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Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications

Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic cond...

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Detalles Bibliográficos
Autores principales: Kilic, Arman, Mandal, Kaushik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3530228/
https://www.ncbi.nlm.nih.gov/pubmed/23304456
http://dx.doi.org/10.1155/2012/502813
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author Kilic, Arman
Mandal, Kaushik
author_facet Kilic, Arman
Mandal, Kaushik
author_sort Kilic, Arman
collection PubMed
description Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed.
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spelling pubmed-35302282013-01-09 Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications Kilic, Arman Mandal, Kaushik Autoimmune Dis Review Article Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed. Hindawi Publishing Corporation 2012 2012-12-11 /pmc/articles/PMC3530228/ /pubmed/23304456 http://dx.doi.org/10.1155/2012/502813 Text en Copyright © 2012 A. Kilic and K. Mandal. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Kilic, Arman
Mandal, Kaushik
Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications
title Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications
title_full Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications
title_fullStr Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications
title_full_unstemmed Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications
title_short Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications
title_sort heat shock proteins: pathogenic role in atherosclerosis and potential therapeutic implications
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3530228/
https://www.ncbi.nlm.nih.gov/pubmed/23304456
http://dx.doi.org/10.1155/2012/502813
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