{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/IdentifiedAndQuantifiedProteins.tsv.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Results.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_PD_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_PD_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_HC_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_PD_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_HC_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_PD_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_HC_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/Neurons_HC_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066765/SearchPD-HC.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["cuda@unicz.it"],"submitter":["Caterina Gabriele"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Parkinson's Disease"],"software":[""],"submitter_keywords":["","Pka-creb pathway","Qvd-oph","Neurodegeneration","Synaptic function","Parkinson’s disease","Midbrain dopaminergic neurons","Apoptosis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066765"],"tissue":["Dopaminergic Neuron","Cell Culture"],"sample_protocol":["Proteomic profiling was performed on four biological replicates each from pooled HC (pHC) and sPD (pPD) mDA neurons, previously lysed as described for Western blotting. Ten micrograms of proteins, after reduction and alkylation, were then processed by Protein Aggregation Capture (PAC). Briefly, 5 µL of MagResyn Hydroxyl beads (100 µg) were equilibrated with two washes in 70% acetonitrile (ACN). Protein binding was induced by adding ACN to 70% final concentration, followed by 10 min incubation at 1100 rpm. The beads were washed three times in ACN and once in 70% ethanol, then resuspended in 50 µL of 50 mM triethylammonium bicarbonate (TEAB). Proteins were digested overnight at 37 °C with 200 ng of Trypsin-LysC (Pierce, Thermo Fisher) at a 1:50 enzyme-to-substrate ratio. Peptides were collected and residual material eluted with 50 µL of 0.1% formic acid. Harvested peptides were injected for LC-MS/MS analysis without further purification.Peptides were analyzed by nanoLC-MS/MS using an Orbitrap Exploris 480 mass spectrometer coupled to an Easy-nLC 1200 system (Thermo Fisher). Peptides were loaded onto a 17 cm in-house packed silica capillary column (75 µm i.d., 3 µm C18; Dr. Maisch). Separation was achieved using a binary gradient of mobile phase A (2% ACN, 0.1% FA) and mobile phase B (80% ACN, 0.1% FA) at 300 nL/min over 140 min: 3–25% B over 90 min, 25–40% over 30 min, 40–100% over 8 min, followed by 10 min at 100% B. The column was re-equilibrated at 0% B for 2 min. Data were acquired using data-independent acquisition (DIA) mode. Full scans were acquired at a resolution of 60,000, followed by 30 DIA scans at a resolution of 30,000 with 5e5 AGC target, 50 ms maximum injection time, and 25% normalized collision energy. DIA isolation windows consisted of 23 × 15 m/z, 4 × 30 m/z, and 3 × 50 m/z segments (0.5 m/z overlap) covering 350–1010 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw files were analyzed with Spectronaut (v18.7) using the Human 1 Protein 1 Gene database (20,577 sequences, March 2022). Quantitative analysis was performed using Perseus (v2.0.11.0). Protein abundances were log2-transformed and filtered to include only proteins detected in ≥3 replicates per group. Differentially expressed proteins (DEPs) were identified via two-sample t-tests with permutation-based FDR correction (FDR < 0.05; S0 = 0.2).A total of 6,414 proteins were identified, of which 443 were differentially expressed between pPD and pHC mDAs (|log2FC| > 1.5; q < 0.05)."],"omics_type":["Proteomics"],"labhead":["Giovanni Cuda"],"instrument_platform":[""],"labhead_affiliation":["Department of Experimental and Clinical Medicine, University of Catanzaro,Catanzaro (IT)"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["cgabriele86@gmail.com"],"publication":["42121856 Covello R, Benedetto GL, Scalise S, Gabriele C, Valente D, Zannino C, Puccio B, Quattrone A, Guzzi PH, Gaspari M, Quattrone A, Cuda G, Parrotta EI. Cytoskeletal Imbalance and Axonal Vulnerability in Sporadic PSP-RS: Early Changes in a Human iPSC-Derived Neuronal Model with Altered mTOR Signaling. Cells. 2026 15(9):754 10.3390/cells15090754"],"submitter_affiliation":["Università Magna Graecia di Catanzaro"],"submitter_country":["Italy"],"pubmed_abstract":["Progressive supranuclear palsy-Richardson's syndrome (PSP-RS) is a primary 4R tauopathy in which early axonal dysfunction may precede overt neurodegeneration; however, the mechanisms linking Tau dysregulation to cytoskeletal vulnerability remain poorly defined. Here, we generated induced pluripotent stem cell (iPSC)-derived midbrain dopaminergic neurons from individuals with sporadic PSP-RS and matched healthy controls and performed integrated transcriptomic and proteomic analyses. PSP-RS neurons exhibited coordinated suppression of dopaminergic and synaptic programs alongside activation of cytoskeletal remodeling and stress-related pathways. These changes were accompanied by increased Tau phosphorylation, neurofilament accumulation, and structural alterations of the axonal compartment, consistent with an early axonopathic phenotype. Notably, mechanistic target of rapamycin (mTOR) signaling significantly increased. Pharmacological inhibition of mTOR reduced Tau phosphorylation and neurofilament levels, indicating that mTOR activity contributes to the maintenance of cytoskeletal imbalance. In conclusion, our findings support a model in which early cytoskeletal dysfunction in PSP-RS arises from the convergence of Tau dysregulation, impaired structural homeostasis, and altered signaling pathways. Rather than acting as a primary driver, mTOR appears to function as a pathogenic amplifier that sustains axonal stress. This study provides a human cellular framework to investigate early axonopathic mechanisms in sporadic PSP-RS."],"pubmed_title":["Cytoskeletal Imbalance and Axonal Vulnerability in Sporadic PSP-RS: Early Changes in a Human iPSC-Derived Neuronal Model with Altered mTOR Signaling."],"pubmed_authors":["Covello Raffaele R, Benedetto Giorgia Lucia GL, Scalise Stefania S, Gabriele Caterina C, Valente Desirèe D, Zannino Clara C, Puccio Barbara B, Quattrone Andrea A, Guzzi Pietro Hiram PH, Gaspari Marco M, Quattrone Aldo A, Cuda Giovanni G, Parrotta Elvira Immacolata EI"],"additional_accession":[]},"is_claimable":false,"name":"Caspase inhibition restores dopaminergic identity through the PKA–CREB–BDNF axis in Parkinson’s disease neurons","description":"The progressive loss of dopaminergic identity in midbrain neurons is a hallmark of Parkinson’s disease (PD), contributing to synaptic dysfunction and neurodegeneration. However, the molecular mechanisms linking disease-specific stress to dopaminergic transcriptional failure remain poorly understood. Here, we used human induced pluripotent stem cell (hiPSC)-derived midbrain dopaminergic neurons (mDAs) from sporadic PD patients to investigate early alterations in neuronal identity, plasticity, and survival. We found that PD-derived mDAs exhibit upregulation of phosphorylated α-synuclein, marked reductions in dopaminergic markers (TH, NURR1), deficient dopamine handling and impaired synaptogenesis. Transcriptomic and protein analyses revealed sustained activation of apoptotic caspases (caspase-3, -7) and downregulation of the PKA–CREB–BDNF signaling axis, which underpins dopaminergic differentiation and synaptic maturation. Pharmacological inhibition of caspases with Q-VD-OPh restored pCREB, BDNF, and downstream dopaminergic markers, leading to morphological recovery and functional synaptic rescue. Inhibition of PKA with H89 abrogated these effects, positioning the caspase–PKA–CREB cascade as a critical regulator of dopaminergic identity in PD neurons. These findings define a novel non-apoptotic role for caspases in disrupting the transcriptional program of mDAs and identify a druggable pathway capable of rescuing key aspects of dopaminergic function in a patient-derived cellular model. This work provides a mechanistic rationale for targeting caspase signaling in early-stage 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