ER Stress Proteins in Autoimmune and Inflammatory Diseases

Over the past two decades, heat shock proteins (HSPs) have been implicated in inflammatory responses and autoimmunity. HSPs were originally believed to maintain protein quality control in the cytosol. However, they also exist extracellularly and appear to act as inflammatory factors. Recently, a gro...

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Main Authors:	Morito, Daisuke, Nagata, Kazuhiro
Format:	Online
Language:	English
Published:	Frontiers Research Foundation 2012
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3342303/

id	pubmed-3342303
recordtype	oai_dc
spelling	pubmed-33423032012-05-07 ER Stress Proteins in Autoimmune and Inflammatory Diseases Morito, Daisuke Nagata, Kazuhiro Immunology Over the past two decades, heat shock proteins (HSPs) have been implicated in inflammatory responses and autoimmunity. HSPs were originally believed to maintain protein quality control in the cytosol. However, they also exist extracellularly and appear to act as inflammatory factors. Recently, a growing body of evidence suggested that the other class of stress proteins such as, endoplasmic reticulum (ER) stress proteins, which originally act as protein quality control factors in the secretory pathway and are induced by ER stress in inflammatory lesions, also participate in inflammation and autoimmunity. The immunoglobulin heavy-chain binding protein (Bip)/glucose-regulated protein 78 (GRP78), calnexin, calreticulin, glucose-regulated protein 94 (GRP94)/gp96, oxygen regulated protein 150 (ORP150)/glucose-regulated protein 170 (GRP170), homocysteine-induced ER protein (Herp) and heat shock protein 47 (hsp47)/Serpin H1, which are expressed not only in the ER but also occasionally at the cell surface play pathophysiological roles in autoimmune and inflammatory diseases as pro- or anti-inflammatory factors. Here we describe the accumulating evidence of the participation of ER stress proteins in autoimmunity and inflammation and discuss the critical differences between the two classes of stress proteins. Frontiers Research Foundation 2012-03-15 /pmc/articles/PMC3342303/ /pubmed/22566930 http://dx.doi.org/10.3389/fimmu.2012.00048 Text en Copyright © 2012 Morito and Nagata. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Morito, Daisuke Nagata, Kazuhiro
spellingShingle	Morito, Daisuke Nagata, Kazuhiro ER Stress Proteins in Autoimmune and Inflammatory Diseases
author_facet	Morito, Daisuke Nagata, Kazuhiro
author_sort	Morito, Daisuke
title	ER Stress Proteins in Autoimmune and Inflammatory Diseases
title_short	ER Stress Proteins in Autoimmune and Inflammatory Diseases
title_full	ER Stress Proteins in Autoimmune and Inflammatory Diseases
title_fullStr	ER Stress Proteins in Autoimmune and Inflammatory Diseases
title_full_unstemmed	ER Stress Proteins in Autoimmune and Inflammatory Diseases
title_sort	er stress proteins in autoimmune and inflammatory diseases
description	Over the past two decades, heat shock proteins (HSPs) have been implicated in inflammatory responses and autoimmunity. HSPs were originally believed to maintain protein quality control in the cytosol. However, they also exist extracellularly and appear to act as inflammatory factors. Recently, a growing body of evidence suggested that the other class of stress proteins such as, endoplasmic reticulum (ER) stress proteins, which originally act as protein quality control factors in the secretory pathway and are induced by ER stress in inflammatory lesions, also participate in inflammation and autoimmunity. The immunoglobulin heavy-chain binding protein (Bip)/glucose-regulated protein 78 (GRP78), calnexin, calreticulin, glucose-regulated protein 94 (GRP94)/gp96, oxygen regulated protein 150 (ORP150)/glucose-regulated protein 170 (GRP170), homocysteine-induced ER protein (Herp) and heat shock protein 47 (hsp47)/Serpin H1, which are expressed not only in the ER but also occasionally at the cell surface play pathophysiological roles in autoimmune and inflammatory diseases as pro- or anti-inflammatory factors. Here we describe the accumulating evidence of the participation of ER stress proteins in autoimmunity and inflammation and discuss the critical differences between the two classes of stress proteins.
publisher	Frontiers Research Foundation
publishDate	2012
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3342303/
_version_	1611526566739705856

ER Stress Proteins in Autoimmune and Inflammatory Diseases

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