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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Development of a highly effective recombinant protein from human collagen type III Alpha 1 (COL3A1) to enhance human skin cell functionality

  • Young Un Kim (Department of Biomedical Sciences, College of Medicine, Inha University) ;
  • HyunJoon Gi (Department of Biomedical Sciences, College of Medicine, Inha University) ;
  • Eun Kyung Jeong (Department of Food Regulatory Science, Korea University) ;
  • Seokwon Han (ABIOTECH Co., Ltd.) ;
  • Woo-Young Seo (ABIOTECH Co., Ltd.) ;
  • Young Jun Kim (Department of Food Regulatory Science, Korea University) ;
  • Sang Bae Lee (Department of Life Sciences, Jeonbuk National University) ;
  • KyeongJin Kim (Department of Biomedical Sciences, College of Medicine, Inha University)
  • Received : 2024.07.09
  • Accepted : 2024.07.29
  • Published : 2024.09.30
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Abstract

Collagen type III, a member of the fibrillar collagen group, is a major component of the extracellular matrix in various internal organs, the vascular systems, and skin. It is essential to maintain the structural integrity and functionality of these tissues, and plays a significant role in wound healing, often found alongside collagen type I. Despite being the second most abundant collagen in human tissues after type I, its biological functions on various skin properties have not been thoroughly studied. In this study, we have isolated and developed an effective recombinant protein derived from human collagen type III alpha 1 chain (hCOL3A1). Our findings demonstrate that the recombinant proteins hCOL3A1-THR-M1 and M4 stimulate cell proliferation and collagen biosynthesis in human dermal fibroblasts (HDFs), and enhance wound healing. Notably, hCOL3A1-THR-M1 (referred to as HUCOLLATIN3) specifically penetrates both the epidermal and dermal layers in a full-thickness skin model. These results collectively indicate that hCOL3A1-THR-M1 holds promise as a potential biomaterial to prevent skin aging.

Keywords

Acknowledgement

This work was supported by an INHA UNIVERSITY Research Grant to K.K.

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