remains unclear. This study aimed to investigate how acetylation regulates macrophage function and its role in the pathogenesis of SS hypertension. We employed quantitative acetylation proteomics to characterize the acetylome of bone marrow-derived macrophages in Dahl SS hypertensive rats fed either a high-salt or a low-salt diet. We identified 94 hyperacetylated and 49 hypoacetylated sites on 79 and 45 proteins, respectively, in the high-salt group. Notably, acetylation levels increased at lysine 20 (K20) and K46 on histone H2B, at K56 on H3, and at K77 and K79 on H4c2. We also identified conserved acetylation motifs, analyzed their Gene Ontology terms and pathways, and explored the protein–protein interactions of these differentially acetylated proteins using bioinformatics analyses. Finally, we validated the altered acetylation of H2, H3, H4, and several metabolic proteins using immunoprecipitation and western blotting. Overall, these findings offer insights into the role of lysine acetylation in macrophages from SS hypertensive rats, revealing potential therapeutic targets.</p> Graphical Abstract <p>Our analysis showed a landscape of lysine acetylation in bone marrow-derived macrophages (BMDMs) from salt-sensitive rats. Furthermore, we clearly identified significantly altered acetylated sites in low-salt and high-salt groups and validated the altered acetylation levels of several histones and metabolic proteins. IP, immunoprecipitation; TMT, tandem mass tag; LC–MS, liquid chromatography-mass spectrometry; HPLC, high-performance liquid chromatography.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Global Analysis of the Lysine Acetylome in Macrophages from Salt-sensitive Hypertensive Rats

  • 期刊论文

  • 发表日期：

    2025年5月15日

查看全文
  • Di Xie,
  • Yanghong Dong,
  • Jinyu Chi,
  • Wanlin Li,
  • Chunnan Liu,
  • Yang Xu,
  • Yang Li,
  • Jingzhi Wang,
  • Jinfeng Wu,
  • Rui Wang,
  • Kelaier Yang,
  • Xinhua Yin

摘要

Research indicates that patients with salt-sensitive (SS) hypertension experience higher morbidity and target organ damage than in patients with non-SS hypertension. Dysregulated macrophage activation has been implicated in SS hypertension development, with lysine acetylation playing a role in modulating macrophage function. However, the role of macrophage acetylation patterns in SS hypertension remains unclear. This study aimed to investigate how acetylation regulates macrophage function and its role in the pathogenesis of SS hypertension. We employed quantitative acetylation proteomics to characterize the acetylome of bone marrow-derived macrophages in Dahl SS hypertensive rats fed either a high-salt or a low-salt diet. We identified 94 hyperacetylated and 49 hypoacetylated sites on 79 and 45 proteins, respectively, in the high-salt group. Notably, acetylation levels increased at lysine 20 (K20) and K46 on histone H2B, at K56 on H3, and at K77 and K79 on H4c2. We also identified conserved acetylation motifs, analyzed their Gene Ontology terms and pathways, and explored the protein–protein interactions of these differentially acetylated proteins using bioinformatics analyses. Finally, we validated the altered acetylation of H2, H3, H4, and several metabolic proteins using immunoprecipitation and western blotting. Overall, these findings offer insights into the role of lysine acetylation in macrophages from SS hypertensive rats, revealing potential therapeutic targets.

Graphical Abstract

Our analysis showed a landscape of lysine acetylation in bone marrow-derived macrophages (BMDMs) from salt-sensitive rats. Furthermore, we clearly identified significantly altered acetylated sites in low-salt and high-salt groups and validated the altered acetylation levels of several histones and metabolic proteins. IP, immunoprecipitation; TMT, tandem mass tag; LC–MS, liquid chromatography-mass spectrometry; HPLC, high-performance liquid chromatography.