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Heat Shock Proteins Modulate Keloid Formation
Objective: Heat shock proteins (HSPs) modulate the intensity of the inflammatory and synthetic response to stress in wound healing. Induction of HSPs at the site of wounds improves healing by acting as a molecular chaperone. However, the role of HSPs may augment the inflammatory response, leading to...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Open Science Company, LLC
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086522/ https://www.ncbi.nlm.nih.gov/pubmed/21559318 |
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author | Totan, Serhat Echo, Anthony Yuksel, Eser |
author_facet | Totan, Serhat Echo, Anthony Yuksel, Eser |
author_sort | Totan, Serhat |
collection | PubMed |
description | Objective: Heat shock proteins (HSPs) modulate the intensity of the inflammatory and synthetic response to stress in wound healing. Induction of HSPs at the site of wounds improves healing by acting as a molecular chaperone. However, the role of HSPs may augment the inflammatory response, leading to an uncontrolled synthetic process. Propensity for keloid development involves genetic predisposition, physical factors, and an aggressive inflammatory response. The aim of this study is to demonstrate the differential expressions of HSPs in keloid and normal tissues. Methods: Twenty-five keloid and adjacent normal tissue samples were removed from 24 patients who were between 16 and 45 years of age. Western blot, enzyme-linked immunosorbent assay, and immunofluorescence studies were performed to examine hsp27, hsp47, hsp60, hsp70, and hsp90 levels in keloid and normal tissue. Results: Our results demonstrated a significant overexpression of hsp27, hsp47, and hsp70 in keloid tissue compared to that of normal tissue. Statistical analysis using the Student t test revealed a significant difference between these 2 groups (P < .01), while the expression of hsp60 and hsp90 were not significantly different between the keloid and normal tissue samples. Conclusion: The overexpression of HSPs indicates that both a proliferative (hsp70) and a matrix synthesis (hsp47, hsp27) component are present in keloid tissue. From this point of view, it is probable that HSPs play a pivotal role in keloid formation. Unveiling HSP-keloid interactions may allow us to manipulate the inflammatory and proliferative phases of wound healing with the potential to control keloid formation. |
format | Text |
id | pubmed-3086522 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Open Science Company, LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-30865222011-05-10 Heat Shock Proteins Modulate Keloid Formation Totan, Serhat Echo, Anthony Yuksel, Eser Eplasty Journal Article Objective: Heat shock proteins (HSPs) modulate the intensity of the inflammatory and synthetic response to stress in wound healing. Induction of HSPs at the site of wounds improves healing by acting as a molecular chaperone. However, the role of HSPs may augment the inflammatory response, leading to an uncontrolled synthetic process. Propensity for keloid development involves genetic predisposition, physical factors, and an aggressive inflammatory response. The aim of this study is to demonstrate the differential expressions of HSPs in keloid and normal tissues. Methods: Twenty-five keloid and adjacent normal tissue samples were removed from 24 patients who were between 16 and 45 years of age. Western blot, enzyme-linked immunosorbent assay, and immunofluorescence studies were performed to examine hsp27, hsp47, hsp60, hsp70, and hsp90 levels in keloid and normal tissue. Results: Our results demonstrated a significant overexpression of hsp27, hsp47, and hsp70 in keloid tissue compared to that of normal tissue. Statistical analysis using the Student t test revealed a significant difference between these 2 groups (P < .01), while the expression of hsp60 and hsp90 were not significantly different between the keloid and normal tissue samples. Conclusion: The overexpression of HSPs indicates that both a proliferative (hsp70) and a matrix synthesis (hsp47, hsp27) component are present in keloid tissue. From this point of view, it is probable that HSPs play a pivotal role in keloid formation. Unveiling HSP-keloid interactions may allow us to manipulate the inflammatory and proliferative phases of wound healing with the potential to control keloid formation. Open Science Company, LLC 2011-04-29 /pmc/articles/PMC3086522/ /pubmed/21559318 Text en Copyright © 2011 The Author(s) http://creativecommons.org/licenses/by/2.0/ This is an open-access article whereby the authors retain copyright of the work. The article is 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 | Journal Article Totan, Serhat Echo, Anthony Yuksel, Eser Heat Shock Proteins Modulate Keloid Formation |
title | Heat Shock Proteins Modulate Keloid Formation |
title_full | Heat Shock Proteins Modulate Keloid Formation |
title_fullStr | Heat Shock Proteins Modulate Keloid Formation |
title_full_unstemmed | Heat Shock Proteins Modulate Keloid Formation |
title_short | Heat Shock Proteins Modulate Keloid Formation |
title_sort | heat shock proteins modulate keloid formation |
topic | Journal Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086522/ https://www.ncbi.nlm.nih.gov/pubmed/21559318 |
work_keys_str_mv | AT totanserhat heatshockproteinsmodulatekeloidformation AT echoanthony heatshockproteinsmodulatekeloidformation AT yukseleser heatshockproteinsmodulatekeloidformation |