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Size dependent classification of heat shock proteins: a mini-review
Molecular chaperones are ubiquitous and abundant within cellular environments, functioning as a defense mechanism against outer environment. The range of molecular chaperones varies from 10 to over 100 kDa. Depending on the size, the specific locations and physiological roles of molecular chaperones...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Korean Society of Exercise Rehabilitation
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5031383/ https://www.ncbi.nlm.nih.gov/pubmed/27656620 http://dx.doi.org/10.12965/jer.1632642.321 |
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author | Jee, Hyunseok |
author_facet | Jee, Hyunseok |
author_sort | Jee, Hyunseok |
collection | PubMed |
description | Molecular chaperones are ubiquitous and abundant within cellular environments, functioning as a defense mechanism against outer environment. The range of molecular chaperones varies from 10 to over 100 kDa. Depending on the size, the specific locations and physiological roles of molecular chaperones vary within the cell. Multifunctionality of heat shock proteins (HSPs) expressed via various cyto-stress including heat shock have been spotlighted as a reliable prognostic target biomarker for therapeutic purpose in neuromuscular disease or cancer related studies. HSP also plays a critical role in the maintenance of proteins and cellular homeostasis in exercise-induced adaptation. Such various functions of HSPs give scientists insights into intracellular protective mechanisms in the living body thus HSPs can be target molecules to know the defense mechanism in cellular environment. Based on experimental results regarding small to large scaled HSPs, this review aims to provide updated important information regarding the modality of responses of intracellular HSPs towards extracellular stimulations. Further, the expressive mechanisms of HSPs data from tremendous in vivo and in vitro studies underlying the enhancement of the functionality of living body will be discussed. |
format | Online Article Text |
id | pubmed-5031383 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Korean Society of Exercise Rehabilitation |
record_format | MEDLINE/PubMed |
spelling | pubmed-50313832016-09-21 Size dependent classification of heat shock proteins: a mini-review Jee, Hyunseok J Exerc Rehabil Review Article Molecular chaperones are ubiquitous and abundant within cellular environments, functioning as a defense mechanism against outer environment. The range of molecular chaperones varies from 10 to over 100 kDa. Depending on the size, the specific locations and physiological roles of molecular chaperones vary within the cell. Multifunctionality of heat shock proteins (HSPs) expressed via various cyto-stress including heat shock have been spotlighted as a reliable prognostic target biomarker for therapeutic purpose in neuromuscular disease or cancer related studies. HSP also plays a critical role in the maintenance of proteins and cellular homeostasis in exercise-induced adaptation. Such various functions of HSPs give scientists insights into intracellular protective mechanisms in the living body thus HSPs can be target molecules to know the defense mechanism in cellular environment. Based on experimental results regarding small to large scaled HSPs, this review aims to provide updated important information regarding the modality of responses of intracellular HSPs towards extracellular stimulations. Further, the expressive mechanisms of HSPs data from tremendous in vivo and in vitro studies underlying the enhancement of the functionality of living body will be discussed. Korean Society of Exercise Rehabilitation 2016-08-31 /pmc/articles/PMC5031383/ /pubmed/27656620 http://dx.doi.org/10.12965/jer.1632642.321 Text en Copyright © 2016 Korean Society of Exercise Rehabilitation This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Jee, Hyunseok Size dependent classification of heat shock proteins: a mini-review |
title | Size dependent classification of heat shock proteins: a mini-review |
title_full | Size dependent classification of heat shock proteins: a mini-review |
title_fullStr | Size dependent classification of heat shock proteins: a mini-review |
title_full_unstemmed | Size dependent classification of heat shock proteins: a mini-review |
title_short | Size dependent classification of heat shock proteins: a mini-review |
title_sort | size dependent classification of heat shock proteins: a mini-review |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5031383/ https://www.ncbi.nlm.nih.gov/pubmed/27656620 http://dx.doi.org/10.12965/jer.1632642.321 |
work_keys_str_mv | AT jeehyunseok sizedependentclassificationofheatshockproteinsaminireview |