Human collagen alpha-2 type I stimulates collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs)

Abstract

Skin aging appears to be the result of overlapping intrinsic (including genetic and hormonal factors) and extrinsic (external environment including chronic light exposure, chemicals, and toxins) processes. These factors cause decreases in the synthesis of collagen type I and elastin in fibroblasts and increases in the melanin in melanocytes. Collagen Type I is the most abundant type of collagen and is a major structural protein in human body tissues. In previous studies, many products containing collagen derived from land and marine animals as well as other sources have been used for a wide range of purposes in cosmetics and food. However, to our knowledge, the effects of human collagen-derived peptides on improvements in skin condition have not been investigated. Here we isolate and identify the domain of a human COL1A2-derived protein which promotes fibroblast cell proliferation and collagen type I synthesis. This human COL 1A2-derived peptide enhances wound healing and elastin production. Finally, the human collagen alpha-2 type I-derived peptide (SMM) ameliorates collagen type I synthesis, cell proliferation, cell migration, and elastin synthesis, supporting a significant anti-wrinkle effect. Collectively, these results demonstrate that human collagen alpha-2 type I-derived peptides is practically accessible in both cosmetics and food, with the goal of improving skin condition.

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

“…Previous studies have suggested that collagen type I synthesis and fibroblast cell proliferation are required to maintain the strength and elasticity of the skin ( 19 - 21 ). We have previously reported that hCOL1A2-derived proteins promote collagen type I synthesis, elastin production, and fibroblast cell proliferation in normal HDFs ( 18 ). To investigate the biological function of hCOL1A1—another major component of human collagen type I, in human skin fibroblasts—we examined the effects of hCOL1A1 domains on collagen type I synthesis in normal HDFs, similar to our previous study ( 18 ).…”

“…We have previously reported that hCOL1A2-derived proteins promote collagen type I synthesis, elastin production, and fibroblast cell proliferation in normal HDFs ( 18 ). To investigate the biological function of hCOL1A1—another major component of human collagen type I, in human skin fibroblasts—we examined the effects of hCOL1A1 domains on collagen type I synthesis in normal HDFs, similar to our previous study ( 18 ). Full-length hCOL1A1 and various deletion mutants were generated ( Fig.…”

“…We compared the effects of hCOL1A1-CED and EGF on HDF cell proliferation, as these have previously been reported to promote cell proliferation ( 8 , 18 , 23 ). As shown in Fig.…”

“…Our previous study has shown that human collagen alpha-2 type I (hCOL1A2) promotes collagen synthesis, elastin production, and wound healing in normal dermal fibroblasts ( 18 ). Our analysis has identified that the hCOL1A2-derived peptide promotes the improvement of skin properties compared with the effects of marine collagen.…”

Cosmetic Potential of a Recombinant 50 kDa Protein

“…Unexpectedly, this 50 kDa human collagen protein alone was able to enhance both collagen I and III production in fibroblasts comparable to or even better than the TGFβ1 positive control [48]. A specific motif in collagen type I alpha 2 chain has been found to induce collagen I synthesis in human dermal fibroblasts, but no such motif has been reported for collagen type III induction [49].…”