Proteomics

Dataset Information

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Whole-protein lactylation proteome analysis of rat nucleus pulposus tissues


ABSTRACT: Lactate accumulation is a hallmark and contributing factor of intervertebral disc degeneration (IVDD). Lactate accumulation facilitates protein lactylation, while the role and mechanism of protein lactylation in IVDD remain unclear. In this study, we performed sequencing of the lactylation sites of whole protein in nucleus pulposus tissues of 3 normal and 3 acupuncture induced intervertebral disc degeneration rats to explore the function of different lactylation sites and their effects on intervertebral disc degeneration.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Bone Marrow

SUBMITTER: Yuyao Zhang  

LAB HEAD: Changqing Li

PROVIDER: PXD072520 | Pride | 2026-04-13

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
RD266LPLaB4_RO_1_Slot1-38_1_9027.d.zip Other
RD266LPLaB4_RO_1_Slot1-38_1_9027.zip Other
RD266LPLaB4_RO_2_Slot1-39_1_9029.d.zip Other
RD266LPLaB4_RO_2_Slot1-39_1_9029.zip Other
RD266LPLaB4_RO_3_Slot1-40_1_9031.d.zip Other
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Publications

SOD1 lactylation impair its enzymatic activity by conformational change to aggravate intervertebral disc degeneration.

Zhang Yuyao Y   Zhai Yu Y   Liu Chao C   Chen Minghang M   Zhang Yang Y   Bian Zhiqun Z   Chang Xian X   Hu Zhilei Z   Li Jianmin J   Zhang Chao C   Ni Zhenhong Z   Xie Yangli Y   Chen Lin L   Liu Minghan M   Li Changqing C  

Nature communications 20260228 1


Lactate accumulation is a hallmark and contributing factor of intervertebral disc degeneration (IVDD), while the role of protein lactylation caused by lactate accumulation in IVDD remains unclear. Via metabolomics, single-cell RNA-sequencing analysis, and lactylation proteomics, we reveal the lactylome landscape in IVDD and identified superoxide dismutase 1 (SOD1) lactylation at lysine 123 (SOD1<sup>K123la</sup>) as crucial for IVDD aggravation. Using in vitro site-directed mutagenesis, in vivo  ...[more]

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