Tumor immunotherapy based on tumor-derived heat shock proteins (Review)

Heat shock proteins (HSPs), the most important type of molecular chaperone, are expressed in all eukaryotic cells and have multiple functions, including the folding and unfolding of other proteins and peptides, the transport of proteins and peptides and the support of antigen presentation processes....

Full description

Saved in:
Bibliographic Details
Published inOncology letters Vol. 6; no. 6; pp. 1543 - 1549
Main Authors ZHANG, YUNFEI, ZHENG, LIANHE
Format Journal Article
LanguageEnglish
Published Greece D.A. Spandidos 01.12.2013
Spandidos Publications UK Ltd
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Heat shock proteins (HSPs), the most important type of molecular chaperone, are expressed in all eukaryotic cells and have multiple functions, including the folding and unfolding of other proteins and peptides, the transport of proteins and peptides and the support of antigen presentation processes. Due to these important properties, the use of HSPs has been explored as a promising tumor immunotherapy strategy. It has been previously demonstrated that HSP peptide complex (HSP.PC) derived from tumors is the immunogenic entity that elicits powerful antitumor immune responses. Previous animal studies and phase III clinical trials have demonstrated the efficacy, safety and feasibility of HSP-based tumor vaccines. However, the limitations are also apparent and specific alternatives have been developed. The present review focused on the history of HSP-based immunotherapy, the mechanism of its immunogenicity and the previous efforts to promote the efficacy. The current review may be useful for antitumor studies based on the tumor-derived HSPs.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ISSN:1792-1074
1792-1082
DOI:10.3892/ol.2013.1616