Proteomics

Dataset Information

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Lactylation of nucleus pulposus cells

ABSTRACT: Nucleus pulposus (NP) resides in hypoxic microenvironment due to the avascular structure of intervertebral disc (IVD). Intracellular lactate drives lysine lactylation (Kla) as a newly epigenetic modification. However, the impact of Kla on NPCs remains unknown. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), we showed a global lactylome profiling on NPCs cultured in normoxia and hypoxia environment and found that 3510 lactylation sites on 1052 proteins in NPCs on non-histone proteins. Moreover, there are 18 proteins with 129 Kla sites exclusively detected in the normoxia group, and 117 Kla sites in 27 proteins were specific in hypoxia group. Together, our dates reveals that Kla plays an important role in regulating cellular metabolism and may contribute to IDD progression.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Cell Culture

SUBMITTER: Jun Dai  

LAB HEAD: Jun Dai

PROVIDER: PXD048244 | Pride | 2025-05-06

REPOSITORIES: Pride

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Dataset's files

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Action DRS
AE141LPLa_HY1_Slot2-17_1_10726.d.zip Other
AE141LPLa_HY2_Slot2-18_1_10728.d.zip Other
AE141LPLa_HY3_Slot2-19_1_10730.d.zip Other
AE141LPLa_NC1_Slot2-14_1_10720.d.zip Other
AE141LPLa_NC2_Slot2-15_1_10722.d.zip Other
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Publications

Systematic analysis of lysine lactylation in nucleus pulposus cells.

Sheng Lei L   Xu Haoran H   Wang Yuexing Y   Ni Jinhao J   Xiang Taiyang T   Xu Huanhuan H   Zhou Xiaozhong X   Wei Kang K   Dai Jun J  

iScience 20241011 11

Nucleus pulposus (NP) resides in hypoxic microenvironment and NP cells (NPCs), primarily reply on glycolysis and producing high levels of lactate. Intracellular lactate drives lysine lactylation (Kla) as a newly epigenetic modification. However, the impact of Kla on NPCs remains unknown. Here, single-cell RNA sequencing (scRNA-seq) data suggested an altered balance between glycolysis and aerobic oxidation in intervertebral disc degeneration (IDD). Liquid chromatography-tandem mass spectrometry (  ...[more]

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