Collagen peptides promote photoaging skin cell repair by activating the TGF-β/Smad pathway and depressing collagen degradation

光老化 羟脯氨酸 化学 SMAD公司 前胶原肽酶 生物化学 抗氧化剂 透明质酸 细胞生物学 转化生长因子 皮肤老化 药理学 伤口愈合 信号转导 分子生物学 生物 免疫学 医学 皮肤病科 遗传学
作者
Zehua Liu,Yang Yang,Hongdong Song,Juan He,Li Ge,Yayao Zheng,Бо Лі
出处
期刊:Food & Function [The Royal Society of Chemistry]
卷期号:10 (9): 6121-6134 被引量:56
标识
DOI:10.1039/c9fo00610a
摘要

Collagen hydrolysate has been widely used as a nutraceutical agent against skin aging and has gained increasing attention. Previous research has suggested that oral administration of antioxidant collagen peptides (ACPs) exerted beneficial effects on the photoaging skin structure and collagen. However, the bioactive components in ACP metabolites that are responsible for the repair effects have not been elucidated. In this study, serum containing collagen peptides (CPS) after oral administration and collagen peptides isolated from serum metabolites (SCP) were collected and their effects on cell proliferation, hyaluronic acid secretion and the collagen synthesis pathway in UVA-induced skin fibroblasts (ESF) were evaluated. Furthermore, hydroxyproline (Hyp)-containing collagen peptides from SCP were analyzed and their repair effects were examined. The repair effects of ACP metabolites in serum differed depending on the preparation method and SCP were the active components responsible for the repair effects. SCP displayed repair effects by activating the TGF-β/Smad pathway to promote procollagen synthesis and suppressing AP-1, MMP-1 and MMP-3 protein expression to prevent collagen degradation, in which SHCP exhibited the strongest bioactivity. In addition, SCP showed repair effects by reactive oxygen species (ROS) scavenging activity and preserving the endogenous antioxidant defense systems. Furthermore, IO (Ile-Hyp) and AOG (Ala-Hyp-Gly) were identified as the active peptides promoting procollagen synthesis by activating the TGF-β/Smad3 pathway. These results may be useful in screening of anti-photoaging factors in metabolites and producing highly efficient collagen peptide products.
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