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How to help the skin cope with glycoxidation

  • Louis Danoux EMAIL logo , Solène Mine , Nabil Abdul-Malak , Florence Henry , Christine Jeanmaire , Olga Freis , Gilles Pauly , Lysiane Cittadini , Valérie André-Frei and Andreas Rathjens
Published/Copyright: April 2, 2013

Abstract

Background: Protein glycation refers to the spontaneous reaction of reducing sugars with proteins and the subsequent formation of stable advanced glycation end products (AGEs). Glycation is linked with oxidative stress, and this association is called “glycoxidation”. Glycoxidation alters the protein structure and function and causes tissue aging, as seen in human skin. Therefore, research on substances inhibiting glycoxidation appears to be crucial in the prevention of skin aging. With this aim, several plant extracts have been screened for antiglycation activity, and the results of the best candidates are presented in this article.

Methods: Glycation was studied on human skin proteins (collagen, elastin, and albumin) and on a model of reconstructed skin. Oxidative stress has been addressed by testing the copper-induced low-density lipoprotein oxidation, ultraviolet irradiation of glycated dermis, and carbonyl activation of human dermal fibroblasts. A clinical test evaluated the extent of oxidative stress induced by ultraviolet A irradiation.

Results: Among the tested products, several plant extracts have decreased the glycation effects on skin proteins collagen, elastin, and albumin. In addition, a plant extract has significantly inhibited the different forms of oxidative stress associated with protein glycation.

Conclusions: We have demonstrated that plant extracts can relieve the deleterious effects of glycation on human skin. Moreover, a plant extract rich in antioxidant molecules has also significantly preserved the human skin from glycoxidation attacks.


Corresponding author: Louis Danoux, BASF Beauty Care Solutions France SAS, 3 rue de Seichamps, CS71040 Pulnoy, 54272 Essey les Nancy Cedex, France, E-mail:

The excellent assistance of Natacha Benoit in the preparation of plant extracts; Lydie Martin-Teixeira, Lucile Deposito, and Emmanuel Charrois in biochemistry and cell culture assays; Corinne Naudin and Carine Tedeschi in immunohistochemistry assays; Nadine Duc-Sikora and Catherine Bonnaud-Rosaye in clinical assay; and Aurélie Courtois in the publication management are acknowledged.

Conflict of interest statement

Authors’ conflict of interest disclosure: The authors stated that there are no conflicts of interest regarding the publication of this article.

Research funding: None declared.

Employment or leadership: None declared.

Honorarium: None declared.

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Received: 2012-11-30
Accepted: 2013-3-7
Published Online: 2013-04-02
Published in Print: 2014-01-01

©2014 by Walter de Gruyter Berlin Boston

Articles in the same Issue

  1. Masthead
  2. Masthead
  3. Editorial
  4. Frontiers in research on the Maillard reaction in aging and chronic disease
  5. Reviews
  6. Role of the Maillard reaction in aging and age-related diseases. Studies at the cellular-molecular level
  7. Advanced glycation end-products and skin autofluorescence in end-stage renal disease: a review
  8. Glucosepane: a poorly understood advanced glycation end product of growing importance for diabetes and its complications
  9. Mini Reviews
  10. Post-translational modification derived products (PTMDPs): toxins in chronic diseases?
  11. Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes
  12. Augmentation of blood lipid glycation and lipid oxidation in diabetic patients
  13. Maillard reaction products: some considerations on their health effects
  14. The Maillard reaction and food allergies: is there a link?
  15. Perspectives
  16. Chelation therapy for the management of diabetic complications: a hypothesis and a proposal for clinical laboratory assessment of metal ion homeostasis in plasma
  17. Genetics and Molecular Diagnostics
  18. Genetic variability in enzymes of metabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality
  19. General Clinical Chemistry and Laboratory Medicine
  20. Quantification of glyoxal, methylglyoxal and 3-deoxyglucosone in blood and plasma by ultra performance liquid chromatography tandem mass spectrometry: evaluation of blood specimen
  21. A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes
  22. Increased circulating advanced glycation endproducts (AGEs) in acute trauma patients
  23. Circulating soluble RAGE increase after a cerebrovascular event
  24. Pentosidine determination in CSF: a potential biomarker of Alzheimer’s disease?
  25. Cardiovascular Diseases
  26. Skin autofluorescence as proxy of tissue AGE accumulation is dissociated from SCORE cardiovascular risk score, and remains so after 3 years
  27. Plasma advanced glycation end products (AGEs) and NF-κB activity are independent determinants of diastolic and pulse pressure
  28. Total plasma Nε-(carboxymethyl)lysine and sRAGE levels are inversely associated with a number of metabolic syndrome risk factors in non-diabetic young-to-middle-aged medication-free subjects
  29. Translational Research Papers
  30. Advanced glycation end-products induce endoplasmic reticulum stress in human aortic endothelial cells
  31. Formation of nitri- and nitrosylhemoglobin in systems modeling the Maillard reaction
  32. Skin aging by glycation: lessons from the reconstructed skin model
  33. How to help the skin cope with glycoxidation
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