Skin glycation is a non-enzymatic chemical reaction in which excess sugar molecules, primarily glucose, bind irreversibly to structural proteins in the dermis, specifically collagen and elastin, forming Advanced Glycation End-products (AGEs). This process is a key biochemical driver of extrinsic and intrinsic skin aging, leading to a loss of elasticity, increased stiffness, and the formation of wrinkles. It is closely linked to metabolic health and insulin resistance, highlighting the connection between internal hormonal balance and external appearance.
Origin
The term combines skin, the integumentary organ, and glycation, the process of sugar binding to proteins, derived from the Greek glykys meaning sweet. The phenomenon was first described in the context of food chemistry by Louis-Camille Maillard in the early 20th century, and its role in human aging and disease was later elucidated in the latter half of the century. This discovery provided a molecular link between diet and aging.
Mechanism
The mechanism, known as the Maillard reaction, begins with the initial binding of a sugar molecule to a free amino group on a protein, forming a reversible Schiff base. This is followed by a rearrangement to form a more stable Amadori product, which then undergoes further complex reactions to form irreversible, cross-linking AGEs. These AGEs stiffen the collagen matrix, impairing its function and stimulating inflammatory pathways in the skin, which is often exacerbated by poor glucose control and systemic hormonal imbalance.
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