Authors: | Facciponte, J. G.; Wang, X. Y.; MacDonald, I. J.; Park, J. E.; Arnouk, H.; Grimm, M. J.; Li, Y.; Kim, H.; Manjili, M. H.; Easton, D. P.; Subjeck, J. R. |
Article Title: | Heat shock proteins HSP70 and GP96: Structural insights |
Abstract: | 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. © Springer-Verlag 2005. |
Keywords: | nonhuman; conference paper; binding affinity; protein domain; protein function; neoplasms; animals; antineoplastic activity; structure-activity relationship; tumor antigen; immune response; cancer vaccines; membrane glycoproteins; tumor immunity; innate immunity; heat shock protein 70; adenosine triphosphate; protein structure; adaptive immunity; tumor vaccine; hsp70 heat-shock proteins; heat shock proteins; chaperone; tumor immunology; glycoprotein gp 96; antigen presenting cells; anti-tumor immunity |
Journal Title: | Cancer Immunology, Immunotherapy |
Volume: | 55 |
Issue: | 3 |
ISSN: | 0340-7004 |
Publisher: | Springer |
Date Published: | 2006-03-01 |
Start Page: | 339 |
End Page: | 346 |
Language: | English |
DOI: | 10.1007/s00262-005-0020-y |
PUBMED: | 16032399 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | --- - "Cited By (since 1996): 11" - "Export Date: 4 June 2012" - "CODEN: CIIMD" - "Source: Scopus" |