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High Mobility Group Box Protein-1 in Wound Repair

High-mobility group box 1 protein (HMGB1), a member of highly conserved non-histone DNA binding protein family, has been studied as transcription factor and growth factor. Secreted extracellularly by activated monocytes and macrophages or passively released by necrotic or damaged cells, extracellula...

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Detalles Bibliográficos
Autores principales: Ranzato, Elia, Martinotti, Simona, Pedrazzi, Marco, Patrone, Mauro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901153/
https://www.ncbi.nlm.nih.gov/pubmed/24710526
http://dx.doi.org/10.3390/cells1040699
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author Ranzato, Elia
Martinotti, Simona
Pedrazzi, Marco
Patrone, Mauro
author_facet Ranzato, Elia
Martinotti, Simona
Pedrazzi, Marco
Patrone, Mauro
author_sort Ranzato, Elia
collection PubMed
description High-mobility group box 1 protein (HMGB1), a member of highly conserved non-histone DNA binding protein family, has been studied as transcription factor and growth factor. Secreted extracellularly by activated monocytes and macrophages or passively released by necrotic or damaged cells, extracellular HMGB1 is a potent mediator of inflammation. Extracellular HMGB1 has apparently contrasting biological actions: it sustains inflammation (with the possible establishment of autoimmunity or of self-maintaining tissue damage), but it also activates and recruits stem cells, boosting tissue repair. Here, we focus on the role of HMGB1 in physiological and pathological responses, the mechanisms by which it contributes to tissue repair and therapeutic strategies base on targeting HMGB1.
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spelling pubmed-39011532014-04-07 High Mobility Group Box Protein-1 in Wound Repair Ranzato, Elia Martinotti, Simona Pedrazzi, Marco Patrone, Mauro Cells Review High-mobility group box 1 protein (HMGB1), a member of highly conserved non-histone DNA binding protein family, has been studied as transcription factor and growth factor. Secreted extracellularly by activated monocytes and macrophages or passively released by necrotic or damaged cells, extracellular HMGB1 is a potent mediator of inflammation. Extracellular HMGB1 has apparently contrasting biological actions: it sustains inflammation (with the possible establishment of autoimmunity or of self-maintaining tissue damage), but it also activates and recruits stem cells, boosting tissue repair. Here, we focus on the role of HMGB1 in physiological and pathological responses, the mechanisms by which it contributes to tissue repair and therapeutic strategies base on targeting HMGB1. MDPI 2012-09-28 /pmc/articles/PMC3901153/ /pubmed/24710526 http://dx.doi.org/10.3390/cells1040699 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Ranzato, Elia
Martinotti, Simona
Pedrazzi, Marco
Patrone, Mauro
High Mobility Group Box Protein-1 in Wound Repair
title High Mobility Group Box Protein-1 in Wound Repair
title_full High Mobility Group Box Protein-1 in Wound Repair
title_fullStr High Mobility Group Box Protein-1 in Wound Repair
title_full_unstemmed High Mobility Group Box Protein-1 in Wound Repair
title_short High Mobility Group Box Protein-1 in Wound Repair
title_sort high mobility group box protein-1 in wound repair
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901153/
https://www.ncbi.nlm.nih.gov/pubmed/24710526
http://dx.doi.org/10.3390/cells1040699
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