IGF1 promotes resistance to apoptosis in melanoma cells through an increased expression of BCL2, BCL-X(L), and survivin.

作者: Caroline Hilmi , Lionel Larribere , Sandy Giuliano , Karine Bille , Jean-Paul Ortonne

DOI: 10.1038/SJ.JID.5701185

关键词:

摘要: IGF1 plays a key role in the development and growth of multiple tumors prevention apoptosis. In melanoma cells, has been shown to mediate resistance anoikis-induced However, effect on other proapoptotic stimuli never reported. Further, molecular mechanisms by which mediates its prosurvival properties cells remain unknown. Here, we demonstrate that impairs onset tumor necrosis factor–related apoptosis-inducing ligand staurosporine-induced apoptosis expressing either wild-type or oncogenic B-Raf. show inhibits mitochondrial damage occurs during apoptosis, thereby indicating acts at level mitochondria antiapoptotic stimuli. Accordingly, increases mRNA levels protein expression members BCL2 family—BCL2 BCL-X(L)—and inhibitor protein, survivin. their specific silencing small interfering RNA prevents protective IGF1. These findings therefore delineate provide basis for clinical strategies designed neutralize target genes.

参考文章(30)
Erika Cretney, Kazuyoshi Takeda, Hideo Yagita, Moira Glaccum, Jacques J. Peschon, Mark J. Smyth, Increased Susceptibility to Tumor Initiation and Metastasis in TNF-Related Apoptosis-Inducing Ligand-Deficient Mice Journal of Immunology. ,vol. 168, pp. 1356- 1361 ,(2002) , 10.4049/JIMMUNOL.168.3.1356
Nancy E Dagdigian, Walter A Blättler, Thomas Chittenden, Lisa M Garrett, Erin K Maloney, Rajeeva Singh, Katherine M Connors, Xiao-Mai Zhou, Jennifer L McLaughlin, An anti-insulin-like growth factor I receptor antibody that is a potent inhibitor of cancer cell proliferation. Cancer Research. ,vol. 63, pp. 5073- 5083 ,(2003)
L Larribere, M Khaled, S Tartare-Deckert, R Busca, F Luciano, K Bille, G Valony, A Eychene, P Auberger, J P Ortonne, R Ballotti, C Bertolotto, PI3K mediates protection against TRAIL-induced apoptosis in primary human melanocytes. Cell Death & Differentiation. ,vol. 11, pp. 1084- 1091 ,(2004) , 10.1038/SJ.CDD.4401475
Guido Kroemer, Naoufal Zamzami, Santos A. Susin, Mitochondrial control of apoptosis Immunology Today. ,vol. 18, pp. 44- 51 ,(1997) , 10.1016/S0167-5699(97)80014-X
William C. Earnshaw, Luis M. Martins, Scott H. Kaufmann, Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis Annual Review of Biochemistry. ,vol. 68, pp. 383- 424 ,(1999) , 10.1146/ANNUREV.BIOCHEM.68.1.383
Adda Grimberg, Mechanisms by which IGF-I may promote cancer. Cancer Biology & Therapy. ,vol. 2, pp. 630- 635 ,(2003) , 10.4161/CBT.2.6.678
Fengzhi Li, Xiang Ling, Survivin study: An update of “What is the next wave?” Journal of Cellular Physiology. ,vol. 208, pp. 476- 486 ,(2006) , 10.1002/JCP.20634
Elisabeth Heere-Ress, Christiane Thallinger, Trevor Lucas, Hermine Schlagbauer-Wadl, Volker Wacheck, Brett P. Monia, Klaus Wolff, Hubert Pehamberger, Burkhard Jansen, Bcl‐XL is a chemoresistance factor in human melanoma cells that can be inhibited by antisense therapy International Journal of Cancer. ,vol. 99, pp. 29- 34 ,(2002) , 10.1002/IJC.10248
Marcus E Peter, Peter H Krammer, Mechanisms of CD95 (APO-1/Fas)-mediated apoptosis Current Opinion in Immunology. ,vol. 10, pp. 545- 551 ,(1998) , 10.1016/S0952-7915(98)80222-7
Frank C. Kischkel, David A. Lawrence, Antoine Tinel, Heidi LeBlanc, Arvind Virmani, Peter Schow, Adi Gazdar, John Blenis, David Arnott, Avi Ashkenazi, Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. Journal of Biological Chemistry. ,vol. 276, pp. 46639- 46646 ,(2001) , 10.1074/JBC.M105102200