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Glycation of extracellular matrix (ECM) collagen and proteins plays an important role in the aging process This is not to be confused with glycosylation of collagen, which is an enzyme-mediated process in the intracellular step of collagen biosynthesis Glycation is a nonenzymatic series of biologic events that involves adding a reducing sugar molecule (such as glucose or fructose) to ECM collagen and proteins This reaction is also known as the Maillard reaction The sugar molecule mainly reacts with the amino group side chains
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Basement membrane Blood vessel Dermis
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FIGURE 2-1 Histopathology of the dermal-epidermal junction The basement membrane separates the epidermis and the dermis (Image courtesy of George Loannides, MD)
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Amino group of protein + Sugar N-substituted glycosylamine + water
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Advanced Glycation End Products (AGEs)
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FIGURE 2-3 Glycation of proteins is thought to play a role in the aging process of lysine and arginine of collagen and ECM proteins Subsequently, the product of this process undergoes oxidative reactions resulting in the formation of advanced glycation end products (AGEs) (Fig 2-3) AGEs have been implicated in the aging process and agerelated diseases such as diabetes mellitus,1 3 chronic renal failure,4,5 and Alzheimer s disease 6 8 It is believed that with time, AGEs increase,9 accumulate on human collagen10 and elastin fibers,11 and contribute to aging of the skin As a result of glycation, collagen networks lose their ability to contract, and they become stiffer and resistant to remodeling Fibroblasts are key elements for collagen contracture, as they apply contracture force on the collagen lattice via their actin cytoskeleton12 Glycated collagen modifies the actin cytoskeleton of the fibroblasts thereby diminishing their collagen contraction capacity13 Fibroblasts also secrete collagenase (MMP-1), which is essential for collagen turnover Glycated collagen has been proven to decrease levels of collagenase I (MMP-1), leading to less tissue remodeling14 Studies have shown that UV exposure may also contribute to the production and function of AGEs N e -(carboxymethyl) lysine TABLE 2-1 Major Collagen Types Found in the Dermis COLLAGEN TYPE I III IV V VII XVII OTHER NAME Fetal collagen LOCATION Bone, tendon, skin Dermis, GI, vessels Basement membranes Dermis, diffusely distributed Anchoring brils Hemidesmosome FUNCTION Gives tensile strength Gives compliance Forms a lattice Unknown Stabilizes DEJ (CML) is one of the AGEs in which the amino side chain of lysine is reduced This product was shown to accumulate on elastin tissue of photoaged skin and proven to be higher in sun-exposed skin as compared to sun-protected skin11 In addition, it has been proposed that AGE-modified proteins act as endogenous photosensitizers in human skin via oxidative stress mechanisms induced by UVA light15
The Key Types of Collagen Found in the Dermis (Table 2-1)
Type I collagen comprises 80% to 85% of the dermal matrix and is responsible for the tensile strength of the dermis The amount of collagen I has been shown to be lower in photoaged skin, and to be increased after dermabrasion procedures16 Therefore, it is likely that collagen I is the most important collagen type in regard to skin aging Type III is the second most important form of collagen in the dermis, making up anywhere from 10% to 15% of the matrix17 This collagen type has a smaller diameter than type I and forms smaller bundles allowing for skin pliability Type III, also known as fetal collagen because it predominates in
embryonic life, is seen in higher amounts around the blood vessels and beneath the epidermis The other types of collagen that are noteworthy for a cosmetic dermatologist are type IV collagen, which forms a structure lattice that is found in the basement membrane zone and type V collagen, which is diffusely distributed throughout the dermis and comprises roughly 4% to 5% of the matrix Type VII collagen makes up the anchoring fibrils in the DEJ Type XVII collagen is located in the hemidesmosome and plays an important structural role as well The importance of these collagens and other structural proteins is evident in genetic diseases characterized by a lack of these structures and in acquired diseases characterized by antibody formation to these important structures For example, patients with an inherited blistering disease known as dominant dystrophic epidermolysis have been shown to have a scarcity of type VII collagen with resulting abnormalities in their anchoring fibrils An acquired bullous disease, epidermolysis bullosa acquisita (EBA), is caused by antibodies to this same collagen type VII Although the discussion of these diseases is beyond the scope of this text, it is interesting that patients with chronic sun exposure have also been found to have alterations in collagen type VII This may contribute to the skin fragility seen in elderly patients Some investigators have postulated that a weakened bond between the dermis and epidermis caused by loss of the anchoring fibrils (collagen VII) may lead to wrinkle formation18 The importance of collagen and changes seen in aged skin will be discussed further in 6
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