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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

Authors Bogdanowicz P, Haure M, Ceruti I, Bessou-Touya S, Castex-Rizzi N

Received 19 October 2015

Accepted for publication 10 March 2016

Published 22 June 2016 Volume 2016:9 Pages 143—150


Checked for plagiarism Yes

Review by Single anonymous peer review

Peer reviewer comments 3

Editor who approved publication: Dr Jeffrey Weinberg

Patrick Bogdanowicz, Marie-José Haure, Isabelle Ceruti, Sandrine Bessou-Touya, Nathalie Castex-Rizzi

Department of Pharmacology, Pierre Fabre Dermo-Cosmétique, Toulouse, France

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.

Keywords: extracellular matrix, glycylglycine oleamide, glycation, fibrillin-1, matrix metalloproteinase-12, skin aging

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