{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_KO_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_KO_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_WT_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_WT_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_KO_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_WT_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_KO_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/2021-09-13_MS_GG_Proteomics_Urine_WT_01.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD049984/txt.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["medina@tigem.it"],"submitter":["Diego L. Medina"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":[""],"submitter_keywords":["Mucolipidosis","Renal","Trmpl"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD049984"],"tissue":["Urine"],"sample_protocol":["All the experiments have been performed in a labeling free setting. Urine samples were processed using iST-BCT (Preomics). Instruments for LC MS/MS analysis consisted of a NanoLC 1200 coupled via a nano-electrospray ionization source to the quadrupole-based Q Exactive HF benchtop mass spectrometer (Michalski et al., 2011). Peptide separation was carried out according to their hydrophobicity on a home-made chromatographic column, 75m ID, 8Um tip, 350mm bed packed with Reprosil-PUR, C18-AQ, 1.9m particle size, 120 Angstrom pore size, using a binary buffer system consisting of solution A: 0.1% formic acid and B: 80% acetonitrile, 0.1% formic acid. Runs of 120 min after loading were used for proteome samples, with a constant flow rate of 300nl/min. After sample loading, run start at 5% buffer B for 5min, followed by a series of linear gradients, from 5% to 30% B in 90min, then a 10 min step to reach 50% and a 5 min step to reach 95%. This last step was maintained for 10 min. Q Exactive HF settings: MS spectra were acquired using 3E6 as an AGC target, a maximal injection time of 20ms and a 120,000 resolution at 200m/z. The mass spectrometer operated in a data dependent Top20 mode with sub sequent acquisition of higher-energy collisional dissociation (HCD) fragmentation MS/MS spectra of the top 20 most intense peaks. Resolution, for MS/MS spectra, was set to 15,000 at 200m/z, AGC target to 1E5, max injection time to 20ms and the isolation window to 1.6Th. The intensity threshold was set at 2.0 E4 and Dynamic exclusion at 30 seconds."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All experiments were performed in at least three independent biological replicates. Data are presented as mean ± e.v. Statistical analysis of two experimental groups was performed using parametric two-tailed Student's t test.  For mass spectrometry, all acquired raw files were processed using MaxQuant and the implemented Andromeda search engine. For protein assignment, spectra were correlated with the UniProt human database (v. 2023) including a list of common contaminants. Searches were performed with tryptic specifications and default settings for mass tolerances for MS and MS/MS spectra. Carbamidomethyl at cysteine residues was set as a fixed modification, while oxidations at methionine, acetylation at the N-terminus were defined as variable modifications. The minimal peptide length was set to seven amino acids, and the false discovery rate for proteins and peptide-spectrum matches to 1%. The match-between-run feature with a time window of 1 min was used. For further analysis, the Perseus software (1.6.2.3) was used and first filtered for contaminants and reverse entries as well as proteins that were only identified by a modified peptide. The LFQ Ratios were logarithmized, grouped and filtered for min. valid number (min. 3 in at least one group). Missing values have been replaced by random numbers that are drawn from a normal distribution. Two sample t-test was performed using FDR=0.05. Probability values (p) < 0.05 were considered statistically significant. To identify significant enriched GO terms, we utilized the 1D enrichment tool in Perseus. Data visualization was done in the statistical environment R. MS analyses of three independent samples for each experiment were performed. Peptides with Log2 Difference ≥ 1 and -Log p-value > 1.3 were considered significantly enriched."],"omics_type":["Proteomics"],"labhead":["Diego Medina"],"instrument_platform":[""],"labhead_affiliation":["TIGEM"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["medina@tigem.it"],"publication":["40168161 Grieco G, Montefusco S, Nusco E, Capuozzo A, Cervellini F, Polishchuk E, Bishop M, Miele A, D'Apolito L, La Vecchia C, Aurilia M, Schiavo M, Staiano L, Cesana M, Oberman R, Lynch AV, Musolino P, Trepiccione F, Grishchuk Y, Medina DL. TRPML-1 Dysfunction and Renal Tubulopathy in Mucolipidosis Type IV. J Am Soc Nephrol. 2025 36(4):587-601 10.1681/asn.0000000567"],"submitter_affiliation":["Telethon Institue of Genetics and Medicine (TIGEM)"],"submitter_country":["Italy"],"pubmed_abstract":["<h4>Background</h4>Loss-of-function mutations in the lysosomal channel transient receptor potential cation channel (TRPML-1) cause mucolipidosis type IV (MLIV), a rare lysosomal storage disease characterized by neurological defects, progressive vision loss, and achlorhydria. Recent reports have highlighted kidney disease and kidney failure in patients with MLIV during the second to third decade of life; however, the molecular mechanisms driving kidney dysfunction remain poorly understood.<h4>Methods</h4>A cross-sectional review of medical records from 21 patients with MLIV (ages 3–43 years) was conducted to assess kidney function impairment. In addition, we examined the kidney phenotype of MLIV mice at various ages, along with human kidney cells silenced for TRPML-1 and primary tubular cells from wild-type and MLIV mice. Immunohistology and cell biology approaches were used to phenotype nephron structure, the endolysosomal compartment, and inflammation. Kidney function was assessed through proteomic analysis of mouse urine and in vivo kidney filtration measurements.<h4>Results</h4>Of the 21 patients with MLIV, only adults were diagnosed with stage 2–3 CKD. Laboratory abnormalities included lower eGFR and higher levels BUN/creatine in blood and proteinuria. In MLIV mice, we observed significant alterations in endolysosomal morphology, function, and impaired autophagy in proximal and distal tubules. This led to the accumulation of megalin (LRP2) in the subapical region of proximal tubular cells, indicating a block in apical receptor–mediated endocytosis. In vivo and in vitro experiments confirmed reduced fluid-phase endocytosis and impaired uptake of ligands, including β-lactoglobulin, transferrin, and albumin in MLIV proximal tubular cells. Urine analysis revealed tubular proteinuria and enzymuria in mice with MLIV. In addition, early-stage disease was marked by increased inflammatory markers, fibrosis, and activation of the proinflammatory transcription factor NF-κB, coinciding with endolysosomal defects. Importantly, adeno-associated viral–mediated TRPML-1 gene delivery reversed key pathological phenotypes in MLIV mice, underscoring TRPML-1's critical role in kidney function.<h4>Conclusions</h4>Our findings link TRPML-1 dysfunction to the development of kidney disease in MLIV."],"pubmed_title":["TRPML-1 Dysfunction and Renal Tubulopathy in Mucolipidosis Type IV."],"pubmed_authors":["Grieco Giuseppina G, Montefusco Sandro S, Nusco Edoardo E, Capuozzo Antonella A, Cervellini Francesca F, Polishchuk Elena E, Bishop Martha M, Miele Antonio A, D'Apolito Luciano L, La Vecchia Claudia C, Aurilia Miriam M, Schiavo Michela M, Staiano Leopoldo L, Cesana Marcella M, Oberman Rebecca R, Lynch Anna V AV, Musolino Patricia P, Trepiccione Francesco F, Grishchuk Yulia Y, Medina Diego Luis DL"],"additional_accession":[]},"is_claimable":false,"name":"Mucolipidosis type IV links TRPML-1 to renal  tubulopatia","description":"Loss of function mutations in the lysosomal channel TRPML-1 cause Mucolipidosis type IV, a rare lysosomal storage disease (LSD) characterized by neurological defects, progressive vision loss  and achlorhydria.1–4 Recent reports described kidney disease and renal failure in MLIV patients in the second to the third decade of life5, although the molecular mechanisms underlying kidney disease and the physiological role of TRPML-1 in this organ remain unclear. By investigating kidney disease in the mouse model of TRPML-1 KO at different ages, we found an expansion of the lysosomal compartment and the accumulation of autophagic cargo during kidney disease progression. Also,  Proximal Tubular Cells (PTCs) from TRPML-1 KO kidneys showed endocytosis defects. In vivo tracing using fluorescent β-Lactoglobulin confirmed a dramatic reduction in apical endocytosis. Excretome analysis of urine revealed that the lack of TRPML-1 results in proteinuria and enzymuria. Interestingly, TRPML-1 KO kidneys present inflammation, preceding lysosomal defects, with a dramatic upregulation of the macrophage markers F4/80 and Galectin-3. Older TRPML-1 KO mice also shown signs of fibrosis. Importantly, we observed a rescue of lysosomal and inflammatory phenotypes in TRPML-1 KO kidneys  following AAV-mediated gene transfer of TRPML-1, providing direct evidence of the role of TRPML-1 in kidney function. Altogether, we demonstrate that TRPML-1 is a central player in apical endocytosis and absorptive function in PTCs, explaining kidney disease and opening novel therapeutic opportunities to prevent and treat these alterations in MLIV 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