Otwarty dostęp

Dusp6 inhibits epithelial-mesenchymal transition in endometrial adenocarcinoma via ERK signaling pathway

Ming-Jun Fan

Ming-Jun Fan

Department of Obstetrics and Gynecology, Shandong Provincial Hospital Affiliated to Shandong UniversityJinan, China
Wyszukaj tego autora
Sciendo|Google Scholar
Fan, Ming-Jun
, 
Shu-Mei Liang

Shu-Mei Liang

Department of Obstetrics and Gynecology, Shandong Provincial Hospital Affiliated to Shandong UniversityJinan, China
Wyszukaj tego autora
Sciendo|Google Scholar
Liang, Shu-Mei
, 
Peng-Juan He

Peng-Juan He

Department of Obstetrics and Gynecology, Shandong Provincial Hospital Affiliated to Shandong UniversityJinan, China
Wyszukaj tego autora
Sciendo|Google Scholar
He, Peng-Juan
, 
Xing-Bo Zhao

Xing-Bo Zhao

Department of Obstetrics and Gynecology, Shandong Provincial Hospital Affiliated to Shandong UniversityJinan, China
Wyszukaj tego autora
Sciendo|Google Scholar
Zhao, Xing-Bo
, 
Ming-Jiang Li

Ming-Jiang Li

Department of Obstetrics and Gynecology, Shandong Provincial Hospital Affiliated to Shandong UniversityJinan, China
Wyszukaj tego autora
Sciendo|Google Scholar
Li, Ming-Jiang
 oraz 
Feng Geng

Feng Geng

Department of Obstetrics and Gynecology, Shandong Provincial Hospital Affiliated to Shandong UniversityJinan, China
Wyszukaj tego autora
Sciendo|Google Scholar
Geng, Feng
  
24 wrz 2019
Dusp6 inhibits epithelial-mesenchymal transition in endometrial adenocarcinoma via ERK signaling pathway's Cover Image
O artykule
Poprzedni artykuł
Następny artykuł
Zacytuj
Pobierz okładkę
Kategoria artykułu: Research Article
Data publikacji: 24 wrz 2019
Zakres stron: 307 - 315
Otrzymano: 16 maj 2019
Przyjęty: 09 lip 2019
DOI: https://doi.org/10.2478/raon-2019-0034
Słowa kluczowe
© 2019 Ming-Jun Fan, Shu-Mei Liang, Peng-Juan He, Xing-Bo Zhao, Ming-Jiang Li, Feng Geng, published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Figure 1

Expression analysis of Dusp6, E-cadherin and N-cadherin in EAC tissues and the adjacent non-tumor tissues. (A) The protein expression level of DUSP6 was analysed by western-blot and immunohistochemistry analysis in EAC tumor and adjacent non-tumor tissues. (B) The protein expression level of E-cadherin was analysed by western-blot and immunohistochemistry analysis in EAC tumor and adjacent non-tumor tissues. (C) The protein expression level of N-cadherin was analysed by western-blot and immunohistochemistry analysis in EAC tumor and adjacent non-tumor tissues.Data were presented as Mean ±SD. P < 0.05 was considered as significant.* P < 0.05. Each experiment was performed in triplicate.
Expression analysis of Dusp6, E-cadherin and N-cadherin in EAC tissues and the adjacent non-tumor tissues. (A) The protein expression level of DUSP6 was analysed by western-blot and immunohistochemistry analysis in EAC tumor and adjacent non-tumor tissues. (B) The protein expression level of E-cadherin was analysed by western-blot and immunohistochemistry analysis in EAC tumor and adjacent non-tumor tissues. (C) The protein expression level of N-cadherin was analysed by western-blot and immunohistochemistry analysis in EAC tumor and adjacent non-tumor tissues.Data were presented as Mean ±SD. P < 0.05 was considered as significant.* P < 0.05. Each experiment was performed in triplicate.

Figure 2

Effects of DUSP6 overexpression on cellular proliferation and EMT. (A) The protein expression level of DUSP6 was analysed using western-blot. (B) The cell viability of Ishikawa 3H12 cell lines measured using MTT assay. (C) Relative invasion ability of Ishikawa 3H12 cell lines measured using Transwell Matrigel assay. (D) Relative migration ability of Ishikawa 3H12 cell lines measured using wound healing assay. (E) The protein levels of E-cadherin and Vimentin in Ishikawa 3H12 cell lines measured using western-blot analysis. Groups: Negative control, pcDNA3.1 Vector-alone clones, pcDNA3.1-Dusp6 clones. Data were presented as Mean ±SD. P < 0.05 was considered as significant. *P < 0.05. Each experiment was performed in triplicate.
Effects of DUSP6 overexpression on cellular proliferation and EMT. (A) The protein expression level of DUSP6 was analysed using western-blot. (B) The cell viability of Ishikawa 3H12 cell lines measured using MTT assay. (C) Relative invasion ability of Ishikawa 3H12 cell lines measured using Transwell Matrigel assay. (D) Relative migration ability of Ishikawa 3H12 cell lines measured using wound healing assay. (E) The protein levels of E-cadherin and Vimentin in Ishikawa 3H12 cell lines measured using western-blot analysis. Groups: Negative control, pcDNA3.1 Vector-alone clones, pcDNA3.1-Dusp6 clones. Data were presented as Mean ±SD. P < 0.05 was considered as significant. *P < 0.05. Each experiment was performed in triplicate.

Figure 3

Effects of knocking down DUSP6 on cellular proliferation and EMT. The efficiency of transfection was validated by measuring protein expression level of DUSP6 using western blot. (B) The cell viability of Ishikawa 3H12 cell lines measured using MTT assay. (C) Relative invasion ability of Ishikawa 3H12 cell lines measured using Transwell Matrigel assay. (D) Relative migration ability of Ishikawa 3H12 cell lines measured using wound healing assay. (E) The protein levels of E-cadherin and Vimentin in Ishikawa 3H12 cell lines measured using western-blot analysis. Groups: Negative control, sh-NC clones, sh-Dusp6 clones. Data were presented as Mean ±SD. P < 0.05 was considered as significant. *P < 0.05. Each experiment was performed in triplicate.
Effects of knocking down DUSP6 on cellular proliferation and EMT. The efficiency of transfection was validated by measuring protein expression level of DUSP6 using western blot. (B) The cell viability of Ishikawa 3H12 cell lines measured using MTT assay. (C) Relative invasion ability of Ishikawa 3H12 cell lines measured using Transwell Matrigel assay. (D) Relative migration ability of Ishikawa 3H12 cell lines measured using wound healing assay. (E) The protein levels of E-cadherin and Vimentin in Ishikawa 3H12 cell lines measured using western-blot analysis. Groups: Negative control, sh-NC clones, sh-Dusp6 clones. Data were presented as Mean ±SD. P < 0.05 was considered as significant. *P < 0.05. Each experiment was performed in triplicate.

Figure 4

Assessment of effects of overexpressing DUSP6 on ERK signalling pathway. The protein level of phosphorylated ERK and ERK were measured using western blot analysis in Ishikawa 3H12 cell lines when DUSP6 was overexpressed. Β-actin served as an internal control. Groups: Negative control, pcD-NA3.1 Vector-alone clones, pcDNA3.1-Dusp6 clones. Data were presented as Mean ±SD. Each experiment was performed in triplicate.
Assessment of effects of overexpressing DUSP6 on ERK signalling pathway. The protein level of phosphorylated ERK and ERK were measured using western blot analysis in Ishikawa 3H12 cell lines when DUSP6 was overexpressed. Β-actin served as an internal control. Groups: Negative control, pcD-NA3.1 Vector-alone clones, pcDNA3.1-Dusp6 clones. Data were presented as Mean ±SD. Each experiment was performed in triplicate.

Figure 5

Assessment of effects of knocking down DUSP6 on ERK signalling pathway. The protein level of phosphorylated ERK and ERK were measured using western blot analysis in Ishikawa 3H12 cell lines when DUSP6 was knocked down. Β-actin served as an internal control. Groups: Negative control, sh-NC clones, sh-Dusp6 clones. Each experiment was performed in triplicate. Data were presented as Mean ±SD.
Assessment of effects of knocking down DUSP6 on ERK signalling pathway. The protein level of phosphorylated ERK and ERK were measured using western blot analysis in Ishikawa 3H12 cell lines when DUSP6 was knocked down. Β-actin served as an internal control. Groups: Negative control, sh-NC clones, sh-Dusp6 clones. Each experiment was performed in triplicate. Data were presented as Mean ±SD.
Język:
Angielski
Częstotliwość wydawania:
4 razy w roku
Dziedziny czasopisma:
Medycyna, Medycyna kliniczna, Medycyna wewnętrzna, Hematologia, onkologia, Radiologia
Kanał RSS czasopisma