{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/md5sum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/Hk15XF_YY3_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/Hk15XF_HS2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/Hk15XF_YY1_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/Hk15XF_HS1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/Hk15XF_YY2_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/Hk15XF_HS3_3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/MD5Summer.exe","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067686/20241125_135012_sp_MJ20241113312_PP20241118871.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["1312221775@qq.com"],"submitter":["hanyu cao"],"technology_type":["Mass Spectrometry","Top-down proteomics","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Longissimus dorsi muscle","Huoshou black pig","Proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067686"],"tissue":["Longissimus"],"sample_protocol":["Take out the LD samples in the frozen state and put it on ice. The samples were suspended in protein lysis buffer (8M urea,1% SDS) which included appropriate protease inhibitor to inhibit protease activity and the mixture were treated by high-flux tissue grinding machine for 3 times,180s each. Then, the non-contact cryogenic sonication was performed for 30 min. After centrifugation at 16000g at 8°C for 30min, the concentration of protein from the supernatant collected was determined by Bicinchoninic acid (BCA) method by BCA Protein Assay Kit（Thermo Scientific). Protein quantification was performed according to the kit protocol. After protein quantification, SDS-PAGE electrophoresis was performed.  100 μg protein re-suspended with Triethylammonium bicarbonate buffer(TEAB) which with the final concentration of 100mM. The mixture was reduced with Tris(2-carboxyethyl)phosphine (TCEP) which with the final concentration of 10mM at 37 °C for 60min and alkylated with iodoacetamide (IAM) which with the final concentration of 40mM at room temperature for 40min in darkness. After centrifugation at 10000g at 4°C for 20min, the pellet was collected, which re-suspended with 100 μL Triethylammonium bicarbonate buffer(TEAB) which with the final concentration of 100mM. Trypsin was added at 1:50 trypsin-to-protein mass ratio and incubated at 37 °C overnight.  After trypsin digestion, the peptides were dried by vacuum pump. Then, the enzymatically drained peptides were re-solubilized with 0.1% trifluoroacetic acid (TFA), and the peptides were desalted with HLB and dried by vacuum concentrator. Finally, the peptides were quantified using the NANO DROP ONE(Thermo Scientific) by UV absorption value."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Based on peptide quantification results, the peptides were analyzed by an VanquishNeo coupled with an Orbitrap Astral mass spectrometer (Thermo, USA) at Majorbio Bio-Pharm Technology Co. Ltd. (Shanghai, China). Briefly, the uPAC High Throughptu column (75 μm×5.5 cm, Thermo, USA) was used with solvent A (water with 2% ACN and 0.1% formic acid) and solvent B ( water with 80% ACN and 0.1% formic acid). The chromatography run time was set to 8 minutes. Data-independent acquisition (DIA) data were acquired using an Orbitrap Astral mass spectrometer operated in DIA mode. The mass spectrometry scanning range was 100-1700 m/z.  DIA data was performed using Spectronaut (Version 19) with the Sus scrofa UniProt database (UP000008227, release 20230103; containing 47,945 protein sequences). The parameters are as follows up : The peptide length range was set to 7-52；Enzyme cutting site was trypsin/P；The maximum missed cleavage site was 2；Carbamidomethylation of cysteines as fixed modification, and oxidation of methionines and protein N-terminal acetylation as variable modifications；Protein FDR≤0.01，Peptide FDR≤0.01，Peptide Confidence ≥99%，XIC width≤75ppm. The protein quantification method was MaxLFQ."],"omics_type":["Proteomics"],"labhead":["Hanyu Cao"],"instrument_platform":[""],"labhead_affiliation":["College of Animal Science, Anhui Science and Technology University, Chuzhou 239000, China"],"submission_type":["PARTIAL"],"species":["Sus Scrofa Domesticus (domestic Pig)"],"submitter_mail":["1312221775@qq.com"],"publication":["42060591 Cao H, Li X, Xie F, Jiang C, Jin M, Ghonaim AH, Ren M, Hu Q, Li S. Quantitative proteomic analysis of longissimus dorsi muscle in Chinese and Western pigs using DIA mass spectrometry with PRM validation. PLoS One. 2026 21(4):e0346519 10.1371/journal.pone.0346519"],"submitter_affiliation":["College of Animal Science, Anhui Science and Technology University, Chuzhou 239000, China"],"submitter_country":["China"],"pubmed_abstract":["Huoshou black pig (HS) is a well-known indigenous Chinese breed distinguished by superior meat quality compared to Western breeds. To investigate the molecular mechanisms underlying these differences, we performed Data-Independent Acquisition(DIA) proteomic analysis on the longissimus dorsi (LD) muscle from HS and Yorkshire (YY) pigs. We identified 262 differentially expressed proteins (DEPs), including 134 upregulated and 128 downregulated in HS relative to YY. Functional enrichment analysis revealed that these DEPs were significantly involved in small molecule metabolism, oxidoreductase activity, and several key signaling pathways such as the mTOR, AMPK, and PI3K-Akt pathways. Protein -protein interaction network analysis highlighted roles in structural proteins, glycolysis, and ribosome biogenesis. Integrated transcriptomic and proteomic analysis identified five candidate genes (MGST2, PNPO, CALD1, NCAM1, ACSS1) potentially associated with meat quality traits. Parallel reaction monitoring (PRM) and quantitative PCR (qPCR) validated the consistent differential expression of these genes at both the protein and mRNA levels. These findings provide novel insights into the molecular mechanisms regulating pork quality in indigenous pig breeds."],"pubmed_title":["Quantitative proteomic analysis of longissimus dorsi muscle in Chinese and Western pigs using DIA mass spectrometry with PRM validation."],"pubmed_authors":["Cao Hanyu H, Li Xiaojin X, Xie Fei F, Jiang Changsheng C, Jin Mengmeng M, Ghonaim Ahmed H AH, Ren Man M, Hu Qianqian Q, Li Shenghe S"],"additional_accession":[]},"is_claimable":false,"name":"Huoshou black pig (HS) and Yorkshire (YY) proteomic data","description":"Conducted Data-Independent Acquisition (DIA) proteomic analysis on the longissimus dorsi (LD) muscle from HS and YY 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