Results from in vitro and ex vivo skin aging models assessing the antiglycation and anti-elastase MMP-12 potential of glycylglycine oleamide
| Autor: | Isabelle Ceruti, Sandrine Bessou-Touya, Nathalie Castex-Rizzi, Marie-José Haure, Patrick Bogdanowicz |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Oleamide extracellular matrix Dermatology Matrix metalloproteinase matrix metalloproteinase-12 Skin Aging 030207 dermatology & venereal diseases 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Glycation Medicine fibrillin-1 skin aging Original Research biology integumentary system business.industry glycylglycine oleamide In vitro 030104 developmental biology Clinical Cosmetic and Investigational Dermatology Biochemistry chemistry biology.protein glycation business Elastin Type I collagen Ex vivo |
| Zdroj: | Clinical, Cosmetic and Investigational Dermatology |
| ISSN: | 1178-7015 |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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