Identification of lysine-lactylated substrates in gastric cancer cells.
Cancer
Cancer systems biology
Integrative aspects of cell biology
Molecular biology
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
15 Jul 2022
15 Jul 2022
Historique:
received:
31
01
2022
revised:
26
05
2022
accepted:
13
06
2022
entrez:
8
7
2022
pubmed:
9
7
2022
medline:
9
7
2022
Statut:
epublish
Résumé
Cancer cells tend to utilize aerobic glycolysis to generate energy and metabolites; the end product of aerobic glycolysis is lactate, which promotes lysine lactylation (Kla). Kla is a newly discovered histone post-translational modification (PTM) that plays important roles in regulating gene expression. However, Kla in non-histone mammalian proteins is unclear. Here, a comprehensive analysis of lactylated proteins in gastric cancer AGS cells was conducted. There were 2375 Kla sites found in 1014 proteins. Interestingly, KEGG pathway analysis showed that these proteins were significantly enriched in spliceosome function. In addition, Kla was more abundant in gastric tumors than in adjacent tissues, and high levels of Kla in gastric tumors were associated with poor prognosis. These results suggest that Kla could be a prognostic marker in gastric cancer. This lysine lactylome analysis in gastric cancer cells, the first of its kind, provides a valuable foundation for further studies of Kla.
Identifiants
pubmed: 35800753
doi: 10.1016/j.isci.2022.104630
pii: S2589-0042(22)00902-6
pmc: PMC9253728
doi:
Types de publication
Journal Article
Langues
eng
Pagination
104630Informations de copyright
© 2022 The Author(s).
Déclaration de conflit d'intérêts
The authors declare that they have no conflict of interest. Each listed author on the manuscript is aware of and agrees to the contents of the manuscript, including the authorship.
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