CIP2A, an oncoprotein, is associated with cell proliferation, invasion and migration in laryngeal carcinoma cells
Authors: Xu-Dong Chen
Yao-Wen Wang
Li-Tao Zhang
Shi-Xiong Tang
Jian-Hua Zhang
Journal: Oncology Reports (2017)
Discipline: CLINICAL MEDICINE
Keywords: Laryngeal carcinoma; CIP2A; RNA interference; proliferation; invasion
Affiliations: Department of Otolaryngology, First Hospital of Ningbo City, Ningbo City, Zhejiang 315000, P.R. China.

Abstract:  Laryngeal carcinoma is one of the most common malignant tumors in otorhinolaryngology. Moreover, experimental investigation showed that cancerous inhibitor of protein phosphatase 2A (CIP2A) expressed highly in various cancers. Therefore, we investigated whether CIP2A can regulate the proliferation, invasion and migration by RNA interference in Hep-2 cells and AMC-NH-8 cells and further affect the activation of phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway. Overexpression of CIP2A was evaluated in tumor tissue and laryngeal cancer cell lines (Hep-2 and AMC-NH-8 cells) by real-time quantitative polymerase chain reaction (RT-qPCR) and western blot assay. In a follow-up experiment, we confirmed that CIP2A siRNA effectively suppressed the cell proliferation at 48 and 72 h, and arrested cell cycle at G0/G1 in Hep-2 cells and AMC-NH-8 cells. The invasion and migration of cell in siRNA CIP2A group were markedly inhibited. Moreover, the experimental results showed that the expression levels of invasion- and migration-related genes, including E-cadherin, metastasis-associated gene 1 (MTA1) and matrix metalloproteinases-2/9 (MMP-2/9), were regulated by CIP2A siRNA. Phosphorylation levels of PI3K and AKT proteins were reduced by CIP2A siRNA. Importantly, it suggested signaling through PI3K/Akt as a critical mechanism by which CIP2A siRNA may suppress cell proliferation, invasion and migration in laryngeal carcinoma cells. 

Retracted: No

PubPeer comments:
 ![file] , 
 #1 The arrow is a little vague. What I m seeing is that the bottom bands of each lane and possibly the middle bands of the second lanes are uncannily similar. There are some matching specks in the two gels. The rest of the bands are different. , 
 Perhaps what follows will help sort this out. First, it is figures 4B and 5D that are of concern. I show below the panels as they appear in the journal article and a second rendition with the image regions enlarged and the brightness and contrast adjusted to make the details more apparent. The top panels in the two figures are obviously different. To use a turn of phrase common in this forum, the lower panels are more similar than one might expect. Based on my reading of the text and the figure legends, these two panels represent separate experiments; there is no reason for the lower panels to be in common. I realize this is a fairly old article, but perhaps the authors would care to comment. ![file] ![file] , 
 #3 In fact, most of the bottom panels are identical, as can also be verified by checking the speckle of the background - thanks for the high-contrast images. Interestingly, the fat band in lane 3 of 4B seems to be identical to the fat band in lane 4 of 5D. Awkwardness ensues. , 
 I see what you mean, T. mourzinei. At the very least, highly similar. The plot thickens. ,