Age-related changes in the proteoglycans of human skin.

Skin undergoes dramatic age-related changes in its mechanical properties, including changes in tissue hydration and resiliency. Proteoglycans are macromolecular conjugates of protein and carbohydrate (glycosaminoglycan) which are involved in these tissue properties. In order to examine whether age-related changes in skin proteoglycans may contribute to the age-related changes in the mechanical properties of skin, proteoglycans from human skin of various ages were extracted and analyzed. Samples were obtained from two different fetal ages, from mature skin, and from senescent skin. As a function of age, there is a decrease in the proportion of large chondroitin sulfate proteoglycans (versican) and a concomitant increase in the proportion of small dermatan sulfate proteoglycans (decorin). Based on reactivity with antibodies to various chondroitin sulfate epitopes, fetal versican differs from the versican found in older skin with respect to the chondroitin sulfate chains. Also, the decorin of fetal skin is slightly larger, while the decorin of older skin shows greater polydispersity in both its size and its charge to mass ratio. There are also age-related differences in the size and polydispersity of the core proteins of decorin. The most pronounced change in skin proteoglycans is the appearance in mature skin of a proteoglycan which is smaller than decorin, but which has the same amino terminal amino acid sequence as decorin. This small proteoglycan is abundant in mature skin and may be a catabolic fragment of decorin or an alternatively spliced form of decorin. In light of the known ability of decorin to influence collagen fibrillogenesis and fibril diameter, the appearance of this small decorin-related proteoglycan may have a significant effect on skin elasticity. The observation that proteoglycans in skin show dramatic age-related differences suggests that these changes may be involved in the age-related changes in the physical properties of skin. Copyright 2000 Academic Press.