ABSTRACT
Nasopharyngeal carcinoma (NPC) is a common malignant tumor of the head and neck. Its pathogenesis is complicated and needs further investigation. The aim of this study was to investigate the expression and clinical significance of WWP1 in NPC. Bioinformatics approaches were used to evaluate the expression and functions of WWP1 in NPC. WWP1 protein expression was then detected by immunohistochemistry on a tissue microarray in an NPC cohort and its association with clinical features and prognosis was determined. In addition, WWP1 expression was knocked down in NPC cells using RNA interference, and their colony formation and invasion abilities were assessed. A total of 25 genes closely related to WWP1, which may be enriched in different pathways, were filtered out. WWP1 expression was significantly higher in NPC cells than in normal controls. High WWP1 expression was correlated with lymph node metastasis, tumor recurrence, clinical stage and poor prognosis. Knockdown of WWP1 resulted in attenuated proliferation and invasion of NPC cells. The results suggest that WWP1 may serve as a novel biomarker and prognostic factor for NPC and a potential therapeutic target worthy of further investigation.
Subject(s)
Immunohistochemistry , Nasopharyngeal Carcinoma , Nasopharyngeal Neoplasms , Ubiquitin-Protein Ligases , Humans , Nasopharyngeal Neoplasms/pathology , Nasopharyngeal Neoplasms/metabolism , Nasopharyngeal Neoplasms/diagnosis , Male , Female , Middle Aged , Ubiquitin-Protein Ligases/genetics , Ubiquitin-Protein Ligases/metabolism , Nasopharyngeal Carcinoma/pathology , Nasopharyngeal Carcinoma/metabolism , Nasopharyngeal Carcinoma/genetics , Nasopharyngeal Carcinoma/diagnosis , Cell Line, Tumor , Prognosis , Biomarkers, Tumor/genetics , Biomarkers, Tumor/metabolism , Cell Proliferation , Adult , Neoplasm Invasiveness , Carcinoma/pathology , Carcinoma/metabolism , Carcinoma/genetics , Carcinoma/diagnosis , Lymphatic Metastasis , Gene Expression Regulation, Neoplastic , Clinical RelevanceABSTRACT
Flexible photodetectors are fundamental components for developing wearable systems, which can be widely used for medical detection, environmental monitoring and flexible imaging. However, compared with 3D materials, low-dimensional materials have degraded performance, a key challenge for current flexible photodetectors. Here, a high-performance broadband photodetector has been proposed and fabricated. By combining the high mobility of graphene (Gr) with the strong light-matter interactions of single-walled carbon nanotubes (SWCNTs) and molybdenum disulfide (MoS2), the flexible photodetector exhibits a greatly improved photoresponse covering the visible to near-infrared range. Additionally, a thin layer of gadolinium iron garnet (Gd3Fe5O12, GdlG) film is introduced to improve the interface of the double van der Waals heterojunctions to reduce the dark current. The SWCNT/GdIG/Gr/GdIG/MoS2 flexible photodetector exhibits a high photoresponsivity of 47.375 A/W and a high detectivity of 1.952 × 1012 Jones at 450 nm, a high photoresponsivity of 109.311 A/W and a high detectivity of 4.504 × 1012 Jones at 1080 nm, and good mechanical stability at room temperature. This work demonstrates the good capacity of GdIG-assisted double van der Waals heterojunctions on flexible substrates and provides a new solution for constructing high-performance flexible photodetectors.
ABSTRACT
The transcription factor, AP-1, plays an important role in cellular proliferation, transformation and death. We previously showed that AC3-33 (GenBank name: c3orf33, FLJ31139), significantly inhibited transcriptional activity of AP-1. In this study, we report a method to express and purify AC3-33 in E. coli using glutathione-S-transferase (GST) fusion system. A GST-fusion protein was created by insertion of AC3-33 gene into a pGEX-4T-1 vector. The fusion protein, GST-AC3-33, was expressed in BL21 strain, and purified by GSH-affinity chromatography followed by thrombin cleavage. The digested product was further purified in a GSH-affinity column. After cleavage and purification, the recombinant AC3-33 protein exhibited the expected size of 29 kDa by SDS-PAGE and Western blotting and inhibited transcriptional activity of AP-1 in a dual-luciferase reporter assay. The bioactive recombinant GST-AC3-33, can be used to decipher the physiological and biochemical role of this protein.
