Heat shock proteins: linking danger and pathogen recognition
- 19 July 2007
- journal article
- review article
- Published by Springer Nature in Medical Microbiology and Immunology
- Vol. 197 (1) , 1-8
- https://doi.org/10.1007/s00430-007-0055-0
Abstract
Besides their central function in protein folding and transport within the cell, heat shock proteins (HSP) have been shown to modulate innate and adaptive immune response: (1) HSP mediate uptake and MHC presentation of HSP-associated peptides by antigen-presenting cells (APC). (2) HSP function as endogenous danger signals indicating cell stress and tissue damage to the immune system. (3) HSP bind pathogen-associated molecular pattern (PAMP) molecules and modulate PAMP-induced Toll-like receptor (TLR) signaling. Thus, HSP contribute to both, recognition of “danger” defined as uncontrolled tissue destruction and recognition of dangerous “nonself”. In this review these different aspects of immune stimulation by HSP will be discussed.Keywords
This publication has 68 references indexed in Scilit:
- Enhanced T-cell immunity induced by dendritic cells with phagocytosis of heat shock protein 70 gene-transfected tumor cells in early phase of apoptosisCancer Gene Therapy, 2007
- TLR signalingCell Death & Differentiation, 2006
- The heat‐shock protein receptors: some answers and more questionsTissue Antigens, 2004
- Induction of cytokines by heat shock proteins and endotoxin in murine macrophagesBiochemical and Biophysical Research Communications, 2004
- The heat shock protein Gp96 binds to human neutrophils and monocytes and stimulates effector functionsBlood, 2003
- The immune system evolved to discriminate infectious nonself from noninfectious selfPublished by Elsevier ,2003
- Endotoxin Contamination in Recombinant Human Heat Shock Protein 70 (Hsp70) Preparation Is Responsible for the Induction of Tumor Necrosis Factor α Release by Murine MacrophagesJournal of Biological Chemistry, 2003
- The Endoplasmic Reticulum-resident Heat Shock Protein Gp96 Activates Dendritic Cells via the Toll-like Receptor 2/4 PathwayJournal of Biological Chemistry, 2002
- HSP70 as Endogenous Stimulus of the Toll/Interleukin-1 Receptor Signal PathwayJournal of Biological Chemistry, 2002
- HEAT-SHOCK PROTEINS, MOLECULAR CHAPERONES, AND THE STRESS RESPONSE: Evolutionary and Ecological PhysiologyAnnual Review of Physiology, 1999