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

BMB Rep. 2021 Jun;54(6):329-334. doi: 10.5483/BMBRep.2021.54.6.038.

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].

MeSH terms

  • Cell Movement
  • Cell Proliferation
  • Cells, Cultured
  • Collagen / metabolism*
  • Collagen Type I, alpha 1 Chain / genetics
  • Collagen Type I, alpha 1 Chain / metabolism*
  • Elastin / metabolism*
  • Fibroblasts / cytology
  • Fibroblasts / metabolism*
  • Humans
  • Skin / cytology
  • Skin / metabolism*
  • Wound Healing

Substances

  • COL1A1 protein, human
  • Collagen Type I, alpha 1 Chain
  • Collagen
  • Elastin