ABSTRACT
BACKGROUND: The stent embedded in the esophageal mucosa is one of the complications after stenting for esophageal stricture. We present a case of stent adjustment with the aid of a transparent cap after endoscopic injection of an esophageal varices stent. CASE SUMMARY: A 61-year-old male patient came to the hospital with discomfort of the chest after the stent implanted for the stenosis because of endoscopic injection of esophageal varices. The gastroscopy was performed, and the stent embedded into the esophageal mucosa. At first, we pulled the recycling line for shrinking the stent, however, the mucosa could not be removed from the stent. Then a forceps was performed to remove the mucosa in the stent, nevertheless, the bleeding form the mucosa was obvious. And then, we used a transparent cap to scrape the mucosa along the stent, and the mucosa were removed successfully without bleeding. CONCLUSION: A transparent cap helps gastroscopy to remove the mucosa embedded in the stent after endoscopic injection of the esophageal varices stent.
ABSTRACT
BACKGROUND: miRNAs regulate a multitude of cellular processes and their aberrant regulation is linked to human cancer. However, the role of miR-425-5p in lung cancer (LCa) is still largely unclear. Here, we explored the role of miR-425-5p during LCa tumorigenesis. METHODS: Cell proliferation was evaluated by cell counting Kit-8 and colony formation assay. Western blot and real-time PCR were accordingly used to detect the relevant proteins, miRNA and gene expression. Luciferase reporter assays were used to illustrate the interaction between miR-425-5p and PTEN. RESULTS: We demonstrate that miR-425-5p is overexpressed in LCa tissue and enhances the proliferative and colony formation capacity of the LCa cell lines A549 and NCI-H1299. Through predictive binding assays, PTEN was identified as a direct gene target and its exogenous expression inhibited the pro-cancer effects of miR-425-5p. Through its ability to down-regulate PTEN, miR-425-5p activated the PI3K/AKT axis. CONCLUSION: We conclude that miR-425-5p promotes LCa tumorigenesis through PTEN/PI3K/AKT signaling.
Subject(s)
Cell Proliferation/genetics , Gene Expression Regulation, Neoplastic , Lung Neoplasms/genetics , MicroRNAs/genetics , Cell Line, Tumor , Down-Regulation , Humans , Lung Neoplasms/pathology , PTEN Phosphohydrolase/genetics , Phosphatidylinositol 3-Kinases/genetics , Proto-Oncogene Proteins c-akt/genetics , Signal Transduction/geneticsABSTRACT
Cisplatin is a chemotherapeutic drug for treatment of many solid tumors. It has been shown to induce apoptosis and/or necrosis in different types of cancer cells. However, the underlying mechanisms remain elusive. In this study, we provide evidences that cisplatin induces necroptosis in receptor-interacting protein 3 (RIP3)-expressing cell lines, but not in cell lines lacking RIP3 protein expression. Deficiency of core components of necroptotic pathway, RIP1, RIP3, or mixed lineage kinase domain-like protein (MLKL) blocked cisplatin-induced cell death in L929 cells. This phenomenon is dependent on RIP1/RIP3/MLKL necrosome formation and translocation to mitochondria-associated membrane (MAM), but only partially via autocrine production of tumor necrosis factor α (TNFα). Moreover, we demonstrate that the mitochondrial permeability transition pore opening (mPTP) opening and reactive oxygen species (ROS) generation is a critical downstream event of the formation of necrosome in cisplatin-induced necroptosis, which is TNFα independent. Deficiency of cyclophilin-D (CypD) partially reduced cisplatin-induced cell death, indicating CypD mediated-mPTP opening plays an important role during cisplatin-induced necroptosis. Both deletion of CypD and TNFα completely blocked cisplatin-induced cell death, suggesting that cisplatin could induce necroptosis through TNFα dependent and independent pathway. These findings provide new insight into the molecular mechanisms underlying cisplatin-induced necroptosis.
Subject(s)
Apoptosis/drug effects , Cisplatin/pharmacology , Signal Transduction/drug effects , Tumor Necrosis Factor-alpha/metabolism , Animals , Autocrine Communication/drug effects , Base Sequence , Peptidyl-Prolyl Isomerase F , Cyclophilins/metabolism , HEK293 Cells , HeLa Cells , Humans , Membrane Potential, Mitochondrial/drug effects , Mice , Mitochondrial Membrane Transport Proteins/metabolism , Mitochondrial Membranes/metabolism , Mitochondrial Permeability Transition Pore , Models, Biological , Necrosis , Protein Binding/drug effects , Protein Kinases/metabolism , Protein Transport/drug effects , Receptors, Tumor Necrosis Factor, Type I/metabolismABSTRACT
Hepatitis B virus (HBV) X gene, encoding a pleotropic transactivator of HBx protein, has been associated with the development of hepatocellular carcinoma (HCC). Molecular information on liver-derived HBV variants isolated from HCC among Taiwanese population was studied. Amplification of the HBV X genes of 20 HCC patients in high stringency with HBV specific primers was observed. The resulting amplified HBV X genes were purified and individually-cloned into pUC-T vector. Sequences of the eight liver-derived X gene were aligned and compared with the wild type, the ayw HBV serotype. Results indicate that the HBx protein of variants were found predominantly within the regions of amino acid positions 26-45 in N-terminus, and positions 87, 88, 116, 118, 119, 127 and 144. Sequences from six out of the eight variants were found to be identical. These accumulated sequence mutations among the eight HBx variants were found to coincide within the B-cell epitopes (positions 29-48), particularly in the HBx proline and serine rich (PSR) domain, and the T-cell epitopes regions (positions 116-127). These frequent mutations of HBV variants, rather than subtype-specific polymorphic sites, may be involved in immunoevasion.
