H-ras oncogene expression and angiogenesis in experimental liver cirrhosis
Authors: Betül Unal
Gülsüm Özlem Elpek
Sevgi Bozova
Journal: Gastroenterology Research and Practice (2013)
Discipline: CLINICAL MEDICINE
Keywords: Proto-oncogenes; ras; angiogenesis; diethylnitrosamine; liver fibrosis
Affiliations: Akdeniz University Medical School, Department of Pathology, 07070 Antalya, Turkey., Antalya Training and Research Hospital, Department of Pathology, 07070 Antalya, Turkey, Serik State Hospital, Department of Pathology, 07070 Antalya, Turkey

Abstract:  Background. Proto-oncogenes, particularly ras, may not only affect cell proliferation but also contribute to angiogenesis by influencing both proangiogenic and antiangiogenic mediators. The aim of this study was to investigate whether any relationship exists between ras expression and angiogenesis during diethylnitrosamine- (DEN-) induced experimental liver fibrosis. Materials and Methods. Liver cirrhosis was induced in rats by intraperitoneal injections of DEN. The animals were sacrificed 2 weeks after the last administrations and a hepatectomy was performed. Masson's trichrome staining was used in the evaluation of the extent of liver fibrosis. The vascular density in portal and periportal areas was assessed by determining the count of CD34 labeled vessel sections. For quantitative evaluation of H-ras expression, in each section positive and negative cells were counted. Results. In fibrotic group H-ras expression was higher than that in nonfibrotic group and was more widespread in cirrhotic livers. Friedman's test showed that there was a significant correlation between H-ras expression and VD (P &lt; 0.01). Conclusion. The results of this descriptive study reveal that H-ras expression gradually increases according to the severity of fibrosis and strongly correlates with angiogenesis. 

Retracted: No

PubPeer comments:
 Figure 3 A and C use images twice for different cell lines and treatments. ![file] ![file] Additionally, the bottom left 3 images in 3A are extremely poor quality and the background is a different color. , 
 We thank Dr. Dendrodoa Grossularia so much for pointing out the mistake in Figure 3A and C. We do deepest apologize to all readers for the mistake we made. We mistakely sortied the imges of 109NC and 109FAT1WT. We have checked the original data and corrected the mistake. Please check the corrected figure. We are contacting the editor office of Cancer Letter to make correction of this figure. Thank you again. We are really appreciated for your comment. ![file] , 
 ![file] An obvious splice in Fig. 6B, p-ERK1 2, could the authors explain? , 
 #3 We thank very much for your comment. In the experiment, we run different gel of 150NC, FAT1sh1, FAT1sh2 in the absence or presence of U0126 to block p-ERK1 2, total ERK1 2, and other proteins. We run the gels for western blotting following the loading sequence: 150NC, FAT1sh1, FAT1sh2 in the absence of U0126, and then following 150NC, FAT1sh1, FAT1sh2 in the presence of U0126. However, we accidently loaded the samples of 150NC, FAT1sh1, FAT1sh2 with U0126 firstly and then samples without U0126 for blocking p-ERK1 2 (see the following initial photo). To easily compare the protein levels, we cut the p-ERK1 2 blot of 150NC, FAT1sh1, FAT1sh2 with U0126, and switched them after150NC, FAT1sh1, FAT1sh2 without U0126. The initial photo of western blot for p-ERK1 2 of KYSE150 as following. ![file] ,