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Hoyle"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Top-down proteomics"],"disease":["Alport Syndrome"],"software":[""],"submitter_keywords":["Turnover","Alports","Ecm","Kidney"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067091"],"tissue":["Kidney"],"sample_protocol":["For the pulse-time experiments, wildtype mice were pulse-labelled with 13C-Lys (heavy diet) for 1-, 2, 4- or 8-weeks and were sacrificed at 22 weeks for tissue harvesting (see Figure 2B). For the Alport syndrome study, mice were fed either 4- or 8-week pulses of 13C-Lys diet and were sacrificed aged 16 weeks for tissue harvesting (see Figure 3A). Frozen-thawed kidneys were placed in a glass dish and cut into small pieces (<1mm3) and washed three times. To solubilise the kidney, 200l of SL-DOC buffer (1.1% (vol/vol) sodium dodecanoate; 0.3% (vol/vol) sodium deoxycholate; 25mM ammonium bicarbonate; 0.5mM dithiothreitol (DTT); protease and phosphate inhibitors as per manufacturer’s guidance; pH 7) was added to the kidney tissue along with six 1.6mm steel beads. Samples were homogenised at maximum speed for 5 minutes at 4oC. This sample was designated soluble fraction 1 (F1; cellular compartment). Remaining pellets were further solubilised using 75l of High Salt Buffer (3M sodium chloride (Sigma); 25mM DTT (Sigma); 25mM ammonium bicarbonate (Sigma), protease and phosphate inhibitors as per manufacturer’s guidance (Sigma); pH 7) and further homogenised using a bullet blender at maximum speed for an additional 5 minutes. Following centrifugation the pellets were sonicated in 300l of Lysis buffer (5% sodium dodecyl sulphate (Sigma); 50mM triethylammonium bicarbonate (TEAB) (Sigma); pH7) supplemented with protease and phosphatase inhibitors. To generate the matrix-enriched fraction 2 (F2; matrix compartment), the supernatants from the High Salt and Lysis buffer extractions were pooled.  Samples were reduced with DTT, alkylated with IAA and quenched with DTT. 50µg of protein from each sample was prepared in 5% SDS and acidified with H3PO4. 350µL binding buffer (90% methanol, 10% distilled water; 100mM 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 then digested overnight at 37oC with 5µg of trypsin in Digestion buffer (50mM TEAB; 0.1% formic acid, FA, Sigma; at pH 8.5). Peptides were eluted from the column in Digestion buffer, 0.1% FA in distilled water, and finally with 0.1% FA, 30% acetonitrile in water. Peptides were desalted using Oligo R3 resin beads, according to the manufacturer’s protocol, in a 96-well, 0.2µm polyvinylidene fluoride  filter plate . The immobilised peptides were washed twice with 0.1% FA prior to elution in 2x 50µL 0.1% FA with 30% ACN, and lyophilisation using a speed-vac. Peptides were resuspended in 10µl 0.1% FA in 5% ACN. Liquid chromatography (LC) separation was performed on a Thermo RSLC system consisting of an NCP3200RS nano pump, WPS3000TPS autosampler and TCC3000RS column oven configured with buffer A as 0.1% (vol/vol) FA in water and buffer B as 0.1% (vol/vol) DA in ACN. The analytical column (Waters nanoEase M/Z Peptide CSH C18 Column, 130Å, 1.7µm, 75µm x 250mm) was kept at 35°C and at a flow rate of 300nL/minute for 8 minutes. The injection valve was set to load before a separation consisting of a 105-minute multistage gradient ranging from 2-65% of buffer B. The LC system was coupled to a Thermo Exploris 480 mass spectrometry system via a Thermo Nanospray Flex ion source. The nanospray voltage was set at 1900V and the ion transfer tube temperature set to 275°C. Data was acquired in a data-dependent manner using a fixed cycle time of 2 seconds, an expected peak width of 15 seconds and a default charge state of +2. Full mass spectra were acquired in positive mode over a scan range of 300 to 1750Th, with a resolution of 120000, a normalised automatic gain control (AGC) target of 300% and a maximum fill time of 25ms for a single microscan. Fragmentation data was obtained from signals with a charge state of +2 or +3 with an intensity over 5000 and they were dynamically excluded from further analysis for a period of 15 seconds after a single acquisition within a 10-ppm window. Fragmentation spectra were acquired with a resolution of 15000, a normalised collision energy of 30%, an AGC target of 300%, a first mass of 110Th, and a maximum fill time of 25ms for a single microscan. All data was collected in profile mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry analysis was carried out using a SILAC 1plex (Lys6) method in Proteome Discoverer (version 3.2) (Thermo Fisher Scientific). Carbamidomethylation of cysteine was selected as a fixed modification and variable modifications included oxidation of methionine, hydroxylation of proline and phosphorylation of threonine, serine, and tyrosine. A maximum of 2 missed cleavages per peptide was allowed. The minimum precursor mass was set to 350 Da with a maximum of 5000 Da. Precursor mass tolerance was set to 10 ppm, fragment mass tolerance was 0.02 Da and minimum peptide length was 6. Peptides were searched against the mouse Swiss-Prot database with additional TreEMBLl matrix protein sequences (unreviewed) 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. Known contaminants were removed. Abundance was calculated from the MS1 ion current peaks and combined for both heavy and light channels. Values were exported to Perseus (version 2.0.11.0) for further analysis, proteins were filtered for those with at least 3 calculated abundances, normalised by median subtraction (either to all proteins or, for F2, to matrisome proteins) and then missing data was imputed based on standard deviation. Heavy-to-light ratios were determined using the abundance of a protein detected in the heavy channel, containing 13C-lysine, compared to the light channel."],"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"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["10.1016/J.CELREP.2026.117356"],"submitter_mail":["anna.hoyle@kennedy.ox.ac.uk"],"submitter_affiliation":["University of Oxford"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Basement membrane turnover and circulating matrix biomarkers in kidney disease","description":"Chronic kidney disease (CKD) is characterised by kidney fibrosis and represents a major public health concern. Alport syndrome, a common monogenic cause of kidney failure caused by genetic variants in the type IV collagen genes COL4A3, COL4A4 or COL4A5, leads to abnormal basement membrane remodelling and kidney fibrosis. Understanding the dynamics and mechanisms of kidney matrix remodelling is crucial for directing emerging gene therapies and developing non-invasive biomarkers to detect and stage kidney fibrosis earlier, ultimately enabling risk stratification and timely intervention. To define the temporal and spatial dynamics of kidney matrix remodelling, we applied a multi-omics strategy in a Col4a5-/- mouse model of X-linked Alport syndrome, integrating stable isotope metabolic labelling, deep proteomic profiling, bulk RNA sequencing, super-resolution imaging, and bioinformatic prediction. Transcriptomic profiling identified enrichment of extracellular matrix degradation pathways and upregulation of matrix proteases. 13C-Lysine labelling coupled with mass spectrometry revealed altered abundance and accelerated turnover of basement membrane components in Alport kidneys. Super-resolution imaging confirmed spatial disorganisation of matrix proteins, supporting a loss of structural integrity. Using peptide location fingerprinting, we mapped damage modifications and predicted fragmentation in ~40 kidney matrix proteins, including collagens, laminins and nidogens. Targeted assays validated the presence of these predicted matrix fragments in serum from children with COL4A3–5 variants, demonstrating detectable alterations in circulating basement membrane peptides compared to healthy controls. These data define an uncoupling of matrix synthesis and degradation as a hallmark of Alport-associated kidney fibrosis. Our integrative approach establishes a framework for linking matrix proteolysis and basement membrane fragmentation with clinically accessible biomarkers of kidney matrix remodelling. The detection of circulating matrix fragments offers a promising non-invasive strategy to monitor basement membrane integrity and stage kidney fibrosis, with potential utility in both diagnosis and therapeutic response assessment in Alport syndrome and broader CKD contexts.","dates":{"publication":"2026-05-21","submission":"2025-08-07"},"accession":"PXD067091","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902"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