Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
As more is learned about lactate, it acts as both a product and a substrate and functions as a shuttle system between different cell populations to provide the energy for sustaining tumor growth and proliferation. Recent discoveries of protein lactylation modification mediated by lactate play an increasingly significant role in human health (e.g., neural and osteogenic differentiation and maturation) and diseases (e.g., tumors, fibrosis and inflammation, etc.). These views are critically significant and first described in detail in this review. Hence, here, we focused on a new target, protein lactylation, which may be a "double-edged sword" of human health and diseases. The main purpose of this review was to describe how protein lactylation acts in multiple physiological and pathological processes and their potential mechanisms through an in-depth summary of preclinical in vitro and in vivo studies. Our work aims to provide new ideas for treating different diseases and accelerate translation from bench to bedside.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10777551 | PMC |
| http://dx.doi.org/10.1186/s12967-023-04842-9 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Integrative analysis of scRNA-seq and bulk RNA-seq to identify lactylation-related gene signatures in lung ischemia-reperfusion injury after lung transplantation.
Int Immunopharmacol
August 2025
Department of Anesthesiology, Shanghai Pulmonary Hospital, School of Medicine, Tongji University, Shanghai, China; Shanghai Engineering Research Center of Lung Transplantation, Shanghai, China. Electronic address:
Background: Protein lactylation has been implicated in stress-responsive cellular mechanisms, yet its role in lung transplantation-associated ischemia-reperfusion injury (IRI) remains undefined.
Methods: Transcriptomic profiles from GSE145989 were analyzed through differential expression analysis (limma) and weighted gene co-expression network analysis (WGCNA). Integrating the identified genes with lactylation-related signatures uncovered key lactylation-related genes (LRGs) as potential targets.
LncRNA BASP1-AS1 Drives PCBP2 K115 Lactylation to Suppress Ferroptosis and Confer Oxaliplatin Resistance in Gastric Cancer.
Free Radic Biol Med
September 2025
Department of General Surgery, Jiangnan University Medical Center, Wuxi, PR China. Electronic address:
In oxaliplatin-resistant gastric cancer (GC), multi-omics profiling combined with organoid libraries reveals altered metabolic pathways associated with chemoresistance. We identify a novel lactylation modification at K115 of Poly(RC)-binding protein 2 (PCBP2K115la), which confers functional oxaliplatin resistance. Mechanistic studies demonstrate that the long non-coding RNA BASP1-AS1 assembles a complex containing Unc-51 Like Autophagy Activating Kinase 1 (ULK1) and lactate dehydrogenase A (LDHA), thereby activating LDHA enzymatic activity to increase lactate production.
View Article and Find Full Text PDFLactylation modification in lung cancer: A review of current research and future directions (Review).
Oncol Rep
November 2025
Department of Lung Oncology, The Affiliated Hospital to Changchun University of Chinese Medicine, Changchun, Jilin 130021, P.R. China.
Lung cancer is a common malignancy that poses risks to human health and quality of life. The primary treatment options currently available include surgery, chemotherapy and radiotherapy. However, the aggressive metastatic nature of the disease combined with the development of drug and radiation resistance results in suboptimal survival outcomes.
View Article and Find Full Text PDFHK2-mediated augmentation of endothelial cell glycolysis promotes placental vascular disorders through lactylation and pyroptosis.
Acta Biochim Biophys Sin (Shanghai)
September 2025
Preeclampsia (PE) involves complex metabolic-inflammatory interactions, yet the mechanistic links among glycolysis, protein lactylation, and pyroptosis in placental pathogenesis remain undefined. In this study, we explore their tripartite relationship with PE development by combining bioinformatics analysis of PE-associated transcriptomes with experimental validation using placental tissues from PE patients and healthy controls. To elucidate the underlying mechanism, we utilize models involving hypoxic endothelial cell cultures, pharmacological glycolysis inhibition via 2-deoxyglucose, and genetic modulation of hexokinase 2 (HK2) expressions through siRNA silencing and plasmid-based overexpression.
View Article and Find Full Text PDFLactylation formation, gene regulation, biological functions, and clinical relevance.
Histol Histopathol
September 2025
Department of Cardiology, Affiliated Hospital of Zunyi Medical University, Zunyi, China.
Lactate, as an end-product of glycolysis, has been considered as a metabolic waste that participates in a few physiological functions. Recently, a novel study by Zhao's laboratory reported that lactate can serve as an epigenetic modification substrate, causing histone or nonhistone lysine residues to undergo lactylation, which then regulates gene transcription, translation, and protein function. Subsequent studies confirmed that lactylation plays an important role in a series of physiological and pathological processes, such as inflammation, cancer, and other biological processes.
View Article and Find Full Text PDF