{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb_KO2_Slot2-20_1_2690.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb_KO4_Slot2-22_1_2694.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT4_Slot2-27_1_2705.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT1_Slot2-23_1_2697.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT3_Slot2-26_1_2703.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb_KO1_Slot2-19_1_2688.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb_KO3_Slot2-21_1_2692.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT2_Slot2-24_1_2699.mzML"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT4.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb03.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/2025June_ChengLab_Cdrive_search_Peaks13admin.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb02.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb01.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/WT2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069389/Kb04.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["chih-jen-cheng@uiowa.edu"],"submitter":["Chiao Hui Hsieh"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Bartter Disease Type 3"],"software":["Not available"],"submitter_keywords":["Mitochondria","Cell cycle","Metabolism","Bartter syndrome type 3","Clc-k2"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069389"],"tissue":["Distal Convoluted Tubule","Thick Ascending Limb Of Loop Of Henle","Kidney"],"sample_protocol":["The protein concentration was determined using the Qubit protein assay kit (Thermo Fisher Scientific, Q33212), and 20 µg of protein was used for downstream processing. To each sample, 0.1 M TCEP was added to achieve a final concentration of 5 mM, followed by alkylation with 10 mM CAA at 95°C for 10 minutes. Proteins were acidified with 43% phosphoric acid to a final concentration of 27.5% and then mixed with methanol/100 mM TEABC on ice for 5 minutes. The mixture was loaded onto S-Trap micro columns (ProtiFi LLC, C02-micro80) and centrifuged at 4,000 × g for 30 seconds; this process was repeated three times. The columns were washed three times with 90% methanol in 100 mM TEABC. Proteins were digested on columns with trypsin at 37°C for 16 hours. Peptides were eluted sequentially with 50 mM TEABC, 0.2% formic acid (FA), and 50% acetonitrile (ACN). Each sample was desalted using C18 Spin Tips (Thermo Fisher Scientific, ZJ394337). The dried peptides were resuspended in 50% trifluoroacetic acid (TFA) to adjust the pH to 2–3. C18 Tips were prewetted with 80% ACN/0.1% TFA and equilibrated with 0.1% TFA. The peptides were bound to the tips by aspirating and dispensing the solution three times, followed by washing with 0.1% TFA. Elution was performed using 20 µl of 70% ACN/0.1% TFA, which was also aspirated and dispensed three times. The eluates were centrifuged at 20,000 × g for 10 minutes, dried, and then resuspended in 3% ACN/0.1% FA for LC-MS analysis"],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peptide samples were analyzed on a timsTOF HT mass spectrometer (Bruker) coupled to a nanoElute2® UHPLC system (Bruker). Peptides were loaded onto a 25 cm × 150 µm ID analytical column packed with 1.5 µm C18 reverse-phase particles and separated using a linear gradient from 3% to 35% acetonitrile in 0.1% formic acid over 60 minutes at a flow rate of 500 nL/min. The column temperature was maintained at 50 °C. The mass spectrometer was operated in data-independent acquisition (DIA) mode using the diaPASEF method. Ion mobility separation was conducted over a range of 1/K₀ = 0.7 to 1.3 Vs/cm², and precursor ions were fragmented across a mass range of m/z 300–1700 using a set of overlapping isolation windows. Each cycle comprised 8 diaPASEF scans, with a total cycle time of approximately 0.95 seconds. The MS/MS spectral information was evaluated using PEAKS Studio software (Version 13, Bioinformatics Solution Inc.). Data files were used to query the uniport mouse database using the following parameters: The precursor and fragment mass tolerance are set to 20 ppm. The enzyme specificity was set to be semi-specific, meaning one end can be non-tryptic. Fixed modification was Carbamidomethylation. Variable modification was Deamidation (NQ) and Oxidation (M). Proteins with more than one unique peptide were selected for further analysis in both animal models. It was assumed that for all data, the treatment-over-control ratio of the proteins was normally distributed. Processed proteomics data were analyzed using RStudio (2025.02.28) with R (version 4.4.3, February 2025). Data were generally handled with tidyverse (v2.0.0) (4). A linear model for differential expression (DE) analysis was generated in limma (v3.62.2) (5) with disease group and technical batch as covariates in the design model. PCA was performed with PCAtools (v2.8.0) (6). Comparisons between Clc-k2-/- and wild-type controls were performed in limma with a moderated t-test, which was adjusted by Benjamini-Hochberg correlation. Pathway enrichment analysis was conducted using Ingenuity Pathway Analysis (IPA, version 01-23-01) on significantly differentially expressed genes (Log2Fold change >0.6 or <–0.6 and adjusted P-value < 0.05). Figures were plotted with ggplot2 (v3.5.2) (3) or complexheatmap (v2.22.0) (2) when applicable."],"omics_type":["Proteomics"],"labhead":["Chih-Jen Cheng"],"instrument_platform":[""],"labhead_affiliation":["Division of Nephrology, Department of Medicine Carver College of Medicine, University of Iowa"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["chiao-hui-hsieh@uiowa.edu"],"submitter_affiliation":["University of iowa"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Mitochondrial dysfunction underlies cell cycle arrest and tubular hypoplasia in ClC-Kb-deficient Bartter syndrome mice","description":"The pathogenesis of Bartter syndrome (BS) has long been attributed to decreased NaCl reabsorption in the thick ascending limb of Henle’s loop (TAL). By studying Clc-k2 (mouse ortholog of ClC-Kb)-knockout (Clc-k2-/-) mice, we recently uncovered an additional mechanism in which loss of transport function induces TAL hypoplasia, exacerbating the severity of BS. Here, we further investigated this mechanism. TALs and distal convoluted tubules (DCTs) isolated from Clc-k2-/- and wild-type mice were used for transcriptome, proteomics, and cell cycle and proliferation assays. Mitochondrial morphology and function were studied using electron microscopy and mitochondrial respiration assays. Our results revealed impairments in cell proliferation, S-to-G2/M cell cycle transition, mitochondrial biogenesis, oxidative phosphorylation, glycolysis, and fatty acid oxidation in Clc-k2-/- TALs and DCTs. Increasing transport activity by introducing a gain-of-function with-no-lysine 4 (Wnk4) mutation in Clc-k2-/- mice restored all the abovementioned impairments and improved medulla maturation and phenotype. Transgenic overexpression of Pgc1α, a master activator of mitochondrial biogenesis, in Clc-k2-/- mice also alleviated mitochondrial dysfunction and phenotype. These findings support the hypothesis that mitochondrial hypofunction resulting from decreased transport activity contributes to cell cycle arrest and tubular hypoplasia in BS. Targeting mitochondria early in life could be a potential therapeutic approach for 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