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Skin aging by glycation: lessons from the reconstructed skin model.
Clin Chem Lab Med. 2014 Jan 01; 52(1):169-74.CC

Abstract

BACKGROUND

Aging is the result of several mechanisms which operate simultaneously. Among them, glycation is of particular interest because it is a reaction which affects slowly renewing tissues and macromolecules with elevated half-life, like the dermis, a skin compartment highly affected by aging. Glycation produces crosslinks between macromolecules thereby providing an explanation for the increased age-related stiffness of the skin. Glycation products, also called AGEs (advanced glycation end products), accumulate primarily in extracellular matrix molecules like collagen or elastin.

METHODS

In order to reproduce this phenomenon in vitro we have created a model of reconstructed skin modified by glycation of the collagen used to fabricate the dermal compartment.

RESULTS

This system allowed us to uncover biological modifications of dermal markers, and more surprisingly epidermal markers, as well as an increase of metalloproteinases responsible for degradation of the dermal matrix. Consequently, the imbalance between synthesis and degradation that results from glycation, may contribute to skin aging, as shown in this model. Moreover these modifications were shown to be prevented by the addition of aminoguanidine, a well-known inhibitor of glycation.

CONCLUSIONS

Using this experimental approach our results taken together stress the importance and possibly central role of glycation in skin aging and the usefulness of the reconstructed skin as a model of physiological aging.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

23770560

Citation

Pageon, Hervé, et al. "Skin Aging By Glycation: Lessons From the Reconstructed Skin Model." Clinical Chemistry and Laboratory Medicine, vol. 52, no. 1, 2014, pp. 169-74.
Pageon H, Zucchi H, Rousset F, et al. Skin aging by glycation: lessons from the reconstructed skin model. Clin Chem Lab Med. 2014;52(1):169-74.
Pageon, H., Zucchi, H., Rousset, F., Monnier, V. M., & Asselineau, D. (2014). Skin aging by glycation: lessons from the reconstructed skin model. Clinical Chemistry and Laboratory Medicine, 52(1), 169-74. https://doi.org/10.1515/cclm-2013-0091
Pageon H, et al. Skin Aging By Glycation: Lessons From the Reconstructed Skin Model. Clin Chem Lab Med. 2014 Jan 1;52(1):169-74. PubMed PMID: 23770560.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Skin aging by glycation: lessons from the reconstructed skin model. AU - Pageon,Hervé, AU - Zucchi,Hélène, AU - Rousset,Françoise, AU - Monnier,Vincent M, AU - Asselineau,Daniel, PY - 2013/02/04/received PY - 2013/05/24/accepted PY - 2013/6/18/entrez PY - 2013/6/19/pubmed PY - 2014/8/1/medline SP - 169 EP - 74 JF - Clinical chemistry and laboratory medicine JO - Clin. Chem. Lab. Med. VL - 52 IS - 1 N2 - BACKGROUND: Aging is the result of several mechanisms which operate simultaneously. Among them, glycation is of particular interest because it is a reaction which affects slowly renewing tissues and macromolecules with elevated half-life, like the dermis, a skin compartment highly affected by aging. Glycation produces crosslinks between macromolecules thereby providing an explanation for the increased age-related stiffness of the skin. Glycation products, also called AGEs (advanced glycation end products), accumulate primarily in extracellular matrix molecules like collagen or elastin. METHODS: In order to reproduce this phenomenon in vitro we have created a model of reconstructed skin modified by glycation of the collagen used to fabricate the dermal compartment. RESULTS: This system allowed us to uncover biological modifications of dermal markers, and more surprisingly epidermal markers, as well as an increase of metalloproteinases responsible for degradation of the dermal matrix. Consequently, the imbalance between synthesis and degradation that results from glycation, may contribute to skin aging, as shown in this model. Moreover these modifications were shown to be prevented by the addition of aminoguanidine, a well-known inhibitor of glycation. CONCLUSIONS: Using this experimental approach our results taken together stress the importance and possibly central role of glycation in skin aging and the usefulness of the reconstructed skin as a model of physiological aging. SN - 1437-4331 UR - https://www.unboundmedicine.com/medline/citation/23770560/Skin_aging_by_glycation:_lessons_from_the_reconstructed_skin_model_ L2 - https://www.degruyter.com/doi/10.1515/cclm-2013-0091 DB - PRIME DP - Unbound Medicine ER -