LMO2 attenuates glycolytic metabolism and facilitates cytotoxic T-lymphocyte infiltration in the tumor environment of lung and breast cancers

• Published in: Biochemical and biophysical research communications Vol. 675; pp. 170 - 176
• Main Authors: Wang, Wenhao, Meng, Yingying, Yu, Yanhong, Wang, Hang, Sun, Wei
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.10.2023
• Subjects: breast neoplasms; breasts; cytotoxicity; excretion; glucose; Glycolysis; Lactic acid; LMO2; lungs; T-lymphocytes; Tumor-infiltrating T Cells; Glycolysis; Lactic acid; LMO2; Tumor-infiltrating T Cells
• ISSN: 0006-291X; 1090-2104; 1090-2104
• DOI: 10.1016/j.bbrc.2023.07.024

Aerobic glycolysis preferentially exists in many cancer cells. LMO2 is an adaptor protein ubiquitously expressed in many epithelia and their malignancies, and it mediates broad-spectrum protein interactions. In this study, results showed that LMO2 directly interacted with glycolytic enzymes PGK1, PGAM1 and LDHA/LDHB, attenuated the glycolytic metabolism flow characterized by decreased glucose intake, ATP production and lactic acid excretion in lung and breast cancer cells, and was positively associated with of CD8+ T-lymphocyte infiltration in the tumor microenvironment. These findings reveal a novel role of LMO2 on modulating glycolysis in tumor cells and cytotoxic T-lymphocyte infiltration in the tumor microenvironment, which expands our knowledge of LMO2 in the field of solid tumors. [Display omitted] •LMO2 targets to key glycolytic enzymes PGK1, PGAM1 and LDHB via protein binding.•LMO2 generally attenuates intracellular glycolysis flow and lactate excretion in tumor cells.•LMO2 was specifically associated with CD8+ T-cell infiltration in human tumor datasets.•High LMO2 level in tumor cells leads to increased CD8+ T-cell infiltration in mouse tumor xenograft.