Effects of human collagen α-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts
Su Jin Hwang, Su Hwan Kim, Woo‐Young Seo, Yelin Jeong, Min Cheol Shin, Dongryeol Ryu, Sang Bae Lee, Young Jin Choi, KyeongJin Kim
Abstract
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].