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KMID : 0624620210540060329
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BMB Reports
2021 Volume.54 No. 6 p.329 ~ p.334
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Effects of human collagen α-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts
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Hwang Su-Jin
Kim Su-Hwan
Seo Woo-Young
Jeong Ye-Lin
Shin Min-Cheol
Ryu Dong-Ryeol
Lee Sang-Bae
Choi Young-Jin
Kim Kyeong-Jin
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Abstract
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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.
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KEYWORD
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Collagen synthesis, Elastin, hCOL1A1, Human dermal fibroblasts
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