Effects of human collagen α-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts

• Published in: BMB reports Vol. 54; no. 6; pp. 329 - 334
• Main Authors: Hwang, Su Jin, Kim, Su Hwan, Seo, Woo-Young, Jeong, Yelin, Shin, Min Cheol, Ryu, Dongryeol, Lee, Sang Bae, Choi, Young Jin, Kim, KyeongJin
• Format: Journal Article
• Language: Korean
• Published: 생화학분자생물학회 30.06.2021
• Subjects: Collagen synthesis; Elastin; hCOL1A1; Human dermal fibroblasts; hCOL1A1; Collagen synthesis; Human dermal fibroblasts; Elastin
• ISSN: 1976-6696; 1976-670X

Collagen type I is the most abundant form of collagen in human tissues, and is composed of two identical α-1 type I chains and an α-2 type I chain organized in a triple helical structure. A previous study has shown that human collagen α-2 type I (hCOL1A2) promotes collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs). However, the biological effects of human collagen α-1 type I (hCOL1A1) on various skin properties have not been investigated. Here, we isolate and identify the hCOL1A1-collagen effective domain (CED) which promotes collagen type I synthesis. Recombinant hCOL1A1-CED effectively induces cell proliferation and collagen biosynthesis in HDFs, as well as increased cell migration and elastin production. Based on these results, hCOL1A1-CED may be explored further for its potential use as a preventative agent against skin aging. [BMB Reports 2021; 54(6): 329-334]