Proteomic study reveals a co-occurrence of gallic acid-induced apoptosis and glycolysis in B16F10 melanoma cells.
Gallic acid (GA) has long been associated with a wide range of biological activities. In this study, its antitumor effect against B16F10 melanoma cells was demonstrated by MTT assay, cell migration assay, wound-healing assay, and flow cytometric analysis. GA with a concentration >200 μM shows apoptotic activity toward B16F10 cells. According to Western blotting data, overexpressions of cleaved forms of caspase-9, caspase-3, and PARP-1 and pro-apoptotic Bax and Bad, accompanied by underexpressed anti-apoptotic Bcl-2 and Bcl-xL indicate that GA induces B16F10 cell apoptosis via mitochondrial pathway. The 2-DE based comparative proteomics was further employed in B16F10 cells with and without GA treatment for a large-scale protein expression profiling. A total of 41 differential protein spots were quantified, and their identities were characterized using LC-MS/MS analysis and database matching. In addition to some regulated proteins that were associated with apoptosis, interestingly, some identified proteins involved in glycolysis such as glucokinase, α-enolase, aldolase, pyruvate kinase, and GAPDH were simultaneously up-regulated, which reveals that the GA-induced cellular apoptosis in B16 melanoma cells is associated with metabolic glycolysis.
['Liu|Cheng|C|', 'Lin|Jen-Jie|JJ|', 'Yang|Zih-Yan|ZY|', 'Tsai|Chi-Chu|CC|', 'Hsu|Jue-Liang|JL|', 'Wu|Yu-Jen|YJ|']
D053148:Caspase 3 D045744:Cell Line, Tumor D049109:Cell Proliferation D005707:Gallic Acid D006019:Glycolysis D006801:Humans D008545:Melanoma D008928:Mitochondria D040901:Proteomics D019253:Proto-Oncogene Proteins c-bcl-2 D051028:bcl-2-Associated X Protein
proteomics apoptosis glycolysis gallic acid 2-DE mitochondrial dysfunction