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eISSN: 1643-3750

S100A16 Regulates HeLa Cell through the Phosphatidylinositol 3 Kinase (PI3K)/AKT Signaling Pathway

Haibin Zhang, Yongxiu Yang, Xueyao Ma, Wenhu Xin, Xuefen Fan

The First School of Clinical Medicine of Lanzhou University, Lanzhou, Gansu, China (mainland)

Med Sci Monit 2020; 26:e919757

DOI: 10.12659/MSM.919757

Available online:

Published: 2020-01-02


BACKGROUND: S100 calcium-binding protein A16 (S100A16) is closely related to the onset and progression of tumors.
MATERIAL AND METHODS: In the research, the mainly purpose was to investigate the effect of S100A16 on the proliferation ability, invasion, and angiogenesis of HeLa cells. An adenoviral vector overexpressing S100A16 (Ad-S100A16) was constructed and transfected into HeLa cells, forming a stable cells line of overexpression. The effect of S100A16 on the proliferative capacity of HeLa cells was evaluated by a Cell Counting Kit-8 (CCK-8) assay. Cell migration capacity was determined by a Transwell migration assay. Changes in matrix metalloproteinase-2 (MMP-2), MMP-9, E-cadherin, and vimentin expression were evaluated by a cell-based immunofluorescence assay. The effect of S100A16 on angiogenesis was verified by knockout experiment.
RESULTS: Overexpression of S100A16 significantly enhanced the proliferative and migratory capacities of HeLa cells (P<0.05), upregulated expression of matrix MMP-2, MMP-9, vimentin, phosphatidylinositol 3 kinase, and phosphorylated protein kinase B, and downregulated expression of E-cadherin. Vascular endothelial growth factor expression increased, phosphatase and tensin homolog expression decreased, and angiogenesis was positively correlated with S100A16 expression. These effects were largely mediated by the activation of the phosphatidylinositol 3 kinase/protein kinase B pathways.
CONCLUSIONS: S100A16 could promote the proliferation, migration, and tumor angiogenesis of HeLa cells by regulating the phosphatidylinositol 3 kinase/protein kinase B signaling pathways.

Keywords: Cell Migration Assays, Cell Proliferation, Phosphatidylinositol 3-Kinases, Uterine Cervical Neoplasms



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