Corrigendum to “Sar131675 Exhibits Anticancer Activity on Human Ovarian Cancer Cells Through Inhibition of Vegfr-3/Erk1/2/Akt Signaling Pathway” [Cellular Signaling 111 (2023) 110856] (Cellular Signalling (2023) 111, (S089865682300270x), (10.1016/J.Cellsig.2023.110856)) Publisher Pubmed

Summary: Why were images repeated in a cancer study? A correction explains that two figure panels shared control images from simultaneous experiments; no new trial was reported. #ResearchIntegrity #Correction

Babaei Z ; Panjehpour M ; Parsian H ; Aghaei M
Source: Cellular Signalling Published:2026

Abstract

The authors regret that Fig. 5A and B contain the same control images without explicit disclosure in the original publication. The experiments presented in these panels were conducted simultaneously under identical experimental conditions using a shared-control design; however, this was not clearly indicated in the original figure presentation and legend. The authors acknowledge this oversight and have revised the figure legend to explicitly state that the control images were shared across both experiments. This clarification does not affect the results, statistical analyses, or conclusions of the study. The revised legend for Fig. 5 has been included below in the corrigendum for clarity. Fig. 5 SAR131675 suppresses the migration ability of OVCAR3 and SKOV3 cells. (A) Cells were grown to 100% confluency and a cleared scratch area was created before stimulation with or without VEGF-CS (50 ng/ml), in the presence or absence of SAR131675 (0.1, 1, and 10 μM). Cell migration was evaluated by the ability of cells to migrate into the scratch area after 24 h. Dashed lines indicate wound edges. VEGFR-3 activation increased the migration ability of OVCAR3 and SKOV3 cells, whereas SAR131675 (0.1–10 μM, 24 h) dose-dependently inhibited cell migration in both cell lines. (B) OVCAR3 and SKOV3 cells were treated with SAR131675 (0.1, 1, and 10 μM) and cell migration was evaluated by the ability of cells to migrate into the scratch area after 24 h. Dashed lines indicate wound edges. SAR131675 (0.1–10 μM, 24 h) decreased OVCAR3 and SKOV3 cell migration in a dose-dependent manner. The control images used in Fig. 5A and B originate from a shared-control experiment and were used in both panels. The closure rate was expressed as the percentage of the initial wounded area recovered by cells after 24 h. Data are presented as the means ± SD from three independent experiments. Statistical analysis was determined with one-way ANOVA, followed by the Dunnett's test; *P < 0.05 vs. control cells; #P < 0.05 vs. VEGF-CS-treated cells. The authors also regret that concerns were raised regarding Figs. 1C and 6A because of an apparent similarity between their GAPDH panels. A detailed review of the original figure assembly files together with the corresponding uncropped Western blot data demonstrated that Figs. 1C and 6A were generated from two independent experiments. Comparison of the original uncropped blots showed that the GAPDH image displayed in Fig. 1C did not correspond to the original experiment for that figure but instead matched the GAPDH panel from the experiment presented in Fig. 6A. This review identified an inadvertent figure assembly error during preparation of the composite figures, whereby the GAPDH band from the experiment underlying Fig. 6A was mistakenly inserted into Fig. 1C. The GAPDH panel in Fig. 6A is the correct original image, whereas Fig. 1C contained an incorrectly inserted GAPDH panel as a result of this assembly error. The corrected Fig. 1C presented in this corrigendum now contains its appropriate original GAPDH panel. The original uncropped blots clearly show distinct band patterns and exposure conditions for the two independent experiments, confirming that no experimental data were duplicated. Furthermore, the quantification of the phosphorylated protein in Fig. 1C was performed relative to the corresponding total protein level, with GAPDH serving only as an additional loading and transfer control. Therefore, replacement of the incorrect GAPDH image does not affect the quantitative analyses, statistical results, or the conclusions of the study. This issue is limited solely to figure assembly and has no impact on the underlying experimental observations or the overall conclusions of the study. A corrected version of Fig. 1C containing the appropriate GAPDH panel is provided in the corrigendum for clarity.[Figure presented] Fig. 1 VEGFR-3 phosphorylation increases OVCAR3 and SKOV3 cell proliferation. (A) VEGFR-3 mRNA expression was determined by qRT-PCR in OVCAR3 and SKOV3 cells. β-actin was used as an internal control. (B) Western blotting showing the VEGFR-3 protein expression in OVCAR3 and SKOV3 cells. GAPDH was used as a loading control. (C) Serum-starved OVCAR3 and SKOV3 cells were treated for 30 min with increasing concentrations of VEGF-CS (1, 10, and 50 ng/ml), and the phosphorylation status of VEGFR-3 was determined by western blotting. VEGF-CS treatment increased the content of phosphorylated VEGFR-3 in a dose-dependent manner with maximum effect at 50 ng/ml. (D) Serum-starved cells were treated with 50 ng/ml VEGF-CS at different time intervals (15, 30, and 60 min), and VEGFR-3 activation was determined by western blotting. VEGF-CS treatment increased the content of phosphorylated VEGFR-3 in a time-dependent manner with maximum effect at 30 min. (E) Serum-starved cells were treated with VEGF-CS (1–100 ng/ml) for 48 h and proliferation was determined by BrdU assay. VEGFR-3 activation significantly increased the proliferation ability of OVCAR3 and SKOV3 cells (≥10 ng/ml VEGF-CS in OVCAR3 and ≥ 50 ng/ml VEGF-CS in SKOV3). Data represent the means ± SD from three independent experiments. Statistical analysis was performed with Student's t-test (for 2 groups) and one-way ANOVA, followed by Dunnett's test (for >2 groups); *P < 0.05, NS: no significant vs. control. The authors would like to apologise for any inconvenience caused. © 2026 Elsevier Inc.