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Autoimmune Diseases
Volume 2012, Article ID 486069, 10 pages
Review Article

Heat Shock Proteins, Autoimmunity, and Cancer Treatment

Division of Molecular and Cellular Biology, Department of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 99 Brookline Avenue, Boston, MA 02215, USA

Received 16 July 2012; Accepted 27 August 2012

Academic Editor: Kamal D. Moudgil

Copyright © 2012 Stuart K. Calderwood et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Heat shock proteins (HSPs) have been linked to the therapy of both cancer and inflammatory diseases, approaches that utilize contrasting immune properties of these proteins. It would appear that HSP family members Hsp60 and Hsp70, whether from external sources or induced locally during inflammation, can be processed by antigen-presenting cells and that HSP-derived epitopes then activate regulatory T cells and suppress inflammatory diseases. These effects also extend to the HSP-rich environments of cancer cells where elevated HSP concentrations may participate in the immunosuppressive tumor milieu. However, HSPs can also be important mediators of tumor immunity. Due to their molecular chaperone properties, some HSPs can bind tumor-specific peptides and deliver them deep into the antigen-processing pathways of antigen-presenting cells (APCs). In this context, HSP-based vaccines can activate tumor-specific immunity, trigger the proliferation and CTL capabilities of cancer-specific CD8+ T cells, and inhibit tumor growth. Further advances in HSP-based anticancer immunotherapy appear to involve improving the properties of the molecular chaperone vaccines by enhancing their antigen-binding properties and combating the immunosuppressive tumor milieu to permit programming of active CTL capable of penetrating the tumor milieu and specifically targeting tumor cells.