Systematic proteomics analysis of lysine acetylation reveals critical features of renal proteins in kidney calculi formation
Shiwei Zhang, Zhu Wang, Hao Jiang, Jieyan Wang, Meiyu Jin, Hui Liang, Qiong Deng, Murat Akand, Miloud Chakit, Miloud Chakit, Miloud Chakit
TL;DR
This study uses proteomics to explore how protein acetylation in rat kidneys is linked to kidney stone formation, identifying potential biomarkers and molecular mechanisms.
Contribution
The study is the first to compare lysine acetylation modifications in kidney calculi and normal kidneys, revealing novel insights into their molecular mechanisms.
Findings
118 proteins were downregulated and 129 upregulated in kidney calculi compared to normal kidneys.
538 upregulated and 133 downregulated lysine acetylation sites were identified in kidney calculi tissues.
Mitochondrial proteins and metabolic pathways were significantly enriched in acetylated proteins.
Abstract
In this study, we systematically integrated proteome and acetyl proteome (acetylome) approaches to investigate the characteristics of renal proteins in a CaOx crystal rat model. We aimed to understand the pathogenesis of kidney calculi and delineate the landscape of acetylation within kidney calculi, potentially leading to the identification of valuable and novel biomarkers. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), we analyzed the protein expression profiles and lysine acetylation (Kac) features in kidney tissues obtained from rats with kidney calculi and those without (normal controls). Our results revealed 118 downregulated and 129 upregulated proteins. Furthermore, we identified 538 upregulated Kac sites in 258 proteins and 133 downregulated Kac sites in 118 proteins between kidney calculi and paired normal rats. Functional enrichment and protein-protein…
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Taxonomy
TopicsKidney Stones and Urolithiasis Treatments · Pediatric Urology and Nephrology Studies · Bladder and Urothelial Cancer Treatments