How to help the skin cope with glycoxidation
-
Louis Danoux
, Solène Mine
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.
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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©2014 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Masthead
- Masthead
- Editorial
- Frontiers in research on the Maillard reaction in aging and chronic disease
- Reviews
- Role of the Maillard reaction in aging and age-related diseases. Studies at the cellular-molecular level
- Advanced glycation end-products and skin autofluorescence in end-stage renal disease: a review
- Glucosepane: a poorly understood advanced glycation end product of growing importance for diabetes and its complications
- Mini Reviews
- Post-translational modification derived products (PTMDPs): toxins in chronic diseases?
- Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes
- Augmentation of blood lipid glycation and lipid oxidation in diabetic patients
- Maillard reaction products: some considerations on their health effects
- The Maillard reaction and food allergies: is there a link?
- Perspectives
- Chelation therapy for the management of diabetic complications: a hypothesis and a proposal for clinical laboratory assessment of metal ion homeostasis in plasma
- Genetics and Molecular Diagnostics
- Genetic variability in enzymes of metabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality
- General Clinical Chemistry and Laboratory Medicine
- Quantification of glyoxal, methylglyoxal and 3-deoxyglucosone in blood and plasma by ultra performance liquid chromatography tandem mass spectrometry: evaluation of blood specimen
- A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes
- Increased circulating advanced glycation endproducts (AGEs) in acute trauma patients
- Circulating soluble RAGE increase after a cerebrovascular event
- Pentosidine determination in CSF: a potential biomarker of Alzheimer’s disease?
- Cardiovascular Diseases
- Skin autofluorescence as proxy of tissue AGE accumulation is dissociated from SCORE cardiovascular risk score, and remains so after 3 years
- Plasma advanced glycation end products (AGEs) and NF-κB activity are independent determinants of diastolic and pulse pressure
- 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
- Translational Research Papers
- Advanced glycation end-products induce endoplasmic reticulum stress in human aortic endothelial cells
- Formation of nitri- and nitrosylhemoglobin in systems modeling the Maillard reaction
- Skin aging by glycation: lessons from the reconstructed skin model
- How to help the skin cope with glycoxidation
Articles in the same Issue
- Masthead
- Masthead
- Editorial
- Frontiers in research on the Maillard reaction in aging and chronic disease
- Reviews
- Role of the Maillard reaction in aging and age-related diseases. Studies at the cellular-molecular level
- Advanced glycation end-products and skin autofluorescence in end-stage renal disease: a review
- Glucosepane: a poorly understood advanced glycation end product of growing importance for diabetes and its complications
- Mini Reviews
- Post-translational modification derived products (PTMDPs): toxins in chronic diseases?
- Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes
- Augmentation of blood lipid glycation and lipid oxidation in diabetic patients
- Maillard reaction products: some considerations on their health effects
- The Maillard reaction and food allergies: is there a link?
- Perspectives
- Chelation therapy for the management of diabetic complications: a hypothesis and a proposal for clinical laboratory assessment of metal ion homeostasis in plasma
- Genetics and Molecular Diagnostics
- Genetic variability in enzymes of metabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality
- General Clinical Chemistry and Laboratory Medicine
- Quantification of glyoxal, methylglyoxal and 3-deoxyglucosone in blood and plasma by ultra performance liquid chromatography tandem mass spectrometry: evaluation of blood specimen
- A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes
- Increased circulating advanced glycation endproducts (AGEs) in acute trauma patients
- Circulating soluble RAGE increase after a cerebrovascular event
- Pentosidine determination in CSF: a potential biomarker of Alzheimer’s disease?
- Cardiovascular Diseases
- Skin autofluorescence as proxy of tissue AGE accumulation is dissociated from SCORE cardiovascular risk score, and remains so after 3 years
- Plasma advanced glycation end products (AGEs) and NF-κB activity are independent determinants of diastolic and pulse pressure
- 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
- Translational Research Papers
- Advanced glycation end-products induce endoplasmic reticulum stress in human aortic endothelial cells
- Formation of nitri- and nitrosylhemoglobin in systems modeling the Maillard reaction
- Skin aging by glycation: lessons from the reconstructed skin model
- How to help the skin cope with glycoxidation