Abstract

Hyaluronic acid (HA) is a high-molecular-weight polysaccharide with high moisturizing power. It is composed of repeating disaccharides of N-acetyl-D-glucosamine and D-glucuronic acid. Low-molecular-weight hyaluronan (LMHA) is obtained by changing the molecular weight or modifying the functional groups of HA and is commonly used together with HA in cosmetics. The objective of this study was to determine whether LMHA promotes the synthesis of filaggrin (FLG). We also investigated whether LMHA activates FLG-degrading enzymes. Three-dimensional (3D) models of the human epidermis were cultured with LMHA. Real-time PCR was used to quantify the mRNA levels of profilaggrin (proFLG), involucrin (IVL), and FLG-degrading enzymes. FLG protein levels were measured by fluorescent antibody staining and Western blotting. The mRNA was quantified using a 3D epidermis model, and it was observed that the mRNA levels of proFLG, IVL, caspase-14 (CASP14), and bleomycin hydrolase were increased by the application of LMHA. Immunofluorescence results showed an increase in FLG proteins, and results from experiments using 3D epidermis models showed that LMHA increased the activity of CASP14. This suggests that the topical application of LMHA would result in an increase in natural moisturizing factor and promote moisturization of the stratum corneum.

Highlights

  • The skin has an important barrier function that prevents stimulation from the outside world and moisture evaporation from inside the body

  • Was quantified using a 3D epidermis model, and it was observed that the mRNA levels of proFLG, IVL, caspase-14 (CASP14), and bleomycin hydrolase were increased by the application of Low-molecular-weight hyaluronan (LMHA)

  • There was no significant difference in the amount of loricrin protein, which is expressed very late in epidermal differentiation, and TGM1 protein between the models applied with all concentrations of Hyaluronic acid (HA) or LMHA and those applied with solvent

Read more

Summary

Introduction

The skin has an important barrier function that prevents stimulation from the outside world and moisture evaporation from inside the body. The main factors that maintain this barrier function are the cornified cell envelope (CE) of stratum corneum cells, natural moisturizing factor (NMF) produced by the breakdown of proteins such as filaggrin (FLG), and intercellular lipids of the stratum corneum. The main component of the CE of stratum corneum cells is a protein called involucrin (IVL). NMF is known to be essential for skin moisturization, and amino acids and their derivatives are the main components of NMF. FLG is a protein involved in differentiation that aggregates keratin fibers and the skeletal protein of the stratum corneum and strengthens the internal structure of the stratum corneum [1]. ProFLG, which consists of 10 to 12 FLG units, is stored in the stratum granulosum and, upon keratinization, it is excised by kallikrein-5 (KLK5) and other proteins to become individual FLGs [2]

Objectives
Methods
Findings
Discussion
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call