BMB Reports

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

DOI QR Code

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

  • Hwang, Su Jin (ABIOTECH Co., Ltd.) ;
  • Kim, Su Hwan (Department of Agricultural Biotechnology, Seoul National University) ;
  • Seo, Woo-Young (ABIOTECH Co., Ltd.) ;
  • Jeong, Yelin (Department of Biomedical Sciences, College of Medicine, Inha University) ;
  • Shin, Min Cheol (Department of Biomedical Sciences, College of Medicine, Inha University) ;
  • Ryu, Dongryeol (Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine) ;
  • Lee, Sang Bae (Division of Life Sciences, Jeonbuk National University) ;
  • Choi, Young Jin (Department of Agricultural Biotechnology, Seoul National University) ;
  • Kim, KyeongJin (Department of Biomedical Sciences, College of Medicine, Inha University)
  • Received : 2021.03.09
  • Accepted : 2021.04.26
  • Published : 2021.06.30
Download PDF
⟨ Previous Next ⟩

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.

Keywords

Acknowledgement

This work was supported by an INHA UNIVERSITY Research Grant to K.K., research funds for newly appointed professors of Jeonbuk National University to S.B.L., and National Research Foundation of Korea (NRF) grants funded by the Korean government (MSIT) to K.K. (2020R1C1C1004015) and S.B.L. (2020R1C1C1014281).

References

  1. 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
  2. Mancini M, Lena AM, Saintigny G et al (2014) MicroRNAs in human skin ageing. Ageing Res Rev 17, 9-15 https://doi.org/10.1016/j.arr.2014.04.003
  3. 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
  4. Rendon MI and Gaviria JI (2005) Review of skin-lightening agents. Dermatol Surg 31, 886-889; discussion 889 https://doi.org/10.1111/j.1524-4725.2005.31736
  5. 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
  6. 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
  7. 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
  8. 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 https://doi.org/10.1038/s41598-018-28492-w
  9. Krutmann J (2011) [Skin aging/anti-aging strategies]. Hautarzt 62, 576 https://doi.org/10.1007/s00105-011-2131-z
  10. Gelse K, Poschl E and Aigner T (2003) Collagens - structure, function, and biosynthesis. Advanced Drug Delivery Reviews 55, 1531-1546 https://doi.org/10.1016/j.addr.2003.08.002
  11. 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
  12. Singer AJ and Clark RA (1999) Cutaneous wound healing. N Engl J Med 341, 738-746 https://doi.org/10.1056/NEJM199909023411006
  13. Imanishi J, Kamiyama K, Iguchi I, Kita M, Sotozono C and Kinoshita S (2000) Growth factors: importance in wound healing and maintenance of transparency of the cornea. Prog Retin Eye Res 19, 113-129 https://doi.org/10.1016/S1350-9462(99)00007-5
  14. Park JS, Kim JY, Cho JY, Kang JS and Yu YH (2000) Epidermal growth factor (EGF) antagonizes transforming growth factor (TGF)-beta1-induced collagen lattice contraction by human skin fibroblasts. Biol Pharm Bull 23, 1517-1520 https://doi.org/10.1248/bpb.23.1517
  15. Van Cauter E and Plat L (1996) Physiology of growth hormone secretion during sleep. J Pediatr 128, S32-37 https://doi.org/10.1016/S0022-3476(96)70008-2
  16. Bartke A (2008) Growth hormone and aging: a challenging controversy. Clin Interv Aging 3, 659-665 https://doi.org/10.2147/CIA.S3697
  17. Sonntag WE, Csiszar A, deCabo R, Ferrucci L and Ungvari Z (2012) Diverse roles of growth hormone and insulin-like growth factor-1 in mammalian aging: progress and controversies. J Gerontol A Biol Sci Med Sci 67, 587-598
  18. 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
  19. Trojanowska M, LeRoy EC, Eckes B and Krieg T (1998) Pathogenesis of fibrosis: type 1 collagen and the skin. J Mol Med (Berl) 76, 266-274 https://doi.org/10.1007/s001090050216
  20. Chiquet M, Matthisson M, Koch M, Tannheimer M and Chiquet-Ehrismann R (1996) Regulation of extracellular matrix synthesis by mechanical stress. Biochem Cell Biol 74, 737-744 https://doi.org/10.1139/o96-080
  21. Majora M, Wittkampf T, Schuermann B et al (2009) Functional consequences of mitochondrial DNA deletions in human skin fibroblasts: increased contractile strength in collagen lattices is due to oxidative stress-induced lysyl oxidase activity. Am J Pathol 175, 1019-1029 https://doi.org/10.2353/ajpath.2009.080832
  22. 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 https://doi.org/10.1038/s41598-017-16290-9
  23. Andl CD, Mizushima T, Nakagawa H et al (2003) Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal Keratinocytes in vitro and in vivo. J Biol Chem 278, 1824-1830 https://doi.org/10.1074/jbc.M209148200
  24. 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
  25. Hu Z, Yang P, Zhou CX, Li SD and Hong PZ (2017) Marine collagen peptides from the skin of nile tilapia (oreochromis niloticus): characterization and wound healing evaluation. Mar Drugs 15, 102 https://doi.org/10.3390/md15040102
  26. Walter MNM, Wright KT, Fuller HR, MacNeil S and Johnson WE (2010) Mesenchymal stem cell-conditioned medium accelerates skin wound healing: an in vitro study of fibroblast and keratinocyte scratch assays. Exp Cell Res 316, 1271-1281 https://doi.org/10.1016/j.yexcr.2010.02.026
  27. Quan T, Shao Y, He T, Voorhees JJ and Fisher GJ (2010) Reduced expression of connective tissue growth factor (CTGF/CCN2) mediates collagen loss in chronologically aged human skin. J Invest Dermatol 130, 415-424 https://doi.org/10.1038/jid.2009.224
  28. Seite S, Zucchi H, Septier D, Igondjo-Tchen S, Senni K and Godeau G (2006) Elastin changes during chronological and photo-ageing: the important role of lysozyme. J Eur Acad Dermatol Venereol 20, 980-987 https://doi.org/10.1111/j.1468-3083.2006.01706.x
  29. Erat MC, Slatter DA, Lowe ED et al (2009) Identification and structural analysis of type I collagen sites in complex with fibronectin fragments. Proc Natl Aca Sci U S A 106, 4195-4200 https://doi.org/10.1073/pnas.0812516106
  30. Freitas-Rodriguez S, Folgueras AR and Lopez-Otin C (2017) The role of matrix metalloproteinases in aging: Tissue remodeling and beyond. Biochim Biophys Acta Mole Cell Res 1864, 2015-2025 https://doi.org/10.1016/j.bbamcr.2017.05.007