Heat shock proteins HSP70 and GP96: structural insights

Springer Science and Business Media LLC - Tập 55 - Trang 339-346 - 2005
John G. Facciponte1, Xiang-Yang Wang2,3, Ian J. MacDonald2, Jun-eui Park4, Hilal Arnouk5, Melissa J. Grimm2, Ying Li1, Hyung Kim6,3, Masoud H. Manjili7, Douglas P. Easton8, John R. Subjeck2
1Department of Immunology, Roswell Park Cancer Institute, Buffalo, USA
2Department of Cellular Stress Biology, Roswell Park Cancer Institute, Buffalo, USA
3Department of Urology, Roswell Park Cancer Institute, Buffalo, USA
4Department of Medicine and Swim Across America Laboratory, Memorial Sloan-Kettering Cancer Center, New York, USA
5Department of Pathology, Roswell Park Cancer Institute, Buffalo, USA
6Department of Surgery, Roswell Park Cancer Institute, Buffalo, USA
7Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, USA
8Department of Biology, State University of New York, Buffalo, USA

Tóm tắt

Several heat shock proteins (HSPs) act as potent adjuvants for eliciting anti-tumor immunity. HSP-based tumor vaccine strategies have been highly successful in animal models and are undergoing testing in clinical trials. It is generally accepted that HSPs, functioning as chaperones for tumor antigens, elicit tumor-specific adaptive immune responses. HSPs also appear to induce innate immune responses in an antigen-independent fashion. Innate responses generated by HSPs may contribute to anti-tumor immunity. Immunologically active chaperones with anti-tumor activity are referred to as “immunochaperones”. Here, we review the studies that address the role of structural domains or regions of the immunochaperones HSP70 and GP96 that may be involved in the induction of adaptive or innate immune responses.

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