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Heat shock proteins in chronic kidney disease

Heat shock proteins (HSP) form a heterogenous, evolutionarily conserved group of molecules with high sequence homology. They mainly act as intracellular chaperones, protecting the protein structure and folding under stress conditions. The extracellular HSP, released in the course of damage or necros...

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Detalles Bibliográficos
Autores principales: Musiał, Kinga, Zwolińska, Danuta
Formato: Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3098373/
https://www.ncbi.nlm.nih.gov/pubmed/21193931
http://dx.doi.org/10.1007/s00467-010-1709-5
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author Musiał, Kinga
Zwolińska, Danuta
author_facet Musiał, Kinga
Zwolińska, Danuta
author_sort Musiał, Kinga
collection PubMed
description Heat shock proteins (HSP) form a heterogenous, evolutionarily conserved group of molecules with high sequence homology. They mainly act as intracellular chaperones, protecting the protein structure and folding under stress conditions. The extracellular HSP, released in the course of damage or necrosis, play a pivotal role in the innate and adaptive immune responses. They also take part in many pathological processes. The aim of this review is to update the recent developments in the field of HSP in chronic kidney disease (CKD), in regard to three different aspects. The first is the assessment of the role of HSP, either positive or deleterious, in the pathogenesis of CKD and the possibilities to influence its progression. The second is the impact of dialysis, being a potentially modifiable stressor, on HSP and the attempt to assess the value of these proteins as the biocompatibility markers. The last area is that of kidney transplantation and the potential role of HSP in the induction of the immune tolerance in kidney recipients.
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spelling pubmed-30983732011-07-07 Heat shock proteins in chronic kidney disease Musiał, Kinga Zwolińska, Danuta Pediatr Nephrol Review Heat shock proteins (HSP) form a heterogenous, evolutionarily conserved group of molecules with high sequence homology. They mainly act as intracellular chaperones, protecting the protein structure and folding under stress conditions. The extracellular HSP, released in the course of damage or necrosis, play a pivotal role in the innate and adaptive immune responses. They also take part in many pathological processes. The aim of this review is to update the recent developments in the field of HSP in chronic kidney disease (CKD), in regard to three different aspects. The first is the assessment of the role of HSP, either positive or deleterious, in the pathogenesis of CKD and the possibilities to influence its progression. The second is the impact of dialysis, being a potentially modifiable stressor, on HSP and the attempt to assess the value of these proteins as the biocompatibility markers. The last area is that of kidney transplantation and the potential role of HSP in the induction of the immune tolerance in kidney recipients. Springer Berlin Heidelberg 2011-07-01 2011 /pmc/articles/PMC3098373/ /pubmed/21193931 http://dx.doi.org/10.1007/s00467-010-1709-5 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/2.0/Open AccessThis is an open access article distributed under the terms of the Creative Commons Attribution Noncommercial License (https://creativecommons.org/licenses/by-nc/2.0 (https://creativecommons.org/licenses/by-nc/2.0/) ), which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Review
Musiał, Kinga
Zwolińska, Danuta
Heat shock proteins in chronic kidney disease
title Heat shock proteins in chronic kidney disease
title_full Heat shock proteins in chronic kidney disease
title_fullStr Heat shock proteins in chronic kidney disease
title_full_unstemmed Heat shock proteins in chronic kidney disease
title_short Heat shock proteins in chronic kidney disease
title_sort heat shock proteins in chronic kidney disease
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3098373/
https://www.ncbi.nlm.nih.gov/pubmed/21193931
http://dx.doi.org/10.1007/s00467-010-1709-5
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