iProXProteomicsJuntao YangHomo Sapienshttp://www.iprox.org/page/project.html?id=IPX0008346000superyjt79@163.comPeking Union Medical CollegeiProX<h4>Purpose</h4>The hippocampus has long been associated with cognition and memory function, the implications of lysine lactylation (Kla), a recently identified post-translational modification (PTM), in the role of the hippocampus remain largely unexplored.<h4>Experimental design</h4>An LC-MS/MS bottom-up proteomics analysis of three human hippocampal tissue samples was applied to profile the lactylation map in human hippocampi under normal physiological conditions.<h4>Results</h4>We identified 2579 quantifiable Class I lactylated sites in 853 proteins, of which contained four types of modification motifs. Cellular localization analysis implies that a majority of lactylated proteins were distributed in the cytoplasm. Functional enrichment analysis showed that lactylated proteins were mainly involved in energy metabolic pathways. In addition, we found that the lactylation on histones exhibits a certain degree of conservation across different tissues. Compared with previously reported lactylation databases, 213 lactylated proteins were identified for the first time in this study.<h4>Conclusion and clinical relevance</h4>The first global lactylated proteins atlas of human hippocampi was reported in this study. Our work provides a reliable foundation for further research on lactylation in the hippocampus under physiological conditions.Global Profiling of Protein Lactylation in Human Hippocampi.Shi Chun-Mei CM, Wang Qiao-Chu QC, Li Xiao-Lu XL, Yang Ye-Hong YH, Tang Xiao-Yue XY, Wu Yue Y, Ding Tao T, Zhang Xu-Tong XT, Zhang Zhi-Yi ZY, Han Ron R, Kong Jie J, Liu Jiang-Feng JF, Yang Jun-Tao JTfalseGlobal profiling of protein lactylation in Human hippocampiLysine lactylation (Kla) is a novel posttranslational modification, playing important roles in numerous biological processes, including transcription, metabolism, tumorigenesis and nervous system diseases. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), researchers have identified lactylation in many human organs and other species, but no research on lactylation in human hippocampi has been reported. In this study, we performed global profiling of lactylation in human hippocampi under normal physiological conditions, and we identified 2579 Class I (localization probabilities > 0.75) lactylated sites in 853 proteins. Bioinformatics analysis showed that lactylated proteins were mainly located in the cytoplasm and involved in metabolic pathways and some neurological diseases. Compared with those reported lactylation databases, 434 lactylated proteins were identified for the first time in this study. Our work expands the database on human lactylation and helps advance the study on lactylation function and regulation under physiological and pathological conditions.Fri Mar 08 00:00:00 GMT 2024PXD050470960639610256