Related Experiment Video
Updated: May 5, 2026

Evaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen Substrates
Published on: April 22, 2019
Lithospermum erythrorhizon and Forsythia suspensa Prevent Collagen Degradation and Maintain Skin Hydration by
Xiangji Jin1, Qiwen Zheng2, Trang Thi Minh Nguyen2
1Department of Dermatology, School of Medicine, Graduate School, Kyung Hee University, 26 Kyungheedae-ro, Dong-daemun, Seoul 02447, Republic of Korea.
Abstract:
The growing demand for aesthetic enhancement has driven the development of anti-aging cosmetics, with natural compound-based formulations emerging as a new trend to enhance efficacy. This study aims to develop a 30% ethanol extract of a 1:1 mixture of Lithospermum erythrorhizon and Forsythia suspensa (LF) as a potential material for combating UVB-induced skin aging. The bioactive components of LF extract were identified via HPLC. Antioxidant efficacy (DPPH, ABTS, and SOD) and the inhibitory effects on ROS production in cells were evaluated using flow cytometry. MMPs' expressions were analyzed via RT-PCR, while TGF-β/Smad, ERK/AP-1, and HAS2/HYAL1 pathways were examined via ELISA and Western blot. Research findings indicate that LF effectively scavenges reactive oxygen species and enhances the activation of TGF-β signaling, promoting the synthesis of PIP (Procollagen Type I C-Peptide). Collagen degradation was mitigated through the inhibition of the AP-1 pathway, which regulates the expression of MMPs, and by suppressing the expression of TIMP. Additionally, modulation of the HAS2/HYAL1 signaling axis ensures a balanced regulation of hyaluronic acid (HA) synthesis and degradation, thereby contributing to the maintenance of collagen integrity and skin hydration. In conclusion, LF has exhibited significant protective effects against demonstrated anti-aging properties, highlighting its potential as a novel therapeutic agent in cosmetic formulations targeting aging.
Related Concept Videos
Fibril-associated Collagen
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Matrix Proteoglycans and Glycoproteins
Role of Matrix Metalloproteases in Degradation of ECM
Renewal of Skin Epidermal Stem Cells
Tissue Renewal without Stem Cells
However, failure of such a system...
Extracellular Matrix

