The type 1 transmembrane glycoprotein B7‐H3 interacts with the glycolytic enzyme ENO1 to promote malignancy and glycolysis in HeLa cells

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Abstract
The role of the type 1 transmembrane glycoprotein B7‐H3 is controversial in tumorigenesis; thus, a better clarification of its involvement in cancer is crucial. In the present study, 79.3% of cervical cancer samples were found to be B7‐H3 positive and the expression of B7‐H3 was positively correlated with the clinical features of the samples. Silencing B7‐H3 using small interfering RNA or blocking it with intracellular ScFv attenuated the malignancy of HeLa cells. By pull‐down assay and liquid chromatography‐mass spectrometry in HeLa cells, the glycolytic enzyme ENO1 was found to interact with B7‐H3. Subsequently, the involvement of B7‐H3 in glycolysis was investigated. We observed decreases in the levels of ATP and lactate, as well as c‐Myc and lactate dehydrogenase A, upon B7‐H3 downregulation in HeLa cells. The results of the present study provide evidence for B7‐H3 mediating tumor glycolysis.
Funding Information
  • National Natural Science Foundation of China (8177102356)

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