BMB Reports

생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
권호 표지
DOI QR코드

DOI QR Code

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)
  • 투고 : 2024.07.09
  • 심사 : 2024.07.29
  • 발행 : 2024.09.30
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

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.

키워드

과제정보

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

참고문헌

  1. Prockop DJ and Kivirikko KI (1995) Collagens: molecular biology, diseases, and potentials for therapy. Annu Rev Biochem 64, 403-434  https://doi.org/10.1146/annurev.bi.64.070195.002155
  2. Haukipuro K, Risteli L, Kairaluoma MI and Risteli J (1987) Aminoterminal propeptide of type III procollagen in healing wound in humans. Ann Surg 206, 752-756  https://doi.org/10.1097/00000658-198712000-00011
  3. Liu X, Wu H, Byrne M, Krane S and Jaenisch R (1997) Type III collagen is crucial for collagen I fibrillogenesis and for normal cardiovascular development. Proc Natl Acad Sci U S A 94, 1852-1856  https://doi.org/10.1073/pnas.94.5.1852
  4. Smith LT, Schwarze U, Goldstein J and Byers PH (1997) Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis. J Invest Dermatol 108, 241-247  https://doi.org/10.1111/1523-1747.ep12286441
  5. Frank M, Albuisson J, Ranque B et al (2015) The type of variants at the gene associates with the phenotype and severity of vascular Ehlers-Danlos syndrome. Eur J Hum Genet 23, 1657-1664  https://doi.org/10.1038/ejhg.2015.32
  6. El-Domyati M, Attia S, Saleh F et al (2002) Intrinsic aging vs. photoaging: a comparative histopathological, immunohistochemical, and ultrastructural study of skin. Exp Dermatol 11, 398-405  https://doi.org/10.1034/j.1600-0625.2002.110502.x
  7. Petit L and Pierard GE (2003) Skin-lightening products revisited. Int J Cosmet Sci 25, 169-181  https://doi.org/10.1046/j.1467-2494.2003.00182.x
  8. Rendon MI and Gaviria JI (2005) Review of skin-lightening agents. Dermatol Surg 31, 886-889  https://doi.org/10.1111/j.1524-4725.2005.31736
  9. Ganceviciene R, Liakou AI, Theodoridis A, Makrantonaki E and Zouboulis CC (2012) Skin anti-aging strategies. Dermatoendocrinol 4, 308-319  https://doi.org/10.4161/derm.22804
  10. Kim WS, Park BS, Park SH, Kim HK and Sung JH (2009) Antiwrinkle effect of adipose-derived stem cell: activation of dermal fibroblast by secretory factors. J Dermatol Sci 53, 96-102  https://doi.org/10.1016/j.jdermsci.2008.08.007
  11. Edgar S, Hopley B, Genovese L, Sibilla S, Laight D and Shute J (2018) Effects of collagen-derived bioactive peptides and natural antioxidant compounds on proliferation and matrix protein synthesis by cultured normal human dermal fibroblasts. Sci Rep 8, 10474 
  12. Kim J, Kang S, Kwon H, Moon H and Park MC (2019) Dual functional bioactive-peptide, AIMP1-derived peptide (AdP), for anti-aging. J Cosmet Dermatol 18, 251-257  https://doi.org/10.1111/jocd.12671
  13. van Zuijlen PP, Ruurda JJ, van Veen HA et al (2003) Collagen morphology in human skin and scar tissue: no adaptations in response to mechanical loading at joints. Burns 29, 423-431  https://doi.org/10.1016/S0305-4179(03)00052-4
  14. Oikarinen A (1994) Aging of the skin connective-tissue - how to measure the biochemical and mechanical-properties of aging dermis. Photodermatol Photoimmunol Photomed 10, 47-52 
  15. Gelse K, Poschl E and Aigner T (2003) Collagens--structure, function, and biosynthesis. Adv Drug Deliv Rev 55, 1531-1546  https://doi.org/10.1016/j.addr.2003.08.002
  16. Hwang SJ, Ha GH, Seo WY, Kim CK, Kim K and Lee SB (2020) Human collagen alpha-2 type I stimulates collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs). BMB Rep 53, 539-544  https://doi.org/10.5483/BMBRep.2020.53.10.120
  17. Hwang SJ, Kim SH, Seo WY et al (2021) Effects of human collagen alpha-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts. BMB Rep 54, 329-334  https://doi.org/10.5483/BMBRep.2021.54.6.038
  18. Kuivaniemi H and Tromp G (2019) Type III collagen (COL3A1): gene and protein structure, tissue distribution, and associated diseases. Gene 707, 151-171  https://doi.org/10.1016/j.gene.2019.05.003
  19. Singh D, Rai V and Agrawal DK (2023) Regulation of collagen I and collagen III in tissue injury and regeneration. Cardiol Cardiovasc Med 7, 5-16 
  20. Shoulders MD and Raines RT (2009) Collagen structure and stability. Annu Rev Biochem 78, 929-958  https://doi.org/10.1146/annurev.biochem.77.032207.120833
  21. Kuznetsova N and Leikin S (1999) Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? Effect of proteolytic cleavage on fibrillogenesis and on collagen-collagen interaction in fibers. J Biol Chem 274, 36083-36088  https://doi.org/10.1074/jbc.274.51.36083
  22. Chen CZ, Peng YX, Wang ZB et al (2009) The Scar-in-a-Jar: studying potential antifibrotic compounds from the epigenetic to extracellular level in a single well. Br J Pharmacol 158, 1196-1209  https://doi.org/10.1111/j.1476-5381.2009.00387.x
  23. Seo WY, Kim JH, Baek DS et al (2017) Production of recombinant human procollagen type I C-terminal propeptide and establishment of a sandwich ELISA for quantification. Sci Rep 7, 15946 
  24. Martinotti S and Ranzato E (2020) Scratch wound healing assay. Methods Mol Biol 2109, 225-229 https://doi.org/10.1007/7651_2019_259