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Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide
BACKGROUND: Glycation is an aging reaction of naturally occurring sugars with dermal proteins. Type I collagen and elastin are most affected by glycation during intrinsic chronological aging. AIM: To study the in vitro and ex vivo assays in human skin cells and explants and the antiaging effects of...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Dove Medical Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4922745/ https://www.ncbi.nlm.nih.gov/pubmed/27382322 http://dx.doi.org/10.2147/CCID.S98633 |
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author | Bogdanowicz, Patrick Haure, Marie-José Ceruti, Isabelle Bessou-Touya, Sandrine Castex-Rizzi, Nathalie |
author_facet | Bogdanowicz, Patrick Haure, Marie-José Ceruti, Isabelle Bessou-Touya, Sandrine Castex-Rizzi, Nathalie |
author_sort | Bogdanowicz, Patrick |
collection | PubMed |
description | BACKGROUND: Glycation is an aging reaction of naturally occurring sugars with dermal proteins. Type I collagen and elastin are most affected by glycation during intrinsic chronological aging. AIM: To study the in vitro and ex vivo assays in human skin cells and explants and the antiaging effects of glycylglycine oleamide (GGO). MATERIALS AND METHODS: The antiglycation effect of GGO was assessed in a noncellular in vitro study on collagen and, ex vivo, by immunohistochemical staining on human skin explants (elastin network glycation). The ability of GGO to contract fibroblasts was assessed in a functional assay, and its anti-elastase (MMP-12) activity was compared to that of oleic acid alone, glycylglycine (GG) alone, and oleic acid associated with GG. RESULTS: In vitro, GGO reduced the glycation of type I collagen. Ex vivo, GGO restored the expression of fibrillin-1 inhibited by glycation. Furthermore, GGO induced a tissue retraction of almost 30%. Moreover, the MMP-12 activity was inhibited by up to 60%. CONCLUSION: Under the present in vitro and ex vivo conditions, GGO prevents glycation of the major structural proteins of the dermis, helping to reduce the risk of rigidification. By maintaining the elastic function of the skin, GGO may be a promising sparring partner for other topical antiaging agents. |
format | Online Article Text |
id | pubmed-4922745 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Dove Medical Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-49227452016-07-05 Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide Bogdanowicz, Patrick Haure, Marie-José Ceruti, Isabelle Bessou-Touya, Sandrine Castex-Rizzi, Nathalie Clin Cosmet Investig Dermatol Original Research BACKGROUND: Glycation is an aging reaction of naturally occurring sugars with dermal proteins. Type I collagen and elastin are most affected by glycation during intrinsic chronological aging. AIM: To study the in vitro and ex vivo assays in human skin cells and explants and the antiaging effects of glycylglycine oleamide (GGO). MATERIALS AND METHODS: The antiglycation effect of GGO was assessed in a noncellular in vitro study on collagen and, ex vivo, by immunohistochemical staining on human skin explants (elastin network glycation). The ability of GGO to contract fibroblasts was assessed in a functional assay, and its anti-elastase (MMP-12) activity was compared to that of oleic acid alone, glycylglycine (GG) alone, and oleic acid associated with GG. RESULTS: In vitro, GGO reduced the glycation of type I collagen. Ex vivo, GGO restored the expression of fibrillin-1 inhibited by glycation. Furthermore, GGO induced a tissue retraction of almost 30%. Moreover, the MMP-12 activity was inhibited by up to 60%. CONCLUSION: Under the present in vitro and ex vivo conditions, GGO prevents glycation of the major structural proteins of the dermis, helping to reduce the risk of rigidification. By maintaining the elastic function of the skin, GGO may be a promising sparring partner for other topical antiaging agents. Dove Medical Press 2016-06-22 /pmc/articles/PMC4922745/ /pubmed/27382322 http://dx.doi.org/10.2147/CCID.S98633 Text en © 2016 Bogdanowicz et al. This work is published and licensed by Dove Medical Press Limited The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. |
spellingShingle | Original Research Bogdanowicz, Patrick Haure, Marie-José Ceruti, Isabelle Bessou-Touya, Sandrine Castex-Rizzi, Nathalie Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide |
title | Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide |
title_full | Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide |
title_fullStr | Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide |
title_full_unstemmed | Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide |
title_short | Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide |
title_sort | results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase mmp-12 potential of glycylglycine oleamide |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4922745/ https://www.ncbi.nlm.nih.gov/pubmed/27382322 http://dx.doi.org/10.2147/CCID.S98633 |
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