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Samples underwent a series of solubilisation steps to generate a more soluble fraction 1 (F1; cellular compartment) and a matrix-enriched fraction 2 (F2; matrix compartment). 50µg of protein from each sample was prepared in 5% SDS to make a total volume of 50µL, and then acidified using 5µL of 12% H3PO4. 350µL binding buffer (90% methanol, 10% distilled water; 100 mM TEAB) was added and the samples loaded onto an S-Trap plate (ProtiFi) according to the manufacturer’s protocol. Bound proteins were washed in binding buffer and methyl tert-butyl ether (MTBE, Sigma) and digested overnight with 5g of sequencing-grade modified trypsin (Promega) at 37°C. Peptides were eluted from the column with 30% (vol/vol) acetonitrile and 0.1% (vol/vol) formic acid aqueous solution and collected by centrifugation at 4000g for 2 min. After desalting, the peptide samples were dried to completeness by vacuum centrifugation and submitted for analysis by mass spectrometry. Liquid chromatography (LC) separation was performed on a Thermo RSLC system consisting of an NCP3200RS nano pump, WPS3000TPS autosampler and TCC3000RS column. The LC system was coupled to a Thermo Exploris 480 mass spectrometry system via a Thermo Nanospray Flex ion source. Data was acquired in a data-dependent manner in profile mode."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectrometry analysis was carried out using a SILAC 1plex (Lys6) method in Proteome Discoverer (version 2.4) (Thermo Fisher Scientific). Raw spectra data were searched against the mouse Swiss-Prot database using the SEQUEST HT search tool. Identified proteins were required to have a minimum false discovery rate (FDR) of 1% and at least 2 unique peptides."],"omics_type":["Proteomics"],"labhead":["Rachel Lennon"],"instrument_platform":[""],"labhead_affiliation":["Manchester Cell-Matrix Centre, Division of Cell-Matrix Biology and Regenerative Medicine, The University of Manchester, UK"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["anna.hoyle@kennedy.ox.ac.uk"],"publication":["10.1016/J.MBPLUS.2026.100197"],"submitter_affiliation":["University of Oxford"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Kidney matrix dynamics across the life course","description":"Chronic kidney disease (CKD) represents a major public health concern and accounts for massive morbidity, mortality, and financial resource. Advanced age is a major risk factor for progressive CKD and is associated with kidney fibrosis. Dysregulated protein turnover is a hallmark of ageing and leads to matrix accumulation and abnormal matrix remodelling. As there are no current effective therapies to prevent or reverse kidney fibrosis, there is an urgent need to understand mechanisms that drive aberrant kidney matrix remodelling that occurs during ageing.  Using our established experimental workflow for global quantification of protein half-lives in the kidney, we pulse-labelled mice with 13C-Lysine and performed deep proteomic profiling across four time-points which spanned the physiological life course of mice. This approach enabled us to define the natural dynamics of protein turnover in the kidney and specifically examine the influence of development and ageing on kidney matrix dynamics.  This study provides novel insights into the mechanisms of matrix deposition during kidney maturation and begins to unravel the influence of physiological ageing on abnormal kidney matrix remodelling and accumulation. We identify several age-related proteolytic cascades which become dysregulated with age. Targeting early fibrotic remodelling of kidney matrix could help ameliorate inflammation and serve as a powerful tool in combating subsequent progression of age-related 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