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Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds

Psoriasin, which is also known as S100A7, is a member of the S100 protein family, a group of calcium-responsive signalling proteins. Psoriasin expression remains high in patients with psoriasis, whereas it is downregulated in patients with invasive breast carcinoma. This observation suggests that th...

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Autores principales: Rangaraj, Aravindan, Ye, Lin, Sanders, Andrew James, Price, Patricia Elaine, Harding, Keith Gordon, Jiang, Wen Guo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: D.A. Spandidos 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5443246/
https://www.ncbi.nlm.nih.gov/pubmed/28565822
http://dx.doi.org/10.3892/etm.2017.4275
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author Rangaraj, Aravindan
Ye, Lin
Sanders, Andrew James
Price, Patricia Elaine
Harding, Keith Gordon
Jiang, Wen Guo
author_facet Rangaraj, Aravindan
Ye, Lin
Sanders, Andrew James
Price, Patricia Elaine
Harding, Keith Gordon
Jiang, Wen Guo
author_sort Rangaraj, Aravindan
collection PubMed
description Psoriasin, which is also known as S100A7, is a member of the S100 protein family, a group of calcium-responsive signalling proteins. Psoriasin expression remains high in patients with psoriasis, whereas it is downregulated in patients with invasive breast carcinoma. This observation suggests that this protein may be a notable marker of keratinocyte function and differentiation during wound healing. The aim of the present study was to determine the cellular impact of Psoriasin in keratinocytes, which are the primary cell type associated with wound healing. Psoriasin expression in wound tissues was examined using reverse transcription-quantitative polymerase chain reaction and immunochemical staining. Knockdown of Psoriasin in HaCaT cells was performed using anti-Psoriasin ribozyme transgenes and the effect on growth, adhesion and migration of keratinocytes was subsequently determined using in vitro cellular functional assays. Psoriasin expression is upregulated in wounds, particularly at the wound edges. The present study demonstrated that Psoriasin is expressed in keratinocytes and is a fundamental regulator of keratinocyte migration. Significant increases in the rate of keratinocyte adhesion, migration and growth were observed in Psoriasin-deficient cells (P<0.01 vs. control). Application of small inhibitors identified the potential association of neural Wiskott-Aldrich syndrome protein, focal adhesion primase and rho-associated protein kinase signalling pathways with Psoriasin-regulated cell adhesion and motility. In conclusion, Psoriasin serves an important role in the wound healing process, suggesting that it may be utilized as a potential wound healing biomarker.
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spelling pubmed-54432462017-05-30 Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds Rangaraj, Aravindan Ye, Lin Sanders, Andrew James Price, Patricia Elaine Harding, Keith Gordon Jiang, Wen Guo Exp Ther Med Articles Psoriasin, which is also known as S100A7, is a member of the S100 protein family, a group of calcium-responsive signalling proteins. Psoriasin expression remains high in patients with psoriasis, whereas it is downregulated in patients with invasive breast carcinoma. This observation suggests that this protein may be a notable marker of keratinocyte function and differentiation during wound healing. The aim of the present study was to determine the cellular impact of Psoriasin in keratinocytes, which are the primary cell type associated with wound healing. Psoriasin expression in wound tissues was examined using reverse transcription-quantitative polymerase chain reaction and immunochemical staining. Knockdown of Psoriasin in HaCaT cells was performed using anti-Psoriasin ribozyme transgenes and the effect on growth, adhesion and migration of keratinocytes was subsequently determined using in vitro cellular functional assays. Psoriasin expression is upregulated in wounds, particularly at the wound edges. The present study demonstrated that Psoriasin is expressed in keratinocytes and is a fundamental regulator of keratinocyte migration. Significant increases in the rate of keratinocyte adhesion, migration and growth were observed in Psoriasin-deficient cells (P<0.01 vs. control). Application of small inhibitors identified the potential association of neural Wiskott-Aldrich syndrome protein, focal adhesion primase and rho-associated protein kinase signalling pathways with Psoriasin-regulated cell adhesion and motility. In conclusion, Psoriasin serves an important role in the wound healing process, suggesting that it may be utilized as a potential wound healing biomarker. D.A. Spandidos 2017-05 2017-03-28 /pmc/articles/PMC5443246/ /pubmed/28565822 http://dx.doi.org/10.3892/etm.2017.4275 Text en Copyright: © Rangaraj et al. This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
spellingShingle Articles
Rangaraj, Aravindan
Ye, Lin
Sanders, Andrew James
Price, Patricia Elaine
Harding, Keith Gordon
Jiang, Wen Guo
Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds
title Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds
title_full Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds
title_fullStr Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds
title_full_unstemmed Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds
title_short Molecular and cellular impact of Psoriasin (S100A7) on the healing of human wounds
title_sort molecular and cellular impact of psoriasin (s100a7) on the healing of human wounds
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5443246/
https://www.ncbi.nlm.nih.gov/pubmed/28565822
http://dx.doi.org/10.3892/etm.2017.4275
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