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Quantification of lactylation in mouse peritoneal macrophages with or without stimulation of VSV by LS-MS/MS

ABSTRACT: Quantification of lactylation in mouse peritoneal macrophages with or without stimulation of VSV(12h) by LS-MS/MS, And lactylation peptides were enriched by Anti-Lactyllysine antibody conjugated agarose beads (PTM-1404, PTM Bio)

INSTRUMENT(S): Bruker Daltonics timsTOF series

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Peritoneal Macrophage, Macrophage

DISEASE(S): Disease Free

SUBMITTER: Qihang Zhao

LAB HEAD: Pin Wang

PROVIDER: PXD042171 | Pride | 2025-05-06

REPOSITORIES: Pride

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			Action	DRS
	FE139LPLaB1_C1_Slot2-5_1_21433.d.zip	Other
	FE139LPLaB1_C2_Slot2-6_1_21435.d.zip	Other
	FE139LPLaB1_C3_Slot2-7_1_21437.d.zip	Other
	FE139LPLaB1_V1_Slot2-8_1_21439.d.zip	Other
	FE139LPLaB1_V2_Slot2-9_1_21441.d.zip	Other

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Publications

Nonenzymatic lysine D-lactylation induced by glyoxalase II substrate SLG dampens inflammatory immune responses.

Zhao Qihang Q Wang Qiang Q Yao Qinghua Q Yang Zhengdong Z Li Wenfang W Cheng Xiaojie X Wen Yingling Y Chen Rong R Xu Junfang J Wang Xuanying X Qin Dexiang D Zhu Shuyang S He Liujie L Li Nan N Wu Yanfeng Y Yu Yizhi Y Cao Xuetao X Wang Pin P

Cell research 20250106 2

Immunometabolism is critical in the regulation of immunity and inflammation; however, the mechanism of preventing aberrant activation-induced immunopathology remains largely unclear. Here, we report that glyoxalase II (GLO2) in the glycolysis branching pathway is specifically downregulated by NF-κB signaling during innate immune activation via tristetraprolin (TTP)-mediated mRNA decay. As a result, its substrate S-D-lactoylglutathione (SLG) accumulates in the cytosol and directly induces D-lacty ...[more]

PMID: 39757301

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Project description:Cancer cells often rely on aerobic glycolysis for metabolism, and lactylation, a newly discovered post-translational modification, significantly impacts molecular processes. This study comprehensively analyzes lactylation's role in oral squamous cell carcinoma (OSCC), providing initial insights into its impact on progression. Six pairs of OSCC tissues underwent lactylation modification sequencing. 2,765 lactylation modification sites on 1,033 proteins were identified in OSCC, indicating its widespread presence. These modifications influenced metabolic activities, molecular synthesis, and transport.

2024-08-23 | PXD047673 | Pride

Global Profiling of Protein Lactylation Across Subcellular Fractionation Methods in HCT-116

Project description:Protein lactylation is a novel post-translational modification (PTM) involved in many important physiological processes such as macrophage polarization, immune regulation and tumour cell growth. However, most studies to date have focused on the function of lactylation on histones, and little is known about the distribution of lactylation on subcellular proteins. Here, we utilized subcellular fractionation methods to perform the global profiling of lactylation in human colon carcinoma HCT116 cells. This approach detected more unique lactylated proteins compared to the standard method when the amount of antibody and cells was equal. In total, 899 lysine lactylation sites were detected on 441 proteins, including 291 newly discovered lactylation sites and 63 newly lactylated proteins reported under the DDA and DIA acquisition modes. Functional enrichment analysis revealed that the majority of these proteins are involved in nucleosome assembly and slicesome function. For each subcellular fraction, the newly discovered lactylated proteins account for 10% to 20%. Notably, XPC not only has four new lactylation modification sites, but also one of which has been shown to be essential for the nucleotide excision repair process. Additionally, one of the newly discovered lactylation sites in scaffold attachment factor B1 (SAFB1) was found to be very important for the negative regulation of transcriptional activity. In conclusion, we describe a novel method that provides for understanding the characterization of subcellular lactylated proteins.

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Toxoplasma gondii; protein posttranslational modification; lactylation; metabolism; function

Project description:Toxoplasma gondii, a single-celled protozoan parasite (phylum Apicomplexa) and remains the causative pathogen of one of the most wide-spread infectious diseases, toxoplasmosis. To continuously proliferate in warm-blooded animals, this parasite undergoes repeated cycles of invasion, division and induction of host cell rupture. Lactate, which is derived from cellular metabolic pathways, is widely considered not only an energy source in organisms but also a regulatory molecule that participates in gene activation. Lysine lactylation is a new type of protein posttranslational modification (PTM) that was recently associated with chromatin remodeling, but the lysine lactylation of histone and nonhistone proteins has not yet been studied in parasites. To examine the prevalence and function of lactylation in T. gondii parasites, we mapped the lactylation proteome of proliferating tachyzoite cells and found 1,964 lactylation sites on 955 proteins in the T. gondii RH strain. The lactylated proteins were distributed in multiple subcellular compartments and were closely related to a wide variety of biological processes, including mRNA splicing, the citrate cycle (TCA cycle), aminoacyl-tRNA biosynthesis, glyoxylate and dicarboxylate metabolism, glycolysis/gluconeogenesis, oxidative phosphorylation, RNA transport and the HIF-1 signaling pathway. Lysine lactation might regulate numerous cellular processes to aid the establishment of a hospitable environment that allows the survival, replication and dissemination of the parasite. These study offers the first data of the global lactylation proteome and provides a basis for further functional dissection of important proteins associated with T. gondii development and pathogenicity.

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Systematic profiling of lysine lactylation proteome reveals distinct changes in lactylation between the parental AGS cells and cisplatin-resistant AGS cells

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2024-05-09 | PXD050906 | Pride

A Bioorthogonal Chemical Reporter for the Detection and Identification of Protein Lactylation

Project description:L-Lactylation is a recently discovered post-translational modification occurring on histone lysine residues to regulate gene expression. However, the substrate scope of lactylation, especially that in non-histone proteins, remains unknown, largely due to the limitations of current methods for analyzing lactylated proteins. Herein, we report an alkynyl-functionalized bioorthogonal chemical reporter, YnLac, for the detection and identification of protein lactylation in mammalian cells. Our in-gel fluorescence and chemical proteomic analyses show that YnLac is metabolically incorporated into lactylated proteins and directly labels known lactylated lysines of histones. We further apply YnLac to the proteome-wide profiling of lactylation, revealing many novel modification sites in non-histone proteins for the first time.

2022-06-23 | PXD033454 | Pride

Global Proteomic Analysis of Lysine lactylation in HMC3 cells under Normoxia or Hypoxia

Project description:This project carried out a quantitative study of lactylation in HMC3 Cell Line. In order to ensure a high degree of credibility of the results, we used the standard of localization probability>0.75 to filter the authentication data. In this study, a total of 3093 lactylation sites located on 1270 proteins were identified, of which 1601 sites of 751 proteins contain quantitative information. Subsequently, we carried out a systematic bioinformatics analysis of proteins containing quantitative information sites, including protein annotation, functional classification, functional enrichment and cluster analysis based on functional enrichment.

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Global profiling of protein lysine lactylation in hepatocellular carcinoma

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Identification of lysine-lactylated substrates in gastric cancer cells

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SILAC experiment quantifying the proteomics of WT and HBO1-KO HeLa

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