Heat Shock Proteins and Inflammation

by Willem van Eden (Editor)

Overview

Heat shock proteins (HSP) have received ample interest by immunologists over recent years. Initially they were found to be dominantly immunogenic microbial antigens. The connection with inflammation was established when it was uncovered that T cells specific for these antigens have a crucial role in the induction and regulation of experimental arthritis. Since then, the raised presence of immunity to HSPs in virtually all conditions of inflammation, including autoimmune diseases, transplant rejection and atherosclerosis, has emphasised the critical significance of immunity to HSPs in inflammatory diseases.

Product Details

ISBN-13:	9783764369323
Publisher:	Birkhäuser Basel
Publication date:	01/12/2004
Series:	Progress in Inflammation Research
Edition description:	2003
Pages:	280
Product dimensions:	6.10(w) x 9.25(h) x (d)

Table of Contents

HSP60 and the regulation of inflammation: Physiological and pathological.- Heat shock proteins and suppression of inflammation.- Heat shock proteins in immune response.- Heat shock protein-mediated activation of innate immune cells.- Eukaryotic HSP60: A “danger signal” for T- and natural killer cells.- Heat shock proteins and experimental arthritis.- Heat shock proteins and reactive arthritis.- The development of immune therapy with HSP60 for juvenile idiopathic arthritis.- Heat shock proteins and rheumatoid arthritis.- Heat shock proteins for immunotherapy of rheumatoid arthritis.- Immunity to heat shock proteins and atherosclerosis.- Chaperonins: Chameleon proteins that influence myeloid cells.- Heat shock protein receptors, functions and their effect on monocytes and dendritic cells.- Heat shock protein expression in transplanted kidney.- Mycobacterial heat shock proteins and the bovine immune system.- Microbial infection generates pro-inflammatory autoimmunity against the small heat shock protein alpha B-crystallin and provides the fuel for the development of multiple sclerosis.- HSP60-peptide interference with CD94/NKG2 receptors.