{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/checksum.txt"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/Joseneto.mzid"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/Joseneto.DerivedFromSearch1addbb0f-3c8c-4dda-9c63-42c8fe5bf3dc.mgf"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/LC24_C.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/LC24_NOC.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/LC24_MON.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD073655/LC24_PTC.rar"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["labem@unifor.br"],"submitter":["Felipe Sousa"],"technology_type":["HDMSE","Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"disease":["Prostate Adenocarcinoma"],"software":["Not available"],"submitter_keywords":["Microtubule-targeting agents","Cytoskeleton proteins","Proteomics","Pterocarpans","Prostate cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073655"],"tissue":["Prostate Adenocarcinoma Cell","Epithelial Cell Of Prostate"],"sample_protocol":["PC-3 cells were treated with 8.0 µM (+)-PTC for 24 h. The same incubation time was used for the negative control (viz. 0.1% DMSO) and the two positive controls, namely monastrol (50 µM) and nocodazole (0.25 µM). All treatments were performed in duplicate and the samples pooled to reduce biological variation. The cells were harvested with trypsin for 10 min and lysates were transferred into 15 mL conical tubes. Lysis buffer (comprising 8 M urea, 75 mM NaCl, 50 mM Tris, pH 8.2) was added to each tube and one tablet of protease cocktail inhibitor (ex. Roche Diagnostics, Indianapolis, IN, USA) then added per 25 mL of buffer (VILLéN; GYGI). The cells were sonicated (60 s, 4 °C) three times at 2 min intervals using a sonicator operating at an output of 15% of maximum amplitude. Thereafter, the cells were centrifuged at 2,500 x g and 4 °C for 10 min so as to eliminate cellular debris and the supernatant then transferred into new tubes. The soluble protein concentration of each sample was then measured using the Qubit® system."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Quality control samples of PC-3 cells were comprised of one randomly selected sample from the negative control group which was divided into multiple aliquots. These were added to each sample preparation batch then processed and analyzed in parallel with the normal samples. Buffer exchange into 50 mM ammonium bicarbonate was carried out using spin columns (Millipore, USA) with a 5 kDa molecular cut-off. Disulfide bonds associated with the proteins were reduced using 100 mM dithiothreitol (Sigma, UK) at 60 °C for 0.5 h and the ensuing free sulfhydryl moieties were alkylated with 200 mM iodoacetamide (Sigma) in the dark at room temperature for 0.5 h. Proteins were submitted to tryptic digestion (Promega, USA) at a ratio of 1:50 (w/w trypsin/protein) for 17 h at 37 °C. Reactions were quenched through the addition of 8.8 M HCl (1:60 v/v ratio) to each sample that were then were stored at −80 °C and the extracted peptides were re-suspended in 0.1% aqueous formic acid (FA) solution. LC-MSE profiling was carried out in an ACQUITY UPLC M-Class SYNAPT G2-Si UPLC/MS/MS system (Waters, UK). Qualitative and quantitative proteomic analyses were performed in a bidimensional nano-UPLC tandem nano-ESI-MSE platform by multiplexed data-independent acquisition (DIA) experiments. The peptides (1 μg) were injected into a 2D-RP/RP Acquity UPLC M-Class System (Waters Corporation, Milford, MA) interfaced with a Synapt G2-Si mass spectrometer (Waters Corporation, Milford, MA). The samples were fractionated in first-dimension chromatography with an XBridge Peptide BEH C18 NanoEase Column (130 Å, 3.5 μm, 300 μm x 50 mm, Waters Corporation, Milford, MA). Peptide elution was performed using discontinuous steps of acetonitrile (11%, 14%, 17%, 20% and 50% acetonitrile) for 10 min at a flow rate of 2,000 nL/min. After each step, peptide loads were carried to a second-dimension separation using an ACQUITY UPLC HSS T3 nanoACQUITY column (100 Å, 1.8 μm, 75 μm x 150 mm, Waters Corporation, Milford, MA). Peptide elution was achieved using an acetonitrile gradient from 7% to 40% (v/v) for 54 min at a flow rate of 500 nL/min directly into a Synapt G2-Si. The equipment was operated in resolution mode with a m/z resolving power of about 35 000 FWHM using ion mobility with a cross-section resolving power of at least 40Ω/ΔΩ. The effective resolution obtained with the conjoined ion mobility was 1 800 000 FWHM. MS/MS analyses were performed by nano-electrospray ionization in positive ion mode nano-ESI (+) and a NanoLock Spray (Waters, Manchester, UK) ionization source. The lock mass channel was sampled every 30 sec. The mass spectrometer was calibrated with an MS/MS spectrum of [Glu1]-Fibrinopeptide B human (Glu-Fib) solution and was delivered through the reference sprayer of the NanoLock Spray source.  Data base search and proteome quantification  Progenesis QI V2.0 (QIfp) for proteomics (Nonlinear Dynamics/Waters, UK) was used for automated data processing and data base searching. The generated peptide masses were searched against in the UniProt species-specific protein sequence data base using the Progenesis QI V2.0 (QIfp) for proteomics for protein identification and quantification (Nonlinear Dynamics/Waters, UK). Feature extraction, chromatographic/spectral alignment, data filtering and statistical analyses were performed. All runs were selected for detection with an automatic detection limit. Features within RT ranges of 0–5 min and 45–65 min were filtered out as were features with charge ≥ + 8. A normalization factor was then calculated for each run to account for differences in sample loadings between injections. The experimental design was set up to group multiple injections from each run. The algorithm was then used to calculate and tabulate raw and normalized abundances, max fold change and ANOVA p values for each feature in the data set. The features were tagged in sets based on characteristics such as MS/MS > 1 and p < 0.01. The initial ion-matching requirements were ≧2 fragments per peptide, ≧5 fragments per protein and ≧1 peptide per protein. The enzyme specificity was defined by trypsin and one missed cleavage was allowed. For database searching the search parameters included: Variable modifications-Carbamidomethyl (Cys, fixed), Oxidation (Met, variable); peptide mass tolerance -  ± 20 ppm; fragment mass tolerance - ± 0.4 Da; and with Decoy searching used to define the false discovery rate (FDR). The significance threshold of the ion score was calculated based on a false discovery rate of ≤1%. The data were filtered to show only statistically significant differences (p < 0.05, ANOVA) coupled with a change in protein abundance by a 1.5-fold change or greater. Additionally, absolute quantification was performed using ADH as an internal standard so as to give an absolute amount of each identified protein/peptide."],"omics_type":["Proteomics"],"labhead":["Felipe Sousa"],"instrument_platform":[""],"labhead_affiliation":["University of Fortaleza"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["42318340 de Brito Vieira Neto J, Moraes de Farias K, Alves Sales SL, Melo VB, Nascimento Macêdo SM, Koscky Paier CR, Bezerra MJ, Moura AA, Carvalho HF, Domingos de Sousa F, Aquino A, de Oliveira Monteiro AC, Martins-de-Souza D, Banwell MG, Miranda Furtado CL, Pessoa C. The pterocarpan (+)-PTC modulates cytoskeletal proteins and induces apoptosis in metastatic castration-resistant prostate cancer: a proteomic perspective. Front Pharmacol. 2026 17:1770249 10.3389/fphar.2026.1770249"],"submitter_mail":["labem@unifor.br"],"submitter_affiliation":["University of Fortaleza"],"submitter_country":["Brazil"],"doi":["10.6019/PXD073655"],"pubmed_abstract":["Treatment of metastatic, castration-resistant prostate cancer (mCRPC) remains clinically challenging due to tumor heterogeneity and resistance to standard microtubule-targeting agents, such as docetaxel and cabazitaxel. The natural pterocarpan (+)-(6aS,11aS)-2,3,9-trimethoxypterocarpan [(+)-PTC] has previously shown selective cytotoxicity and disruption of bipolar spindle assembly in mCRPC PC-3 cells yet its full mechanism of action and global proteomic impact remain uncharacterized. PC-3 cells were treated with (+)-PTC (2.0 µM or 8.0 µM) for 24 h and assessed by flow cytometry (Annexin V and rhodamine 123) Western blot, and caspase-3/7 luminescence assays. Global proteomic profiling was performed by quantitative LC-MS/MS using a 2D nano-UPLC data-independent acquisition platform with nocodazole (0.25 µM, microtubule depolymerizer) and monastrol (50 µM, Eg5 inhibitor) as comparators. (+)-PTC-induced concentration-dependent apoptosis (19.8% early apoptotic cells at 2.0 µM; 26.1% at 8.0 µM) and progressive mitochondrial membrane depolarization. Western blot and caspase activities assays confirmed upregulation of BAX and caspase-7, consistent with intrinsic pathway activation. Proteomic analysis identified 212 differentially expressed proteins (DEPs) in (+)-PTC-treated cells, with over 80% overlap with nocodazole-treated cells (82% among upregulated and 84% among downregulated proteins), while clustering with monastrol was markedly lower. The top upregulated proteins, TTLL3, ANAPC7, PIK3CA, ARID4B, and COL16A1, are linked to microtubule dynamics and cell cycle regulation; the main downregulated, namely KDM2B, PTOV1, YWHAQ, PSMB6, and PRKCB, are involved in cell survival, protein homeostasis and mitotic checkpoint control. These findings provide proteomic evidence that (+)-PTC interferes with cytoskeletal protein dynamics and promotes apoptosis in mCRPC and so warranting its further investigation as a candidate anti-cancer scaffold."],"pubmed_title":["The pterocarpan (+)-PTC modulates cytoskeletal proteins and induces apoptosis in metastatic castration-resistant prostate cancer: a proteomic perspective."],"pubmed_authors":["de Brito Vieira Neto José J, Moraes de Farias Kaio K, Alves Sales Sarah Leyenne SL, Melo Vitoria Braga VB, Nascimento Macêdo Stella Maria SM, Koscky Paier Carlos Roberto CR, Bezerra Maria Júlia MJ, Moura Arlindo A AA, Carvalho Hernandes F HF, Domingos de Sousa Felipe F, Aquino Adriano A, de Oliveira Monteiro Ana Cristina AC, Martins-de-Souza Daniel D, Banwell Martin G MG, Miranda Furtado Cristiana Libardi CL, Pessoa Claudia C"],"additional_accession":[]},"is_claimable":false,"name":"The pterocarpan (+)-PTC mimics microtubule-destabilizing agents by modulating cytoskeletal proteins in metastatic castration-resistant prostate cancer: a proteomic perspective","description":"Treatment of metastatic castration-resistant prostate cancer (mCRPC) remains clinically challenging due to tumor heterogeneity and drug resistance. Microtubule-targeting agents are a mainstay of mCRPC therapy, but limitations persist regarding progression-free survival. Pterocarpans have emerged as promising anti-cancer agents, exerting effects through inhibition of bipolar spindle formation, cell cycle arrest in mitosis, and apoptosis induction. In this study, we evaluated the cytotoxic and proteomic effects of the natural product (+)-PTC in PC-3 cells and compared its activity to nocodazole (microtubule depolymerizer) and monastrol (Eg5 inhibitor). Flow cytometry after 24 hours of treatment with 8.0 µM (+)-PTC or 0.25 µM nocodazole revealed a ~50% reduction in cell proliferation relative to controls. Proteomic analyses (LC-MS/MS, GSEA, PANTHER) showed that (+)-PTC shares over 80% of differentially expressed proteins with nocodazole, with 82% overlap among up-regulated and 84% among down-regulated proteins. Top up-regulated proteins (TTLL3, ANAPC7, PIK3CA, ARID4B, COL16A1) are involved in microtubule dynamics and cell cycling; top down-regulated ones (KDM2B, PTOV1, YWHAQ, PSMB6, DPP6) impact cell survival and checkpoints. Differential expression analyses identified key regulators of mitosis and stress response. These findings nominate (+)-PTC as a candidate for future mCRPC 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