ArticleMolecular medicine reports2016
Differences in atrial fibrillation‑associated proteins between the left and right atrial appendages from patients with rheumatic mitral valve disease: A comparative proteomic analysis.
Article in Molecular medicine reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- Biomarkers and key pathways in atrial fibrillation associated with mitral valve disease identified by multi-omics study.Annals of translational medicine · 2021Article
- Molecular Signatures of Human Chronic Atrial Fibrillation in Primary Mitral Regurgitation.Cardiovascular therapeutics · 2021Article
- Proteomics and transcriptomics in atrial fibrillation.Herzschrittmachertherapie & Elektrophysiologie · 2018Review
- Dysregulation of the calcium handling protein, CCDC47, is associated with diabetic cardiomyopathy.Cell & bioscience · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of proteomic studies have focused on identifying atrial fibrillation (AF)-associated proteins in the right atrium (RA), thus potential differences in AF‑associated proteins between the RA and left atrium (LA) remain unknown. The aim of the present study was to perform proteomic analysis to compare the potential differences in AF‑associated proteins between the right atrial appendage (RAA) and left atrial appendage (LAA) in patients with rheumatic mitral valve disease (RMVD). RAA and LAA tissues were obtained from 18 patients with RMVD (10 with AF) during mitral valve replacement surgery. Two‑dimensional fluorescence difference gel electrophoresis (2‑D DIGE) proteomics analysis was performed using these tissues to identify AF‑associated proteins in RAA and LAA. Subsequently, the proteomics data was validated using western blot analysis of nine selected proteins. In RAA, 32 AF‑associated proteins were significantly dysregulated (15 upregulated and 17 downregulated). In LAA, 31 AF‑associated proteins were significantly dysregulated (13 upregulated and 18 downregulated). Among these AF‑associated proteins, 17 were AF‑associated in both RAA and LAA, 15 were AF‑associated only in RAA, and 14 were AF‑associated only in LAA. Amongst the differentially expressed proteins, western blot analysis validated the results for 6 AF‑associated proteins, and demonstrated similar distributions in RAA and LAA compared with the 2‑D DIGE results. Of these proteins, 2 proteins were AF‑associated in both RAA and LAA, 2 were AF‑associated only in RAA, and 2 were AF‑associated only in LAA. Additionally, the different distributions of AF‑associated proteins in the RAA and LAA of patients with RMVD was analyzed, which may reflect the different regulatory mechanisms of the RA and LA in AF. These findings may provide new insights into the underlying molecular mechanisms of AF in patients with RMVD.
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