PXD050342 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Systematic proteomics analysis of lysine acetylation reveals critical features of renal proteins in kidney calculi formation |
| Description | 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 revealed118 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 interaction network analyses revealed that the mitochondria were the most abundant acetylated protein fraction, and metabolic pathways were predominated among the GO and KEGG pathways. Furthermore, the LC-MS/MS findings were verified by immunofluorescence. The study is the first comparative study of Kac modification associated with kidney calculi. These findings offer significant insights into the molecular mechanism underlying the formation and development of renal stones. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-02-09 |
| AnnouncementXML | Submission_2026-02-08_16:34:25.348.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Qiong Deng |
| SpeciesList | scientific name: Rattus norvegicus (Rat); NCBI TaxID: NEWT:10116; |
| ModificationList | acetylated residue |
| Instrument | timsTOF Pro |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2024-03-04 18:11:50 | ID requested | |
| ⏵ 1 | 2026-02-08 16:34:26 | announced | |
Publication List
| Zhang S, Wang Z, Jiang H, Wang J, Jin M, Liang H, Deng Q, Systematic proteomics analysis of lysine acetylation reveals critical features of renal proteins in kidney calculi formation. PLoS One, 21(1):e0338641(2026) [pubmed] |
| 10.1371/journal.pone.0338641; |
Keyword List
| submitter keyword: Kidney calculi |
| Acetylation |
| Proteomics |
Contact List
| Qiong Deng |
|---|
| contact affiliation | the People’s Hospital of Longhua, Shenzhen |
| contact email | dengqiong1987@smu.edu.cn |
| lab head | |
| Qiong Deng |
|---|
| contact affiliation | the People’s Hospital of Longhua, Shenzhen |
| contact email | dengqiong1987@smu.edu.cn |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD050342
- Label: PRIDE project
- Name: Systematic proteomics analysis of lysine acetylation reveals critical features of renal proteins in kidney calculi formation
