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Expert Rev Vaccines. 2008 Sep;7(7):1019-30. doi: 10.1586/14760584.7.7.1019.

Heat-shock proteins in cancer vaccines: agents of antigen cross-presentation.

Author information

1
Department of Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA. amurshid@bidmc.harvard.edu

Abstract

Heat-shock proteins (HSPs) derived from tumors are capable of eliciting an anticancer immune response by facilitating antigen cross-presentation in antigen-presenting cells (APCs). This process involves the ability of such chaperones to bind tumor antigens and facilitate their uptake by APCs. Recent evidence reveals that HSP-tumor antigen complexes bind cell surface proteins on APCs that mediate complex internalization and antigen-processing events, as well as inducing an innate immune response. Binding of HSPs to surface receptors is, thus, an imposing gateway to the induction of tumor-specific immune responses. Extensive studies in animals have indicated the usefulness of such HSP-based immunotherapy in killing established tumors and causing tumor regression. Currently, one HSP, the endoplasmic reticulum stress-response protein Gp96 is undergoing clinical trials for cancer treatment and has yielded promising results, including the induction of anti-tumor immunity and some benefit for patients when administered as part of a multidose regimen. Future advances in HSP-based immunotherapy will be aided by an understanding of the mechanisms by which HSP-peptide complexes induce innate and adaptive immunity to tumor cells and target the killing of primary and metastatic cancer cells.

PMID:
18767951
DOI:
10.1586/14760584.7.7.1019
[Indexed for MEDLINE]

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