Related Experiment Video
Updated: May 4, 2026
An Organotypic High Throughput System for Characterization of Drug Sensitivity of Primary Multiple Myeloma Cells
Published on: July 15, 2015
Proteomic studies of multiple myeloma in RPMI8226 cell line treated with bendamustine
Chenglong Sun1, Juan Li, Jingli Gu
1Department of Hematology, First Affiliated Hospital of Sun Yat-sen University, Guangzhou, 510080 China.
Purpose:
Multiple myeloma (MM) is a malignant and incurable neoplasm of plasma cells that accumulate in the bone marrow. Bendamustine, an antitumor agent including double property of alkylating agent and purine analogues, displayed clinical antitumor activity in patients with MM. However, the precise mechanism of action of bendamustine has not been completely elucidated.
Methods:
In this study, we established the cell model of bendamustine-induced MM RPMI8226 cell apoptosis, and used two dimensional differential in-gel electrophoresis (2D-DIGE) proteomics to analyze the bendamustine-induced protein alterations.
Results:
Our results revealed that compared with control group, bendamustine significantly inhibited the proliferation of RPMI8226 cells in a concentration-dependent and time-dependent manner. Proteomic approach was performed to identify 30 differentially expressed proteins in RPMI8226 cells upon bendamustine treatment, which included 15 up-regulated and 15 down-regulated proteins. Of these, protein disulfide isomerase A3 (PDIA3) and cytokine- induced apoptosis inhibitor 1 (CPIN1), were selected for further studies.
Conclusion:
These results implicate PDIA3 and CPIN1 as potential molecular targets for drug intervention in MM and thus provide novel insights into the mechanisms of antitumor activity of bendamustine.
