Proteomic analysis of proteins altered by dibenzoylmethane in human prostatic cancer LNCaP cells

• Published in: Proteomics (Weinheim) 2004-09, Vol.4 (9), p.2814-2821
• Main Authors: Frazier, Monica C., Jackson, Kimberly M., Jankowska-Stephens, Ewa, Anderson, Mark G., Harris, Wayne B.
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Cancer; Cell Line, Tumor; Chalcones - metabolism; Dibenzoylmethane; Electrophoresis, Gel, Two-Dimensional - methods; Female; Fundamental and applied biological sciences. Psychology; Gene Expression Profiling; Gynecology. Andrology. Obstetrics; Humans; LNCaP; Male; Male genital diseases; Medical sciences; Miscellaneous; Molecular Sequence Data; Neoplasm Proteins - chemistry; Neoplasm Proteins - metabolism; Nephrology. Urinary tract diseases; Prostatic Neoplasms; Proteins; Proteome - analysis; Proteomic analysis; Proteomics - methods; Receptors, Androgen - genetics; Receptors, Androgen - metabolism; Tumors; Tumors of the urinary system; Two-dimensional-fluorescence difference gel electrophoresis; Urinary tract. Prostate gland
• ISSN: 1615-9853; 1615-9861
• DOI: 10.1002/pmic.200400834

This paper explores the use of proteomics as a tool for identifying protein species whose expression has been altered by dibenzoylmethane (DBM) in LNCaP cells. Although DBM, a constituent of licorice, has been shown to induce cell cycle arrest and regulate androgen receptor (AR) expression, the mechanism by which these events occur is unknown. To develop a better understanding of the effect of DBM on cancer cells, we analyzed changes in protein expression induced by DBM in LNCaP cells using two‐dimensional (2‐D) gel electrophoresis. The proteomic approach used to study LNCaP cells has lead to the analysis and identification of a number of protein species that increase or decrease as a result of exposure to DBM. In particular, twenty features were found to be differentially expressed in this study based on the quantitation of two separate 2‐D‐fluorescence difference gel electrophoresis analyses. Thirteen of these features were identified through mass spectrometric analysis. The intensity of 10 out of the 13 spots identified increased 2‐ to 3‐fold in response to 25 µM and 50 µM DBM and the remaining three spots decreased 2‐fold in response to the same DBM treatment. This study investigates proteomic changes induced by treatment of cells with DBM in order to develop a model for the mechanism by which DBM induces cell cycle arrest and represses AR expression.