Jian Zhang1, Xin Wen1, Xian-Yue Ren1, Ying-Qin Li1, Xin-Ran Tang1, Ya-Qin Wang1, Qing-Mei He1, Xiao-Jing Yang1, Ying Sun1, Na Liu2, Jun Ma3. 1. Sun Yat-sen University Cancer Center; State Key Laboratory of Oncology in South China, Collaborative Innovation Center of Cancer Medicine, 651 Dongfeng Road East, Guangzhou, People's Republic of China. 2. Sun Yat-sen University Cancer Center; State Key Laboratory of Oncology in South China, Collaborative Innovation Center of Cancer Medicine, 651 Dongfeng Road East, Guangzhou, People's Republic of China. liun1@sysucc.org.cn. 3. Sun Yat-sen University Cancer Center; State Key Laboratory of Oncology in South China, Collaborative Innovation Center of Cancer Medicine, 651 Dongfeng Road East, Guangzhou, People's Republic of China. majun2@mail.sysu.edu.cn.
Correction to: J Exp Clin Cancer Res 35, 109 (2016)https://doi.org/10.1186/s13046-016-0384-1Following publication of the original article [1] and subsequent correction [2], the authors identified that further mismatched images were present in the corrected version of Fig. 3. Specifically, in Fig. 3, the SUNE1-si974 cells at 0 h (Si-NC and Si-974) were incorrect, and have been replaced by the correct images.
Fig. 3
Effects of YPEL3 silencing on NPC cell migration and invasion in vitro. a Representative western blotting analysis of YPEL3 silencing in CNE-2 and SUNE-1 cells. GAPDH served as the loading control. b-d Representative images and quantification of the effects of YPEL3 silencing on the migratory and invasive abilities of CNE-2 and SUNE-1 cells as determined by wound healing (b), Transwell migration (c), and invasion assays (d). All of the experiments were performed at least three times. Data presented are the mean ± SD; **P < 0.01 compared with control using Student t-test
In addition, the figures 2, 3, and 6 in the previous correction [2] were not replaced in the original article [1], thus, the figure 2 and 6 have been replaced together with figure 3.
Fig. 2
Effects of YPEL3 overexpression on NPC cell migration and invasion in vitro. a Representative western blotting analysis of YPEL3 overexpression in CNE-2 and SUNE-1 cells. GAPDH served as the loading control. b-d Representative images and quantification of the effects of YPEL3 overexpression on the migratory and invasive abilities of CNE-2 and SUNE-1 cells as determined by wound healing (b), Transwell migration (c), and invasion (d) assays. All of the experiments were performed at least three times. Data presented are the mean ± SD; **P < 0.01 compared with control using Student t-test
Fig. 6
YPEL3 inhibited the Wnt/β-catenin signaling pathway. a Representative western blotting and quantification analysis of GSK-3β, β-catenin, c-MYC, and cyclin D1 expression levels after YPEL3 overexpression. b Representative western blotting and quantification analysis of GSK-3β, βcatenin, c-MYC, and cyclin D1 expression levels after YPEL3 silencing. c YPEL3 inhibited the nuclear (Nu) translocation of β-catenin. Cyto, cytoplasmic. All of the experiments were performed at least three times. Data presented are the mean ± SD; *P < 0.05 and **P < 0.01 compared with control using Student t-test
Effects of YPEL3 overexpression on NPC cell migration and invasion in vitro. a Representative western blotting analysis of YPEL3 overexpression in CNE-2 and SUNE-1 cells. GAPDH served as the loading control. b-d Representative images and quantification of the effects of YPEL3 overexpression on the migratory and invasive abilities of CNE-2 and SUNE-1 cells as determined by wound healing (b), Transwell migration (c), and invasion (d) assays. All of the experiments were performed at least three times. Data presented are the mean ± SD; **P < 0.01 compared with control using Student t-testEffects of YPEL3 silencing on NPC cell migration and invasion in vitro. a Representative western blotting analysis of YPEL3 silencing in CNE-2 and SUNE-1 cells. GAPDH served as the loading control. b-d Representative images and quantification of the effects of YPEL3 silencing on the migratory and invasive abilities of CNE-2 and SUNE-1 cells as determined by wound healing (b), Transwell migration (c), and invasion assays (d). All of the experiments were performed at least three times. Data presented are the mean ± SD; **P < 0.01 compared with control using Student t-testYPEL3 inhibited the Wnt/β-catenin signaling pathway. a Representative western blotting and quantification analysis of GSK-3β, β-catenin, c-MYC, and cyclin D1 expression levels after YPEL3 overexpression. b Representative western blotting and quantification analysis of GSK-3β, βcatenin, c-MYC, and cyclin D1 expression levels after YPEL3 silencing. c YPEL3 inhibited the nuclear (Nu) translocation of β-catenin. Cyto, cytoplasmic. All of the experiments were performed at least three times. Data presented are the mean ± SD; *P < 0.05 and **P < 0.01 compared with control using Student t-testThe corrected figure is given here. The correction does not affect the conclusions of the article. The original article has been updated.
Authors: Mario Dioguardi; Francesca Spirito; Diego Sovereto; Lucia La Femina; Alessandra Campobasso; Angela Pia Cazzolla; Michele Di Cosola; Khrystyna Zhurakivska; Stefania Cantore; Andrea Ballini; Lorenzo Lo Muzio; Giuseppe Troiano Journal: Biology (Basel) Date: 2022-04-24