ABSTRACT
Bcl2l10, also known as Diva, Bclb and Boo, is a member of the Bcl2 family of proteins, which are involved in signaling pathways that regulate cell apoptosis and autophagy. Previously, it was demonstrated that Bcl2l10 plays a crucial role in the completion of oocyte meiosis and is a key regulator of Aurora kinase A (Aurka) expression and activity in oocytes. Aurka is overexpressed in several types of solid tumors and has been considered a target of cancer therapy. Based on these previous results, in the present study, the authors aimed to investigate the regulatory role of Bcl2l10 in A2780 and SKOV3 human ovarian cancer cells. The protein expression of Bcl2l10 was examined in human cancer tissues and cell lines, including the ovaries, using a tissue microarray and various human ovarian cancer cell lines. It was found that Bcl2l10 regulated the protein stability and activities of Aurka in ovarian cancer cells. Although apoptosis was not affected, the cell cycle was arrested at the G0/G1 phase by Bcl2l10 knockdown. Of note, cell viability and motility were markedly increased by Bcl2l10 knockdown. On the whole, the findings of this study suggest that Bcl2l10 functions as tumor suppressor gene in ovarian cancer.
Subject(s)
Aurora Kinase A/metabolism , Ovarian Neoplasms/pathology , Proto-Oncogene Proteins c-bcl-2/metabolism , Tumor Suppressor Proteins/metabolism , Cell Line, Tumor , Cell Movement/genetics , Cell Survival/genetics , Female , G1 Phase Cell Cycle Checkpoints/genetics , Gene Knockdown Techniques , Humans , Ovary/pathology , Protein Stability , Proto-Oncogene Proteins c-bcl-2/genetics , Tumor Suppressor Proteins/geneticsABSTRACT
The erythrocyte membrane is composed of a phospholipid bilayer, which is known to undergo physicochemical changes during storage at low temperatures. This study was conducted to identify marker phospholipids that indicate alteration during deep-frozen storage and to determine the amount of marker phospholipids. Our research suggested a method to detect phospholipids by profiling analysis of thermally injured red blood cells (RBCs) without protecting agents. Human blood was stored at -80°C for 72 days. The RBC membrane phospholipids were extracted through a modified Bligh and Dyer method. Six selected phospholipids were analyzed and quantified using liquid chromatography-tandem mass spectrometry, and an in vitro model system was developed. The intracellular level of N-nervonoyl-D-erythro-sphingosylphosphorylcholine significantly increased in the thermally injured RBCs, and multiple biomarker candidates were evaluated by profiling analysis and mass spectrometry technology for targeted metabolomics.
