Titlebook: Heat Shock Proteins and Inflammation; Willem Eden Book 2003 Springer Basel AG 2003 Activation.Arthritis.bacteria.diseases.immune response.

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Commodious

,Eukaryotic HSP60: A “danger signal” for T- and natural killer cells,hown that HSP purified from tumour and virus infected cells are also capable of eliciting a protective CTL-mediated immunity [.- .]. Preparations of HSP70 and gp96 are able to activate antigen specific T-cells and the uptake of HSP/peptide complexes is most likely mediated by receptors that are expr

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Heat shock proteins and experimental arthritis,sive and destructive features [.]. As yet, the underlying pathogenic mechanisms of RA remain poorly understood. In order to help gain a better understanding of the disease, several animal models of RA have been developed and have been widely studied. Although these models can be very instructive, no

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积习已深

The development of immune therapy with HSP60 for juvenile idiopathic arthritis,sts a dysfunction in the immune regulation, while a spontaneous relapse or remission of disease suggests a successful immune-regulatory process. Understanding the regulatory mechanisms that control the balance between immunity and tolerance can provide potential new targets for therapeutic intervent

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incubus

Immunity to heat shock proteins and atherosclerosis,cific immune responses. In this chapter, we will describe early atherosclerosis as an autoimmune disorder and heat shock protein 60 (HSP60) as the culprit-autoantigen. After a brief review of experimental . data and results from animal experiments, we will focus on clinical data confirming our patho

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Chaperonins: Chameleon proteins that influence myeloid cells,es, plastids and mitochondria and the TCP-1 subfamily found in eukaryotes and the . This chapter will focus on the GroE subfamily which consists of two members: chaperonin (Cpn)60 and the co-chaperone — Cpn10. Both proteins form oligomeric structures required for protein folding [.] and the mechanis

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Heat shock protein receptors, functions and their effect on monocytes and dendritic cells,or folding intermediate polypeptides, chaperons prevent misfolding and aggregation, and promote folding and translocation [.]. Human and microbial HSP70 consist of an N-terminal ATPase fragment of 44 kD and a C-terminal peptide-binding fragment of 28.5 kD. HSP70 is a highly conserved protein among v