Fermented Fish Collagen Diminished Photoaging-Related Collagen Decrease by Attenuating AGE-RAGE Binding Activity.

Abstract

Ultraviolet (UV) irradiation causes skin wrinkles and decreases elasticity. UV also increases binding between advanced glycation end products (AGEs) and the receptor for AGEs (RAGE), resulting in increased inflammation and activation of NF-κB. We evaluated whether fermented fish collagen (FC) could decrease photoaging via decreasing AGE-RAGE binding activity, which was associated with decreased TNF-α and NF-κB levels in UV-irradiated keratinocytes and animal skin. In the UV-irradiated keratinocytes, AGE-RAGE binding activity and TNF-α secretion levels were increased, and FC decreased these. Additionally, AGE-RAGE binding activity and TNF-α secretion levels were attenuated by soluble RAGE (RAGE inhibitor) in the UV-irradiated keratinocytes. FC decreased AGE-RAGE binding activity, TNF-α levels, and translocation of NF-κB in the UV-irradiated skin. Furthermore, FC decreased the expression of matrix metalloproteinases 1/3/9, which degrades collagen fibers, and Smad7, which inhibits Smad2/3, in UV-irradiated skin. FC increased Smad2/3 and collagen fiber accumulation. FC also increases skin moisture and elasticity. In conclusion, FC could attenuate skin photoaging via decreasing AGE-RAGE binding activity and its downstream signals such as TNF-α and NF-κB.