{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_dbm2_Slot2-26_1_6667.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_db4_Slot2-24_1_6663.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_dbm3_Slot2-27_1_6669.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_dbm4_Slot1-39_1_6609.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_db1_Slot1-32_1_6599.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_db4_Slot1-35_1_6603.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_Results.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_db3_Slot2-23_1_6661.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_db1_Slot2-21_1_6657.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_db2_Slot1-33_1_6600.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_dbm4_Slot2-28_1_6671.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_db3_Slot1-34_1_6602.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_dbm2_Slot1-37_1_6606.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_Results.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_dbm3_Slot1-38_1_6608.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_db2_Slot2-22_1_6659.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734DA_dbm1_Slot1-36_1_6605.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067368/XB05734B1DPLa_dbm1_Slot2-25_1_6665.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["canwei528@hrbmu.edu.cn"],"submitter":["Can Wei"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Lactylome; proteome; protein lactylation; diabetic cardiomyopathy","Lactylome","protein lactylation","diabetic cardiomyopathy","proteome"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067368"],"tissue":["Heart"],"sample_protocol":["The DCM model was established using homozygous leptin receptor-deficient (db/db) mice, while heterozygous (db/m) mice served as the control group. All mice were raised on a normal diet under standard humidity and temperature. Both groups were maintained on a normal diet for 24 weeks. On the last day, the mice in the control group ( n=4 per group ) and DCM group ( n=4 per group) were sacrificed using CO2 anesthesia, and heart tissues were removed under sterile conditions for further detection."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Proteome, lactylome analysis by LC-MS/MS Analysis The tryptic peptides were dissolved in solvent A, directly loaded onto a home-made reversed-phase analytical column (25-cm length, 100 mm i.d.). The mobile phase consisted of solvent A (0.1% formic acid, 2% acetonitrile/in water) and  solvent B (0.1% formic acid in acetonitrile). Following the Proteome analysis, peptides were separated with following gradient: 0-5 min，9%-24%B；5-6 min，24%-35%B；6-7 min，35%-80%B；7-8 min，80%B, and all at a constant flow rate of 600 nl/minon a NanoElute UHPLC system (Bruker Daltonics). For the lactylome analysis, peptides were separated with following gradient: 0-14 min, 6%-22%B；14-16 min, 22%-30%B；16-17 min，30%-80%B；17-20 min，80%B, and all at a constant flow rate of 450 nl/minon a NanoElute UHPLC system (Bruker Daltonics). The peptides were subjected to capillary source followed by the timsTOF HT mass spectrometry. The electrospray voltage applied was 1.6 kV. Precursors and fragments were analyzed at the TOF detector. The timsTOF Pro was operated in data independent parallel accumulation serial fragmentation (dia-PASEF) mode. Following the Proteome analysis, the full MS scan was set as 300-1500 (MS/MS scan range) and 21PASEF MS/MS mode-MS/MS scans were acquired per cycle. The MS/MS scan range was set as 380-1170 and isolation window was set as10 m/z. For the lactylome analysis, the full MS scan was set as100-1700(MS/MS scan range) and 8PASEF (MS/MS mode)-MS/MS scans were acquired per cycle. The MS/MS scan range was set as 425-1025 and isolation window was set as25 m/z . Database Search  The data were processed using Spectronaut (v.18) software.Tandem mass spectra were searched against the Mus_musculus_10090_SP_20231220.fasta (17191 entries) concatenated with reverse decoy database. In proteome analysis, trypsin/P was specified as cleavage enzyme, allowing up to 2 deletions for cleavage, while in lactylome analysis, up to 4 deletions for cleavage are allowed. Carbamidomethyl on Cys was specified as fixed modification. Acetylation on protein N-terminal, and oxidation on Met were specified as variable modifications. The false discovery rates (FDRs) were set at <1% for peptide-spectrum matches and sites and protein identifications. The intensity-based quantification of protein groups was extracted from the MaxQuant result files to represent the expression of a particular protein across samples. The levels of Kla-peptides were calculated based on the raw spectral intensity. To eliminate the level changes of Kla-peptides caused by the dynamics of protein levels, the abundance of each identified Kla-peptide was normalized with the corresponding protein abundance."],"omics_type":["Proteomics"],"labhead":["Can Wei"],"instrument_platform":[""],"labhead_affiliation":["Harbin Medical University"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["42029413 Ma D, Cai W, Yuan H, Shi M, Jin Y, Cui Y, Liu P, Liu X, Wei C. Integrative Investigation of Lactylome-Proteome Interplay in Diabetic Cardiomyopathy for Pinpointing Disease Development-Associated Pathways or Proteins. J Diabetes Res. 2026 2026(1):e3543697 10.1155/jdr/3543697"],"submitter_mail":["canwei528@hrbmu.edu.cn"],"submitter_affiliation":["Harbin Medical University"],"submitter_country":["China"],"pubmed_abstract":["<h4>Background and aim</h4>Lysine lactylation (Kla) has emerged as a novel posttranslational modification implicated in various disease processes, yet its role in diabetic cardiomyopathy (DCM) pathogenesis remains unknown. The objective of this study was to ascertain whether protein lactylation is involved in DCM progression.<h4>Methods</h4>Proteomic and lactate analysis via liquid chromatography with tandem mass spectrometry was performed on the heart tissues of db/m mice (as the control group) and db/db mice (as the DCM group). Subsequently, a series of bioinformatics analyses was employed to analyze the Kla site and Kla-modified proteins in the two groups.<h4>Results</h4>Bioinformatics analysis revealed a greater abundance of Kla sites in the DCM group than in the control group. In addition, subcellular localization analysis indicated that Kla-modified proteins were predominantly located in the cytoplasm and mitochondria. Protein lactylation modification mainly occurred on histone H2, and in comparison to the control group, modification of the H4C1-K32 site was notably elevated in the DCM group. Furthermore, 113 significantly modified Kla sites were associated with 78 modified proteins in the DCM group, whereas 37 significantly modified Kla sites were associated with 25 modified proteins in the control group. These Kla-modified proteins participated in biological processes and pathways related to glucose metabolism and DCM. Finally, five candidate sites were identified using random forest, LASSO regression, support vector machine-recursive feature elimination, and logistic regression: A2ASS6_K928_Ttn, A2ASS6_K13499_Ttn, Q61425_K212_Hadh, Q8K2B3_K517_Sdha, and Q9R0Y5_K100_Ak1.<h4>Conclusions</h4>Our findings suggest that protein lactate modification in the lactylome and proteome could be a promising treatment for DCM. This provides a reliable basis for further investigating the roles of Kla and Kla-modified proteins to develop new and effective therapeutic targets for treating DCM."],"pubmed_title":["Integrative Investigation of Lactylome-Proteome Interplay in Diabetic Cardiomyopathy for Pinpointing Disease Development-Associated Pathways or Proteins."],"pubmed_authors":["Ma Di D, Cai Wenjie W, Yuan Hui H, Shi Meixin M, Jin Ye Y, Cui Yifeng Y, Liu Peng P, Liu Xi X, Wei Can C"],"additional_accession":[]},"is_claimable":false,"name":"Lactylation in Diabetic Cardiomyopathy","description":"Lysine lactylation (Kla), is a newly found post-translational modification that has been found to be involved in the pathogenesis of many diseases. However, the specific effect of protein lactylation has not been reported on the development of diabetic cardiomyopathy (DCM). Here, the purpose of this study was determined whether protein lactylation was involved in the progression of DCM. LC-MS/MS was used to perform proteomic and lactate analysis on the heart tissues of db/m mice (Control group) and db/db mice (DCM group). Subsequently, a series of bioinformatics analyses were used to analyze the kla site and Kla modified proteins in two groups, including GO enrichment, KEGG enrichment, LASSO regression, Logistic regression, random forest (RF), VM-Recursive Feature Elimination (SVM-RFE) algorithm, and other analysis methods. The bioinformatics data analysis showed that the Kla sites in the DCM group were more than those in the Control group. In addition, subcellular localization analysis showed that Kla modified proteins were mainly located in mitochondria and cytoplasm. The protein lactylated modification mainly occurred on histone H2, and compared with the Control group, the modification of H4C1-K32 sites was significantly higher in the DCM group. Furthermore, there were 113 significantly modified kla sites corresponding to 78 modified proteins in the DCM group, while there were 37 significantly modified kla sites corresponding to 25 modified proteins in the Control group. These Kla modified proteins were involved in biological processes and pathways related to glucose metabolism and DCM. Finally, five kla sites were selected as candidate sites by using four machine learning methods, namely A2ASS6 _ K928 _ Ttn, A2ASS6 _ K13499 _ Ttn, Q61425 _ K212 _ Hadh, Q8K2B3 _ K517 _ Sdha, and Q9R0Y5 _ K100 _ Ak1. In conclusions, the present study first reported on the combination of lactylome and proteome of DCM, providing a reliable basis for further investigating the roles of Kla and Kla modified proteins in 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