PXD062952 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Proteomic Characterization of the Rhesus Macaque Lens Nucleus: Similarity to Human Lens, Age Effects on Protein Solubility, and Trends in Posttranslational Modification |
| Description | Proteomes of lens nuclei from young (4 years old) and old (15-16 years old) rhesus macaques (Macaca mulatta) were analyzed to determine similarity of the proteomic profile to that of human lenses, age-related differences in protein solubility, and association of various posttranslational modifications with age and protein solubility. Lens core proteins were separated into water-soluble and water-insoluble fractions using aqueous buffer and centrifugation. The water-insoluble fraction was solubilized using SDS. Proteins were processed using S-trap columns and peptide digests were analyzed using high-resolution, label-free DDA proteomics. Open modification searches were performed using MSFragger to identify possible PTMs. The number of modified peptide tandem mass spectra confidently assigned to samples by age or solubility were compared to find PTMs with statistically significant count differences. The overall proteomic profile of rhesus macaque lenses was very similar to human lenses, consisting of 80.2% crystallins, 1.1% beaded filament proteins, and 18.7% other proteins. The crystallin fraction consisted of 27% alpha crystallins, 67.6% beta/gamma crystallins, and 5.4% taxon-specific psi crystallin. Glycolytic enzymes, beta/gamma crystallins, and a few glutathione-related enzymes were found to have age-related shifts to the water-insoluble fraction. There were significant differences in deamidation, dioxidation, carbamylation, carboxymethylation, and trioxidation based on age and/or solubility of proteins. |
| HostingRepository | PRIDE |
| AnnounceDate | 2025-09-16 |
| AnnouncementXML | Submission_2025-09-16_15:31:05.905.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Phillip Wilmarth |
| SpeciesList | scientific name: Macaca mulatta (Rhesus macaque); NCBI TaxID: 9544; |
| ModificationList | carbamoylated residue; phosphorylated residue; acetylated residue; monohydroxylated residue; formylated residue; deamidated residue; iodoacetamide derivatized residue |
| Instrument | Q Exactive HF |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2025-04-14 16:51:10 | ID requested | |
| ⏵ 1 | 2025-09-16 15:31:06 | announced | |
Publication List
| Hayden BL, Kelley O, Zientek K, Reddy AP, Wilmarth PA, Munds R, Montague MJ, Martinez MI, Wollstein G, Higham JP, Barron Arrambide AO, Danias J, Melin AD, David LL, Whitson JA, Proteomic Characterization of the Rhesus Macaque Lens Nucleus: Similarity to Human Lens, Age Effects on Protein Solubility, and Trends in Post-Translational Modifications. Invest Ophthalmol Vis Sci, 66(12):28(2025) [pubmed] |
| 10.1167/iovs.66.12.28; |
Keyword List
| submitter keyword: non-human primates, post-translational modifications, mass spectrometry, eye lens,Rhesus macaque, quantitative proteomics, aging |
Contact List
| Jeremy Whitson, Ph.D. |
| contact affiliation | Department of Biology Wanek School of Natural Sciences High Point University 1 N University Pkwy High Point, NC 27368 USA |
| contact email | jwhitson@highpoint.edu |
| lab head | |
| Phillip Wilmarth |
| contact affiliation | OHSU |
| contact email | wilmarth@ohsu.edu |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/09/PXD062952 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD062952
- Label: PRIDE project
- Name: Proteomic Characterization of the Rhesus Macaque Lens Nucleus: Similarity to Human Lens, Age Effects on Protein Solubility, and Trends in Posttranslational Modification