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. 2026 Sep 25;16:1965794. doi: 10.3389/fonc.2026.1965794

Correction: The interaction of CDH20 With β-catenin inhibits cervical cancer cell migration and invasion via TGF-β/Smad/SNAIL mediated EMT

Chao Li 1,†,*, Hongfeng Ao 2,†, Guofang Chen 1, Fang Wang 3, Fang Li 1,3,*
PMCID: PMC13650751  PMID: 42857002

There was a mistake in Figure 3 as published. Incorrect vertical axis scales were provided for “panels E and F” of Figure 3. The corrected Figure 3 appears below.

Figure 3.

Panel figure with six parts labeled A through F comparing the effects of CDH20 overexpression versus vector control in cell lines. Panel A shows a western blot with higher CDH20 protein levels in the CDH20 lane, while GAPDH is similar in both. Panel B presents a bar graph of cell number over time (24, 48, 72 hours) showing a significant increase at 72 hours for CDH20 versus vector. Panel C contains four fluorescence microscopy images quantifying cell migration and invasion, showing fewer cells in the CDH20 group. Panels D and E show bar graphs indicating significantly reduced migration and invasion in CDH20-expressing cells, and panels E and F show significantly increased optical density at 570 nanometers in adhesion assays for CDH20 compared to vector.

Upregulated CDH20 enhances cervical cell adhesion but reduces cell migration and invasion. Caski cell lines stably overexpressing CDH20 or empty vector were established by lentivirus infection. (A) The lysates were blotted with the indicated antibodies. (B) Proliferation of the Caski stable cell lines was detected by MTS assay. The cell proliferation index of the vector group at 24 h was defined as 100%. (C) Migration and invasion of Caski stable cell lines were determined by transwell assay. Representative images are shown. (D) Changes in cell migration and invasion were quantified. (E) Cell adhesion to uncoated plates was measured by cell adhesion assay using the Caski stable cell lines. (F) Cell adhesion to fibronectin-coated plates was measured by cell adhesion assay using the Caski stable cell lines. All statistical data were analyzed by one-way analysis of variance (ANOVA). All values represent the means ± SEM. *P < 0.05 compared with the control. NS, non-significant.

There was a mistake in Figure 4 as published. Incorrect immunofluorescence images were provided for the first row of “panel D” in Figure 4. The corrected Figure 4 appears below.

Figure 4.

Four-panel scientific figure showing protein expression in SiHa and Caski cell lines. Panels A and B present Western blot bands for E-cadherin, N-cadherin, β-catenin, CDH20, Vimentin, and GAPDH under various treatments and genetic modifications. Panels C and D display immunofluorescence images of cells stained with DAPI (blue, nuclei), E-cadherin (red), and N-cadherin (green) under different conditions, highlighting changes in protein localization and intensity. Each condition is organized in labeled rows and columns for clear comparison. Scale bars indicate 10 micrometers.

Different expression patterns of CDH20 differently affect the EMT process of cervical cancer cells. (A) CDH20 was downregulated in artificial EMT models induced by TGF-β in both SiHa and Caski cells. Upregulation of N-cadherin or downregulation of E-cadherin and β-catenin expression was verified in EMT models. (B) Western blot analysis of EMT markers (E-cadherin, N-cadherin, β-catenin, and vimentin) in the CDH20 knockdown SiHa cells or the CDH20 overexpression Caski cells compared with those in the control groups. GAPDH was used to normalize protein expression. One representative of three different experiments, for each of the analyses performed, is shown. (C) Immunofluorescence showed that E-cadherin and N-cadherin expression levels were increased or decreased, respectively, in CDH20-overexpressing Caski cells via laser confocal microscopy. (D) Immunofluorescence showed that E-cadherin and N-cadherin expression levels were decreased or increased, respectively, in CDH20-knockdown SiHa cells via laser confocal microscopy. Representative images of E-cadherin and β-catenin N-cadherin localization are shown.

The original version of this article has been updated.

Footnotes

Edited and reviewed by: Tonya J. Webb, University of Maryland School of Medicine, United States

Publisher’s note

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