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Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes
Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutiv...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6882751/ https://www.ncbi.nlm.nih.gov/pubmed/31734893 http://dx.doi.org/10.1007/s12192-019-01044-5 |
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author | Scieglinska, Dorota Krawczyk, Zdzisław Sojka, Damian Robert Gogler-Pigłowska, Agnieszka |
author_facet | Scieglinska, Dorota Krawczyk, Zdzisław Sojka, Damian Robert Gogler-Pigłowska, Agnieszka |
author_sort | Scieglinska, Dorota |
collection | PubMed |
description | Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes. |
format | Online Article Text |
id | pubmed-6882751 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-68827512019-12-12 Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes Scieglinska, Dorota Krawczyk, Zdzisław Sojka, Damian Robert Gogler-Pigłowska, Agnieszka Cell Stress Chaperones Mini Review Heat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes. Springer Netherlands 2019-11-16 2019-11 /pmc/articles/PMC6882751/ /pubmed/31734893 http://dx.doi.org/10.1007/s12192-019-01044-5 Text en © The Author(s) 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Mini Review Scieglinska, Dorota Krawczyk, Zdzisław Sojka, Damian Robert Gogler-Pigłowska, Agnieszka Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
title | Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
title_full | Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
title_fullStr | Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
title_full_unstemmed | Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
title_short | Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
title_sort | heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6882751/ https://www.ncbi.nlm.nih.gov/pubmed/31734893 http://dx.doi.org/10.1007/s12192-019-01044-5 |
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