{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93_vsWT_hyp.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMTvsUntreated.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT3_run2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_hyp4_Run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_hyp4_Run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT4_Run2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_Hyp3_run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT2_run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_Hyp2_run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_hyp1_Run2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_hyp4_Run2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT2_run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT3_run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_Hyp2_run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT3_run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_Hyp3_run2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT4_Run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT2_run2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_hyp1_Run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_TMT4_Run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_Hyp3_run1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_hyp1_Run3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070931/SODG93A_Hyp2_run2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["viviana.greco@unicatt.it"],"submitter":["Viviana Greco"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Mitochondria","Proteomics","Als"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070931"],"tissue":["Brain"],"sample_protocol":["Sample preparation for mass spectrometry analysis Proteins obtained from hypothalamus and cerebellum (used as a control tissue) of 70-day old wild type and SOD1-G93A mice were used for proteomics analysis. Each protein sample, derived from the whole extracts, was subjected to protein digestion following the Filter-Aided Sample Preparation (FASP) protocol as described by Distler et al (10.1038/nprot.2016.042). Briefly, 50 µg of proteins resulting from each condition were reduced (DTT 8 mM in 8 M urea buffer and 100 mM Trizma Base), alkylated (IAA 50 mM in 8 M urea buffer and 100 mM Trizma Base) and then digested with trypsin (final trypsin concentration of 0.01 μg/μL) overnight at 37°C on Microcon Centrifugal Filter Devices (Merck Millipore Ltd., Cork, Ireland) LC-MS/MS analysis: Liquid chromatography-mass spectrometry (LC-MS) analysis were performed by an UltiMate 3000 RSLC nano – HPLC System (Thermo Fisher Scientific, Waltham, MA, USA) coupled with a high-resolution Orbitrap Fusion Lumos Tribrid Mass Spectrometer (Thermo Fisher Scientific) equipped with a Nanospray Flex source (Thermo Fisher Scientific). Specifically, Tryptic peptides (0. 5 μg) from each digested sample were loaded into a PepMap RSLC C18 column (2 μm, 100 Å, 50μm × 15 Cm; Thermo Scientific.) maintained at 40°C and then separated by a 155-minute reversed-phase gradient at 0,3 µL/min flow rate. Eluent A consisted of an aqueous solution of 0.1% FA, while eluent B was ACN with 0.1% FA. The gradient program was set as follows: 0% B and 100% A (min 0-110), 20% B and 80% A (min 110-120), 40% B and 60% A (min 120-125), 90% B and 10% A (min 125-145), 3% B and 97% A (min 145-155). The separated peptides were analyzed using an Orbitrap Fusion Lumos Tribrid mass spectrometer operating in positive ionization mode (2100 V), with fragmentation performed in a Higher-energy Collision Dissociation (HCD) cell and data acquired in Data-Dependent Acquisition (DDA) mode. The MS scan parameters were set as follows: Orbitrap resolution, 120,000; scan range (m/z), 350–1600. The MS/MS scan parameters were: Orbitrap resolution, 15,000. All samples were analyzed in analytical triplicates. Protein Identification and label free quantification:  MS raw data were analysed with the software Proteome Discoverer (v. 2.4.1). The qualitative identification of proteins was obtained by searching all reviewed proteins (Swiss-Prot) within the UniProt Mus Musculus reference proteome (ID: UP000000589, Taxon ID:10090). The search parameters used were set as follows: parent mass error tolerance automatic 10.0 ppm; fragment mass error tolerance 0.02 Da; minimum of 3 fragment ions matched per protein; minimum of 3 peptides matched per protein; maximum 2 missed cleavages. Carbamidomethylation of cysteines was set as a static modification, while oxidation of methionines, methionine loss, acetylation of lysines and N-terminal acetylation, were included as dynamic modifications. A false discovery rate (FDR) threshold of less than 1% was applied to the identification algorithm. The expression analysis was performed considering the technical replicates available for each experimental condition based on the hypothesis that each group was an independent variable. The list of differentially expressed proteins was screened according to a fold change of regulation higher than 20%. Only modulated proteins with p < 0.05 were considered significant."],"repository":["Pride"],"quantification_method":["Not available"],"modification":["4-tetrahydrothiazine-3-carboxylic acid",""],"data_protocol":["ggplot2 library in R3  (Wickham H (2016). ggplot2: Elegant Graphics for Data Analysis. Springer-Verlag New York. ISBN 978-3-319-24277-4, https://ggplot2.tidyverse.org.) and OmicScope4. (10.1038/s41467-024-50875-z.) Pathway analysis: Pathway analysis was conducted using Reactome Pathway Browser (v. 3.7)."],"omics_type":["Proteomics"],"labhead":["Viviana Greco"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Catholic University of the Sacred Heart"],"species":["Mus Musculus (mouse)"],"publication":["41932651 Scaricamazza S, Nesci V, Fenili G, Tiberi M, Percio A, Rosina M, Salvatori I, Riggio F, Candelise N, Pieroni L, Greco V, Chiurchiù V, Ferri A, Valle C. The hypothalamus is an early site of mitochondrial failure and neuro-immune circuit disruption in amyotrophic lateral sclerosis. Mol Metab. 2026:102360 10.1016/j.molmet.2026.102360"],"submitter_mail":["viviana.greco@unicatt.it"],"submitter_affiliation":["Catholic University of the sacred heart"],"submitter_country":["Italy"],"pubmed_abstract":["<h4>Background</h4>Metabolic dysfunction is a defining feature of amyotrophic lateral sclerosis (ALS), emerging early and strongly associated with disease progression and prognosis. While systemic hypermetabolism is well documented, the central mechanisms underlying energy imbalance remain poorly understood. The hypothalamus, a key regulator of whole-body energy homeostasis, has recently been implicated in ALS, but its mechanistic contribution to metabolic failure and disease progression remains unclear.<h4>Methods</h4>We analyzed the hypothalamus SOD1-G93A mouse model using proteomics (ProteomeXchange ID: PXD070931), mitochondrial bioenergetic assays, immunofluorescence, flow cytometry, and gene expression to assess hypothalamic mitochondrial function, glial activation, and melanocortin system integrity. Limited analyses in the hFUS model confirmed the presence of key hypothalamic alterations, supporting a shared vulnerability across ALS models. In SOD1-G93A mice, the metabolic modulator trimetazidine (TMZ) was administered presymptomatically to evaluate effects on hypothalamic pathology, metabolic regulation, disease onset, and survival.<h4>Findings</h4>We provide the first evidence that mitochondrial bioenergetic defects arise specifically in the hypothalamus of ALS models before symptom onset. Proteomic profiling revealed dysregulation of mitochondrial pathways, while functional assays confirmed impaired bioenergetics in the hypothalamus. These deficits were accompanied by local pro-inflammatory activation of astrocytes and microglia, mitochondrial dysfunction in glial cells, and early disruption of the arcuate nucleus melanocortin system. Limited analyses in hFUS mice confirmed selective hypothalamic vulnerability. Early TMZ treatment in SOD1-G93A mice specifically restored hypothalamic bioenergetics, normalized local glial activation and melanocortin signaling, delayed disease onset, and extended survival.<h4>Interpretation</h4>These findings establish the hypothalamus as an early and selectively vulnerable site in ALS, where region-specific mitochondrial dysfunction contributes to metabolic and neuroinflammatory alterations. Targeting hypothalamic bioenergetics represents a promising therapeutic strategy."],"pubmed_title":["The hypothalamus is an early site of mitochondrial failure and neuro-immune circuit disruption in amyotrophic lateral sclerosis."],"pubmed_authors":["Scaricamazza Silvia S, Nesci Valentina V, Fenili Gianmarco G, Tiberi Marta M, Percio Anna A, Rosina Marco M, Salvatori Illari I, Riggio Flaminia F, Candelise Niccolò N, Pieroni Luisa L, Greco Viviana V, Chiurchiù Valerio V, Ferri Alberto A, Valle Cristiana C"],"additional_accession":[]},"is_claimable":false,"name":"The hypothalamus is an early site of mitochondrial failure and neuro-immune circuit disruption in amyotrophic lateral sclerosis","description":"Given the hypothalamus central role in energy homeostasis and its emerging vulnerability in ALS, this study aimed to determine whether hypothalamic mitochondrial dysfunction may contribute to and potentially drive disease-related metabolic disturbances, thereby representing a potential therapeutic 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