Claudin1 promotes the proliferation, invasion and migration of nasopharyngeal carcinoma cells by upregulating the expression and nuclear entry of β‑catenin

Abstract

The aim of the present study was to measure the expression of Claudin (CLDN) 1 in nasopharyngeal carcinoma (NPC) and to determine its biological function and mechanism of action. Reverse transcription-quantitative polymerase chain reaction and western blotting were performed to measure the expression of CLDN1 mRNA and protein, respectively, in the immortalized human nasopharyngeal epithelial cell line NP69 and NPC-TW01 cells. Subsequently, small interfering RNA against CLDN1 and the LV-GFP-PURO-CLDN1 lentivirus were transfected into NPC-TW01 cells. Western blotting was used to determine the effects of CLDN1 down- and upregulation on the expression of the epithelial mesenchymal transition (EMT) markers E-cadherin and vimentin. In addition, the effect of CLDN1 on the expression of β-Catenin was determined. The results demonstrated that levels of CLDN1 mRNA and protein in NPC cells were significantly higher than in NP69 cells. Furthermore, the downregulation of CLDN1 inhibited the proliferation, invasion and migration of NPC-TW01 cells. The results of western blotting demonstrated that the downregulation of CLDN1 resulted in the upregulation of E-cadherin and inhibition of vimentin in NPC-TW01 cells. By contrast, the overexpression of CLDN1 resulted in the downregulation of E-cadherin and upregulation of vimentin in NPC-TW01 cells. The downregulation of β-catenin attenuated the cancer-promoting effect of CLDN1 on NPC-TW01 cells, whereas the upregulation of β-catenin reversed the tumor-suppressing effect of CLDN1 downregulation on NPC-TW01 cells. The results of the present study therefore demonstrate that CLDN1 expression is elevated in NPC cells. As an oncogene, CLDN1 promotes the proliferation, invasion and migration of NPC cells by upregulating the expression and nuclear entry of β-catenin.

Claudin 10 acts as a novel biomarker for the prognosis of patients with ovarian cancer

“…The WNT/β-catenin signaling pathway is implicated in the carcinogenesis of various types of OC and is involved in EMT (41). Previous studies have demonstrated that CLDN1 serves a major role in regulating EMT and in inducing β-catenin expression in cancer cells (42,43), indicating that CLDN10 expression in OC may be associated with EMT or β-catenin. Based on the aforementioned studies, it was hypothesized that CLDN10 may regulate the progression of OC via TGF-β-or WNT/β-catenin-induced EMT, which should be further investigated in future studies.…”

LncRNA SOX2‐OT regulates proliferation and metastasis of nasopharyngeal carcinoma cells through miR‐146b‐5p/HNRNPA2B1 pathway

“…Nasopharyngeal carcinoma (NPC) is considered as a category of the most prevailing head and neck malignant epithelial tumors with a high incidence in southern China. 1 NPC is described as an aggressive malignancy on account of its frequent metastasis and poor prognosis. 2 It is widely accepted that NPC originating from epithelium in the nasopharynx leads to high mortality in patients due to its high metastasis rate.…”

Integrative RNA-Seq and H3 Trimethylation ChIP-Seq Analysis of Human Lung Cancer Cells Isolated by Laser-Microdissection

“…These pathways consisted of the well-known PI3K-Akt signaling pathway and three other pathways associated with cell matrix adhesions in cancer: extracellular matrix (ECM) receptor interaction, cell adhesion molecules (CAMs), and focal adhesion ( Table S11 ). This pathway analysis result also highlights several DEGs associated with tumor-altered H3K4me3 histone marks including downregulated (tumor vs. normal) tumor suppressor genes: Integrin alpha8 ( ITGA8 ) [ 34 ], Fms-like tyrosine kinase-1 ( FLT1 ) [ 35 ], junctional adhesion molecule 2 (JAM2) [ 36 ], calcium voltage-gated channel auxiliary subunit alpha2delta2 ( CACNA2D2 ) [ 37 ], and dystrophin ( DMD ) [ 38 ]; and upregulated potential oncogenes: p-cadherin ( CDH3 ) [ 39 ], claudin-1 ( CLDN1 ) [ 40 ], desmoglein-2 ( DSG2 ) [ 41 ], ephrin A3 ( EFNA3 ) [ 42 ], integrin subunit beta 4 ( ITGB4 ) [ 43 ], integrin subunit beta 8 ( ITGB8 ) [ 44 ], and laminin gamma 2 ( LAMC2 ) [ 45 ].…”