PROTEOMICS INSIGHTS INTO MOLECULAR MECHANISMS OF TRIPTOLIDE AGAINST COLORECTAL CANCER

Triptolide, a diterpene triepoxide extracted from traditional Chinese medicinal plant, Leigongteng, has been shown to have strong anti-tumor activities. However, the molecular mechanisms of triptolide against colorectal cancer remains largely elusive to date. In my study, triptolide was demonstrated to interfere with ROS, actin cytoskeleton, cell migration, cell adhesion, protein synthesis and induce alteration of transcription factors in colorectal cancer cell line HCT 116. In my first project, protein alterations of HCT 116 cells treated with triptolide were profiled at a global level, by using Isobaric Tags for Relative and Absolute Quantitation (iTRAQ) labeling followed by MS/MS analysis. The study of networks provides some insight into the molecular mechanisms of triptolide against colorectal cancer. In my second project, direct binding targets of triptolide were identified, by using combination of Activity-based Protein Profiling (ABPP) and proteomic approaches. Peroxiredoxin I and Annexin A1 were validated to be the direct binding targets of triptolide. Proteomics approaches allows the study of altered proteins by triptolide and binding targets of triptolide at a global level, which provides some insight into the mechanism of action of triptolide and aid to identify potential targets for cancer therapy.

Author dc:creator

• LI JINGLIN

• triptolide, proteomics, iTRAQ, colorectal cancer, mechanism, target