S-Palmitoylation as a Functional Regulator of Proteins Associated with Cisplatin Resistance in Bladder Cancer.

作者: Muhammad Shahid , Minhyung Kim , Peng Jin , Bo Zhou , Yang Wang

DOI: 10.7150/IJBS.45640

关键词:

摘要: Protein S-palmitoylation is a powerful post-translational modification that regulates protein trafficking, localization, turnover, and signal transduction. Palmitoylation controls several important cellular processes, and, if dysregulated, can lead to cancer, cardiovascular disease, neurological disorders. The role of palmitoylation in mediating resistance systemic cisplatin-based chemotherapies cancer currently unknown. This particular interest because cisplatin the gold standard treatment for bladder (BC), there are no feasible options after acquired. Using unbiased global proteomic profiling purified S-palmitoylated peptides combined with intensive bioinformatics analyses, we identified 506 candidate palmitoylated proteins significantly enriched cisplatin-resistant BC cells. One these included PD-L1, which highly resistant Pharmacological inhibition fatty acid synthase (FASN) suppressed PD-L1 expression, suggests potential use FASN-PD-L1-targeted therapeutic strategies patients. Taken together, results highlight chemoresistance.

参考文章(70)
Cameron L Noland, Sarah Gierke, Paul D Schnier, Jeremy Murray, Wendy N Sandoval, Meredith Sagolla, Anwesha Dey, Rami N Hannoush, Wayne J Fairbrother, Christian N Cunningham, None, Palmitoylation of TEAD Transcription Factors Is Required for Their Stability and Function in Hippo Pathway Signaling. Structure. ,vol. 24, pp. 179- 186 ,(2016) , 10.1016/J.STR.2015.11.005
Chun-Te Wu, Wen-Cheng Chen, Ying-Hsu Chang, Wei-Yu Lin, Miao-Fen Chen, The role of PD-L1 in the radiation response and clinical outcome for bladder cancer Scientific Reports. ,vol. 6, pp. 19740- 19740 ,(2016) , 10.1038/SREP19740
Tiziano Dallavilla, Laurence Abrami, Patrick A. Sandoz, Georgios Savoglidis, Vassily Hatzimanikatis, F. Gisou van der Goot, Model-Driven Understanding of Palmitoylation Dynamics: Regulated Acylation of the Endoplasmic Reticulum Chaperone Calnexin. PLOS Computational Biology. ,vol. 12, ,(2016) , 10.1371/JOURNAL.PCBI.1004774
William Fuller, Louise Reilly, Donald W Hilgemann, S-palmitoylation and the regulation of NCX1. Channels. ,vol. 10, pp. 75- 77 ,(2016) , 10.1080/19336950.2015.1099329
David T. Coleman, Alana L. Gray, Steven J. Kridel, James A. Cardelli, Palmitoylation regulates the intracellular trafficking and stability of c-Met. Oncotarget. ,vol. 7, pp. 32664- 32677 ,(2016) , 10.18632/ONCOTARGET.8706
Na Cao, Jia-Kai Li, Yu-Qing Rao, Huijuan Liu, Ji Wu, Baojie Li, Peiquan Zhao, Li Zeng, Jing Li, A potential role for protein palmitoylation and zDHHC16 in DNA damage response BMC Molecular Biology. ,vol. 17, pp. 12- 12 ,(2016) , 10.1186/S12867-016-0065-9
Samaisukh Sophasan, Varanuj Chatsudthipong, Surawat Kraisawekwisai, Kidney Pressures after the Release of 24 Hours of Bilateral Ureteral Ligation in the Rat The Journal of Urology. ,vol. 128, pp. 1081- 1086 ,(1982) , 10.1016/S0022-5347(17)53349-2
Damian Szklarczyk, John H Morris, Helen Cook, Michael Kuhn, Stefan Wyder, Milan Simonovic, Alberto Santos, Nadezhda T Doncheva, Alexander Roth, Peer Bork, Lars J. Jensen, Christian von Mering, The STRING database in 2017: quality-controlled protein-protein association networks, made broadly accessible. Nucleic Acids Research. ,vol. 45, pp. 0- ,(2017) , 10.1093/NAR/GKW937
Joseph Murphy, Saravanan Kolandaivelu, Palmitoylation of Progressive Rod-Cone Degeneration (PRCD) Regulates Protein Stability and Localization Journal of Biological Chemistry. ,vol. 291, pp. 23036- 23046 ,(2016) , 10.1074/JBC.M116.742767
Huaiyu Mi, Xiaosong Huang, Anushya Muruganujan, Haiming Tang, Caitlin Mills, Diane Kang, Paul D. Thomas, PANTHER version 11: expanded annotation data from Gene Ontology and Reactome pathways, and data analysis tool enhancements. Nucleic Acids Research. ,vol. 45, ,(2017) , 10.1093/NAR/GKW1138