Abstract
Ultraviolet (UV) light-induced wrinkle formation is a major dermatological problem and is associated with alteration in collagen. Here, we investigated the potential of α-ionone, a naturally occurring aromatic compound, in regulation of UVB-induced photoaging in human Hs68 dermal fibroblasts and identified the mechanisms involved. We found that in human dermal fibroblasts, α-ionone inhibited UVB-induced loss of collagen. α-Ionone upregulated the molecules participating in the TGF-β–SMAD pathway (TGF-β1, phospho-SMAD2/3, Col1A1, and Col1A2), but downregulated the molecules involved in the MAPK–AP-1 signaling pathway (phospho-p38, phospho-JNK, phospho-ERK, phospho-c-Fos, phospho-c-Jun, MMP1, MMP3, and MMP9), in human dermal fibroblasts. α-Ionone treatment also increased hyaluronic acid contents, and this effect was accompanied by an upregulation of mRNA expression of genes (HAS1 and HAS2) involved in hyaluronic acid synthesis. Thus, α-ionone is effective in the prevention of UVB-induced decrease of collagen and hyaluronic acid in human dermal fibroblasts. We propose that α-ionone may prove beneficial for the prevention of UV-induced wrinkle formation and skin damage.
Highlights
Collagen represents a superfamily of extracellular structural proteins with various physiological roles, such as the promotion of cell migration, cell growth and differentiation, and tissue development [1].In the dermis, collagen is by far the most abundant extracellular matrix (ECM) protein and constitutes the bulk of skin (90% of dry weight) [2]
Procollagen is synthesized by dermal fibroblasts and secreted into the extracellular space, where it is enzymatically processed into collagen
We found that treatment with α-ionone, an aroma compound found in herbs, fruits, roasted almonds, carrots, and raspberries [14,15], led to a robust increase in procollagen content of human dermal fibroblasts. α-Ionone is approved for use as a flavoring agent by the FDA in accordance with 21 CFR 172.515 and is granted the Generally Recognized as Safe status (GRAS) by the Flavor and Extract Manufacturers Association [14]
Summary
Collagen is by far the most abundant extracellular matrix (ECM) protein and constitutes the bulk of skin (90% of dry weight) [2]. Procollagen is synthesized by dermal fibroblasts and secreted into the extracellular space, where it is enzymatically processed into collagen. Alterations in collagen are thought to be responsible for wrinkle formation in aged skin [4]. Both intrinsic (e.g., ethnicity and anatomical variations) and extrinsic factors (e.g., UV radiation, smoking, diet, chemicals, and trauma) cause alterations in dermal collagen via two primary pathways: (1) inhibition of procollagen biosynthesis, leading to a decrease of collagen, and (2) promotion of collagen breakdown, leading to disorganized, fragmented collagen [3,5]. It is believed that in aged skin restoration of the collagen deficiency by the stimulation of new collagen biosynthesis and by a reduction in collagen degradation may be a strategy for preventing and treating the clinical manifestations of wrinkles [6]
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