Identification of EBP50 as a Specific Biomarker for Carcinogens Via the Analysis of Mouse Lymphoma Cellular Proteome

Abstract

To identify specific biomarkers generated upon exposure of L5178Y mouse lymphoma cells to carcinogens, 2-DE and MALDI-TOF MS analysis were conducted using the cellular proteome of L5178Y cells that had been treated with the known carcinogens, 1,2-dibromoethane and Onitrotoluene and the noncarcinogens, emodin and Dmannitol. Eight protein spots that showed a greater than 1.5-fold increase or decrease in intensity following carcinogen treatment compared with treatment with noncarcinogens were selected. Of the identified proteins, we focused on the candidate biomarker ERM-binding phosphoprotein 50 (EBP50), the expression of which was specifically increased in response to treatment with the carcinogens. The expression level of EBP50 was determined by western analysis using polyclonal rabbit anti-EBP50 antibody. Further, the expression level of EBP50 was increased in cells treated with seven additional carcinogens, verifying that EBP50 could serve as a specific biomarker for carcinogens.

Antiangiogenic Activity of the Lipophilic Antimicrobial Peptides from an Endophytic Bacterial Strain Isolated from Red Pepper Leaf

“…Cell lysates were separated by 10% SDS-PAGE electrophoresis and the separated proteins were transferred to polyvinylidene difluoride membranes (Millipore, USA) using standard electroblotting procedures ( Lee et al, 2012b ). The blots were blocked and immunolabeled with primary antibodies against HIF-1α, cyclin D1 and tubulin overnight at 4°C.…”