Cover Image

Heat shock protein-peptide complex-96 (Vitespen) for the treatment of cancer

Robert J. Amato
  • Robert J. Amato
    The Methodist Hospital Research Institute Genitourinary Oncology Program Houston, United States | ramato@tmhs.org

Abstract

Heat shock proteins (HSPs) are the most abundant and ubiquitous soluble intracellular proteins. Members of the HSP family bind peptides, they include antigenic peptides generated within cells. HSPs also interact with antigen-presenting cells (APCs) through CD91 and other receptors, eliciting a cascade of events that includes re-presentation of HSP-chaperoned peptides by major histocompatability complex (MHC), translocation of nuclear factorkappaB (NFkB) into the nuclei, and maturation of dendritic cells (DCs). These consequences point to a key role of heat shock proteins in fundamental immunological phenomena such as activation of APCs, indirect presentation (or crosspriming) of antigenic peptides, and chaperoning of peptides during antigen presentation. The properties of HSPs also allow them to be used for immunotherapy of cancers and infections in novel ways. This paper reviews the development and clinical trial progress of vitespen, an HSP peptide complex vaccine based on tumor-derived glycoprotein 96.

Keywords

Cancer - Cross-priming - Dendritic cells - Heat shock proteins - Major histocompatability complex - Autologous tumor-derived

Full Text:

FULL TEXT
Submitted: 2011-12-14 15:39:32
Published: 2011-12-14 00:00:00
Search for citations in Google Scholar
Related articles: Google Scholar
Abstract views:
698

Views:
FULL TEXT
151

Article Metrics

Metrics Loading ...

Metrics powered by PLOS ALM


Copyright (c) 2011 Robert J. Amato

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
 
© PAGEPress 2008-2018     -     PAGEPress is a registered trademark property of PAGEPress srl, Italy.     -     VAT: IT02125780185