Hsp70: Anti-apoptotic and Tumorigenic Protein

作者: Anne-Laure Rérole , Gaëtan Jego , Carmen Garrido

DOI: 10.1007/978-1-61779-295-3_16

关键词:

摘要: Heat shock protein 70 (Hsp70) is a powerful chaperone whose expression induced in response to wide variety of physiological and environmental insults, including anticancer chemotherapy, thus allowing the cell survive lethal conditions. Hsp70 cytoprotective properties may be explained by its anti-apoptotic function. Indeed, this can inhibit key effectors apoptotic machinery at pre- postmitochondrial level. In cancer cells, abnormally high, participate oncogenesis resistance chemotherapy. rodent models, overexpression increases tumor growth metastatic potential. Depletion or inhibition frequently reduces size tumors even cause their complete involution. But also found extracellular medium. Its role then immunogenic term chaperokine define chaperones has been advanced. tumorigenic functions as well strategies that are being developed therapy order commented chapter.

参考文章(200)
Scott H. Kaufmann, The Intrinsic Pathway of Apoptosis Humana Press. pp. 3- 30 ,(2007) , 10.1007/978-1-59745-221-2_1
R. I. Morimoto, B. S. Polla, U. Feige, I. Yahara, Stress-Inducible Cellular Responses ,(2011)
Maria A. Bausero, Robert Gastpar, Gabriele Multhoff, Alexzander Asea, Alternative Mechanism by which IFN-γ Enhances Tumor Recognition: Active Release of Heat Shock Protein 72 The Journal of Immunology. ,vol. 175, pp. 2900- 2912 ,(2005) , 10.4049/JIMMUNOL.175.5.2900
G. C. Tsokos, S.-N. C. Liossis, J. G. Kiang, X. Z. Ding, Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells. Journal of Immunology. ,vol. 158, pp. 5668- 5675 ,(1997)
Salamatu S. Mambula, Stuart K. Calderwood, Heat Shock Protein 70 Is Secreted from Tumor Cells by a Nonclassical Pathway Involving Lysosomal Endosomes Journal of Immunology. ,vol. 177, pp. 7849- 7857 ,(2006) , 10.4049/JIMMUNOL.177.11.7849
Alexzander Asea, Stine-Kathrein Kraeft, Evelyn A. Kurt-Jones, Mary Ann Stevenson, Lan Bo Chen, Robert W. Finberg, Gloria C. Koo, Stuart K. Calderwood, HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nature Medicine. ,vol. 6, pp. 435- 442 ,(2000) , 10.1038/74697
Christopher V. Nicchitta, Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity. Nature Reviews Immunology. ,vol. 3, pp. 427- 432 ,(2003) , 10.1038/NRI1089
Amy D. H. Doody, Joseph T. Kovalchin, Marianne A. Mihalyo, Adam T. Hagymasi, Charles G. Drake, Adam J. Adler, Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function The Journal of Immunology. ,vol. 172, pp. 6087- 6092 ,(2004) , 10.4049/JIMMUNOL.172.10.6087
Georg Schett, Carl-Walter Steiner, Marion Gröger, Stefan Winkler, Winfried Graninger, Josef Smolen, Qingbo Xu, Günter Steiner, None, Activation of Fas inhibits heat-induced activation of HSF1 and up-regulation of hsp70 The FASEB Journal. ,vol. 13, pp. 833- 842 ,(1999) , 10.1096/FASEBJ.13.8.833
Yutaka Enomoto, Ajit Bharti, Ad Abdul Khaleque, Baizheng Song, Chunlei Liu, Vasso Apostolopoulos, Pei-xiang Xing, Stuart K. Calderwood, Jianlin Gong, Enhanced Immunogenicity of Heat Shock Protein 70 Peptide Complexes from Dendritic Cell-Tumor Fusion Cells Journal of Immunology. ,vol. 177, pp. 5946- 5955 ,(2006) , 10.4049/JIMMUNOL.177.9.5946