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三种不同消融技术前后心房颤动患者的血浆蛋白谱分析

Plasma protein profiling analysis in patients with atrial fibrillation before and after three different ablation techniques.

作者信息

Lin Menglu, Bao Yangyang, Du Zunhui, Zhou Yanting, Zhang Ning, Lin Changjian, Xie Yinyin, Zhang Ruihong, Li Qiheng, Quan Jinwei, Zhu Tingfang, Xie Yuan, Xu Cathy, Xie Yun, Wei Yue, Luo Qingzhi, Pan Wenqi, Wang Lingjie, Ling Tianyou, Jin Qi, Wu Liqun, Yin Tong, Xie Yucai

机构信息

Department of Cardiovascular Medicine, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

State Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, National Research Center for Translational Medicine at Shanghai, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.

出版信息

Front Cardiovasc Med. 2023 Jan 10;9:1077992. doi: 10.3389/fcvm.2022.1077992. eCollection 2022.

DOI:10.3389/fcvm.2022.1077992
PMID:36704472
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9871787/
Abstract

BACKGROUND

There are controversies on the pathophysiological alteration in patients with atrial fibrillation (AF) undergoing pulmonary vein isolation using different energy sources.

OBJECTIVES

We evaluated the changes in plasma proteins in acute phase post-ablation in patients receiving cryoballoon ablation, radiofrequency balloon ablation, or radiofrequency ablation.

METHODS

Blood samples from eight healthy controls and 24 patients with AF were taken on the day of admission, day 1, and day 2 post-ablation and analyzed by the Olink proximity extension assay. Proteins were identified and performed with enrichment analysis. Protein-protein interaction network and module analysis were conducted using Cytoscape software.

RESULTS

Of 181 proteins, 42 proteins in the cryoballoon group, 46 proteins in the radiofrequency balloon group, and 43 proteins in the radiofrequency group significantly changed after ablation. Most of the proteins altered significantly on the first day after ablation. Altered proteins were mainly involved in cytokine-cytokine receptor interaction. Both balloon-based ablations showed a similar shift toward enhancing cell communication and regulation of signaling while inhibiting neutrophil chemotaxis. However, radiofrequency ablation presented a different trend. Seed proteins, including osteopontin, interleukin-6, interleukin-10, C-C motif ligand 8, and matrix metalloproteinase-1, were identified. More significant proteins associated with hemorrhage and coagulation were selected in balloon-based ablations by machine learning.

CONCLUSION

Plasma protein response after three different ablations in patients with AF mainly occurred on the first day. Radiofrequency balloon ablation shared similar alteration in protein profile as cryoballoon ablation compared with radiofrequency ablation, suggesting that lesion size rather than energy source is the determinant in pathophysiological responses to the ablation.

摘要

背景

对于使用不同能量源进行肺静脉隔离的心房颤动(AF)患者,其病理生理改变存在争议。

目的

我们评估了接受冷冻球囊消融、射频球囊消融或射频消融的患者在消融急性期血浆蛋白的变化。

方法

在入院当天、消融后第1天和第2天采集8名健康对照者和24例AF患者的血样,并通过欧林克邻近延伸分析进行分析。鉴定蛋白质并进行富集分析。使用Cytoscape软件进行蛋白质-蛋白质相互作用网络和模块分析。

结果

在181种蛋白质中,冷冻球囊组有42种蛋白质、射频球囊组有46种蛋白质、射频组有43种蛋白质在消融后发生了显著变化。大多数蛋白质在消融后的第一天发生了显著改变。改变的蛋白质主要参与细胞因子-细胞因子受体相互作用。两种基于球囊的消融均显示出类似的变化趋势,即增强细胞通讯和信号调节,同时抑制中性粒细胞趋化性。然而,射频消融呈现出不同的趋势。鉴定出了包括骨桥蛋白、白细胞介素-6、白细胞介素-10、C-C基序配体8和基质金属蛋白酶-1在内的种子蛋白。通过机器学习在基于球囊的消融中选择了与出血和凝血相关的更显著的蛋白质。

结论

AF患者在三种不同消融后的血浆蛋白反应主要发生在第一天。与射频消融相比,射频球囊消融与冷冻球囊消融在蛋白质谱上有相似的改变,这表明病变大小而非能量源是消融病理生理反应的决定因素。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/eebd0f3ff15a/fcvm-09-1077992-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/38eb76e17ccb/fcvm-09-1077992-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/1648a5e97527/fcvm-09-1077992-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/03114185ecab/fcvm-09-1077992-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/ed0364a49dac/fcvm-09-1077992-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/e7d2a78b681e/fcvm-09-1077992-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/43b96321c6d3/fcvm-09-1077992-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/eebd0f3ff15a/fcvm-09-1077992-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/38eb76e17ccb/fcvm-09-1077992-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/1648a5e97527/fcvm-09-1077992-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/03114185ecab/fcvm-09-1077992-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/ed0364a49dac/fcvm-09-1077992-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/e7d2a78b681e/fcvm-09-1077992-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/43b96321c6d3/fcvm-09-1077992-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0c8f/9871787/eebd0f3ff15a/fcvm-09-1077992-g007.jpg

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