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I NTERACTION OF H EAT S HOCK P ROTEINS WITH P EPTIDES AND A NTIGEN P RESENTING C ELLS : Chaperoning of the Innate and Adaptive Immune Responses

I NTERACTION OF H EAT S HOCK P ROTEINS WITH P EPTIDES AND A NTIGEN P RESENTING C ELLS :... ▪ Abstract Heat shock proteins are abundant soluble intracellular proteins, present in all cells. Members of the heat shock protein family bind peptides including antigenic peptides generated within cells. Heat shock proteins also interact with antigen presenting cells through CD91 and other receptors, eliciting a cascade of events including re-presentation of heat shock protein-chaperoned peptides by MHC, translocation of NFκB into the nuclei and maturation of dendritic cells. These consequences point to a key role of heat shock proteins in fundamental immunological phenomena such as activation of antigen presenting cells, indirect presentation (or cross-priming), and chaperoning of peptides during antigen presentation. Heat shock proteins appear to have been involved in innate immune responses since the emergence of phagocytes in early multicellular organisms and to have been commandeered for adaptive immune responses with the advent of specificity. These properties of heat shock proteins also allow them to be used for immunotherapy of cancers and infections in novel ways. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Immunology Annual Reviews

I NTERACTION OF H EAT S HOCK P ROTEINS WITH P EPTIDES AND A NTIGEN P RESENTING C ELLS : Chaperoning of the Innate and Adaptive Immune Responses

Annual Review of Immunology , Volume 20 (1) – Apr 1, 2002

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Publisher
Annual Reviews
Copyright
Copyright © 2002 by Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0732-0582
eISSN
1545-3278
DOI
10.1146/annurev.immunol.20.100301.064801
pmid
11861608
Publisher site
See Article on Publisher Site

Abstract

▪ Abstract Heat shock proteins are abundant soluble intracellular proteins, present in all cells. Members of the heat shock protein family bind peptides including antigenic peptides generated within cells. Heat shock proteins also interact with antigen presenting cells through CD91 and other receptors, eliciting a cascade of events including re-presentation of heat shock protein-chaperoned peptides by MHC, translocation of NFκB into the nuclei and maturation of dendritic cells. These consequences point to a key role of heat shock proteins in fundamental immunological phenomena such as activation of antigen presenting cells, indirect presentation (or cross-priming), and chaperoning of peptides during antigen presentation. Heat shock proteins appear to have been involved in innate immune responses since the emergence of phagocytes in early multicellular organisms and to have been commandeered for adaptive immune responses with the advent of specificity. These properties of heat shock proteins also allow them to be used for immunotherapy of cancers and infections in novel ways.

Journal

Annual Review of ImmunologyAnnual Reviews

Published: Apr 1, 2002

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