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http://dx.doi.org/10.5483/BMBRep.2021.54.6.038

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

Hwang, Su Jin (ABIOTECH Co., Ltd.)
Kim, Su Hwan (Department of Agricultural Biotechnology, Seoul National University)
Seo, Woo-Young (ABIOTECH Co., Ltd.)
Jeong, Yelin (Department of Biomedical Sciences, College of Medicine, Inha University)
Shin, Min Cheol (Department of Biomedical Sciences, College of Medicine, Inha University)
Ryu, Dongryeol (Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine)
Lee, Sang Bae (Division of Life Sciences, Jeonbuk National University)
Choi, Young Jin (Department of Agricultural Biotechnology, Seoul National University)
Kim, KyeongJin (Department of Biomedical Sciences, College of Medicine, Inha University)
Publication Information
BMB Reports / v.54, no.6, 2021 , pp. 329-334 More about this Journal
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.
Keywords
Collagen synthesis; Elastin; hCOL1A1; Human dermal fibroblasts;
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