Heat-shock protein-peptide complex-96 for the treatment of cancer

被引:19
作者
Amato, Robert J. [1 ]
机构
[1] Methodist Hosp, Res Inst, Genitourinary Oncol Program, Houston, TX 77030 USA
关键词
cancer; cross-priming; dendritic cell; heat-shock protein; major histocompatability complex;
D O I
10.1517/14712598.7.8.1267
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Heat-shock proteins (HSPs) are the most abundant and ubiquitous soluble intracellular proteins. Members of the HSP family bind peptides, including antigenic peptides generated within cells. HSPs also interact with antigen-presenting cells (APCs) through CD91 and other receptors, eliciting a cascade of events that includes representation of HSP-chaperoned peptides MHC, translocation of NF-kappa B into the nuclei, and maturation of dendritic cells. These consequences point to a key role of HSPs in fundamental immunologic phenomena such as activation of APCs, indirect presentation (or crosspriming) of antigenic pepticles, and chaperoning of peptides during antigen presentation. The properties of HSPs also allow them to be used for immunotherapy of cancers and infections in novel ways. This paper reviews the development and clinical trial progress of vitespen, an HSP peptide complex vaccine based on tumor-derived glycoprotein 96.
引用
收藏
页码:1267 / 1273
页数:7
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