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Causing Collagen and Elastin fibers to lose their ability to function normally, Glycation is now well recognised and heavily implicated in accelerated skin aging.1-3 Advanced Glycation End Products (A.G.Es) are the end result of a glucose-driven process known as Glycation. Glycation occurs when excess bodily glucose molecules link to the skin’s Collagen and Elastin fibers.6-8 This cross-linking can form chemical bridges between these proteins9. Glycated fibers can become rigid, less elastic and have reduced regenerative ability, which can lead to damage such as laxity, cracking and thinning skin.4-9
In young skin, the Dermal Epidermal Junction has the appearance of a mountain range that helps anchor the Epidermis to the Dermis, forming a network of supportive Collagen fibers.  
As skin ages, fibers in the Dermal Epidermal Junction responsible for the appearance and texture of skin, glycate.5-9  
The genes that make up your A.G.E.x™ score play a key role in skin Glycation. They are responsible for controlling serum glucose levels, energy intake and energy release. Having variations in these genes can alter the functioning of normal glucose levels and energy metabolism. While glucose is a vital cellular fuel, if not completely metabolised by the body Glycation can occur, leading way to wrinkling, dryness and laxity.
Did you know? 1 in 2 people are predisposed to reduced genetic protection against Glycation.
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SkinDNA™ Gene Name/ Descriptor |
Genotype |
Description |
s400976/ Glycation Interruption
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AA
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Responsible for controlling serum glucose levels, energy intake and release. While glucose is a vital cellular fuel, if not fully metabolised Glycation can occur.
Chromosome Location: 1q31
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Collagen: Collagen is the principle structural protein that holds the skin together.10 Collagen is just one of thousands of different proteins in the body. Most proteins occur only in small amounts. But by far the most abundant protein is collagen. In fact, collagen makes up more than one third of all protein in the body and about 75% of the skin.11
Elastin: Elastin is a protein found in connective tissue that is elastic. In the skin, Elastin helps keep flexibility by providing a bounce-back reaction if skin is pulled or pinched. Enough elastin in the skin means that the skin will return to its normal shape after a pull or a pinch. It also helps keep skin smooth as it stretches to accommodate normal activities like flexing a muscle or opening and closing the mouth to talk or eat.
Glucose: Glucose is the body’s prime source of fuel for generating energy. It is a type of sugar that comes from digesting carbohydrates into a chemical that we can easily convert to energy. But glucose has its dark side. If not properly metabolised Glucose can bind tightly to proteins and form abnormal chemical bridges that progressively damage tissue elasticity. This process is referred to as Glycation.
Glycation: Glycation occurs when excess bodily glucose molecules link to the skin’s Collagen and Elastin fibers. This cross-linking can form chemical bridges between these proteins. Glycated fibers can become rigid, less elastic and have reduced regenerative ability, which can lead to damage such as laxity, cracking and thinning skin.
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1. Carmia Borek, P. (2001). "AGE Breakers." Life Extension: 6.
2. Verzijl. N., et al.,(2000). "Age-related accumulation of Maillard reaction products in human articular cartilage collagen." Biochemical Journal 350: 381–387.
3. Dunn. J., et al.,(1991). "Age-dependent accumulation of N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)hydroxylysine in human skin collagen." Biochemistry 30(5): 1205-10.
4. Bank. R., et al., (1998). "Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage. The age-related increase in non-enzymatic glycation affects biomechanical properties of cartilage. ." The Biochemical Journal 330: 345-51.
5. Asselineau. D., et al., (2008). "Reconstructed skin modified by glycation of the dermal equivalent as a model for skin aging and its potential use to evaluate anti-glycation molecules." Experimental Gerontology 43(6): 584-8.
6. Pageon. H (2005). "An in vitro approach to the chronological aging of skin by glycation of the collagen: the biological effect of glycation on the reconstructed skin model." Annals of the New York Academy of Sciences 1043: 529-32.
7. Pageon. H., et al., (2007). "Collagen glycation triggers the formation of aged skin in vitro." European Journal of Dermatology 17(1): 12-20.
8. Pageon. H (2009). "Reaction of glycation and human skin: The effects on the skin and its components, reconstructed skin as a model." Pathologie -biologie (paris).
9. Avery. N., et al., (2006). "The effects of the Maillard reaction on the physical properties and cell interactions of collagen." Pathologie -biologie (paris) 54(7): 387-95.
10. Varani. J., et al., (2006). "Decreased Collagen Production in Chronologically Aged Skin" American Journal of Pathology 168: 1861-1868.
11. Available at: http://www.biospecifics.com/collagendefined.html. Accessed October 22, 2008.
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