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Effect of Ascorbic Acid, Silicon, Fe, Proline and Lysine on Proliferation and Collagen Synthesis in the Human Dermal Fibroblast Cell (HS27)

비타민 C, Silicon, 철분, Proline 및 Lysine의 처리가 피부 섬유아세포의 증식 및 Collagen I과 III의 발현에 미치는 효과 비교

  • Kim, Sun-Ah (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University) ;
  • Lee, Jin-Ah (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University) ;
  • Kim, Jung-Min (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University) ;
  • Kim, Hyun-Ae (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University) ;
  • Kim, Young-Ae (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University) ;
  • Yun, Hye-Jeong (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University) ;
  • Cho, Yun-Hi (Dept. of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University)
  • 김선아 (경희대학교 동서의학대학원 의학영양학과) ;
  • 이진아 (경희대학교 동서의학대학원 의학영양학과) ;
  • 김정민 (경희대학교 동서의학대학원 의학영양학과) ;
  • 김현애 (경희대학교 동서의학대학원 의학영양학과) ;
  • 김영애 (경희대학교 동서의학대학원 의학영양학과) ;
  • 윤혜정 (경희대학교 동서의학대학원 의학영양학과) ;
  • 조윤희 (경희대학교 동서의학대학원 의학영양학과)
  • Published : 2009.11.30

Abstract

In the dermis, fibroblast plays an important role in the turnover of the dermal extracellular matrix. Collagen I and III, which are the most important dermal proteins of the extracellular matrix, function as a stabilizing scaffold of dermal connective tissues, as well as a regulator of differentiation and migration of dermal cells. In this study, we investigated the effect of various nutrients, such as ascorbic acid, silicon, Fe, lysine and proline which function as cofactors or building blocks on collagen synthesis. When the physiological concentrations of ascorbic acid (0-100 ${\mu}M$), silicon (0-50 ${\mu}M$), Fe (0-50 ${\mu}M$), lysine (0-150 ${\mu}M$) and proline (0-300 ${\mu}M$) were treated at HS27 for either 3 or 5 days, 5 day treatment of ascorbic acid at the low concentration (5-10 ${\mu}M$) increased the expression of collagen I and III protein by 115-1300% without increasing cell proliferation. 3 or 5 days treatment of Fe increased the expression of collagen I and III proteins up to 323% in parallel with cell proliferation by 164%. However, cell proliferation and expression of collagen I and III protein in silicon treated HS27 did not differ. Proline and lysine only increased cell proliferation up to 247.9%. Taken together, we demonstrate that the physiological concentrations of ascorbic acid and Fe enhance the expression of collagen I and III protein for treatment of 3 or 5 days.

본 연구에서는 HS27 피부 섬유아세포에 비타민 C, silicon, 철분, proline 및 lysine을 혈청 및 피부 내 농도 범위로 처리한 후 세포의 증식을 비롯하여 콜라겐 I과 III의 mRNA 및 단백질의 발현을 비교하였다. 비타민 C는 처리 기간 및 농도와 무관하게 세포 증식 및 mRNA 발현에 영향을 미치지 않았으며 콜라겐 type I 및 III의 단백질 발현은 각각 5-50 ${\mu}M$, 10-50 ${\mu}M$ 농도에서 5일 처리 시 683.9%, 182% 이상으로 발현을 증가시켰다. Silicon의 3일 및 5일 농도별 처리는 세포증식과 콜라겐 mRNA 및 단백질 발현을 다소 감소시키거나 영향을 미치지 않았다. 철분의 3일 및 5일 처리는 혈청 내 농도(11-35 ${\mu}M$)에서 콜라겐 mRNA 발현에 영향을 미치지 않았으며 세포 증식 및 콜라겐 단백질 발현을 증가시켰다. 또한 철분의 5-30 ${\mu}M$의 농도 처리는 5일 처리보다 3일 처리 시 발현수준이 훨씬 컸다. 콜라겐의 구성 아미노산인 proline 및 lysine은 섬유아세포의 증식을 증가시켰다. 따라서 단기간의 콜라겐의 합성 증가는 철분의 섭취가 적합하나 장기간의 섭취에는 비타민 C의 섭취와 더불어 철분의 섭취가 필요한 것으로 여겨진다.

Keywords

References

  1. Ishikawa T, Ishikawa O, Miyachi Y. 1995. Measurement of skin elastic properties with a new suction device (Ⅰ): Relationship to age, sex and the degree of obesity in normal individuals. J Dermatol 22: 713-717 https://doi.org/10.1111/j.1346-8138.1995.tb03907.x
  2. Elsner P, Wilhelm D, Maibach H.I. 1990. Mechanical properties of human forearm and vulvar skin. Br J Dermatol 122: 607-614 https://doi.org/10.1111/j.1365-2133.1990.tb07282.x
  3. Jemec G.B, Jemec B, Jemec B.I, Serup J. 1990. The effect of superficial hydration on the mechanical properties of human skin in vivo: implications for plastic surgery. Plast Reconstr Surg 85: 100-103 https://doi.org/10.1097/00006534-199001000-00017
  4. Uitto J, Olsen D.R, Fazio M.J. 1989. Extracellular matrix of the skin: 50 years process. J Invest Dermatol 92: 61s-77s https://doi.org/10.1111/1523-1747.ep13075039
  5. Nimni M.E, Harkness R.D. 1993. Molecular structure and functions of collagen. In Collagen. Nimni ME, ed. CRC Press, Florida. p 1-3
  6. Kim N.M, Koo B.S, Lee S.K, Hwang E.I, So S.H, Do J.H. 2007. Effect of Korean red ginseng on collagen biosynthesis and MMP-1 activity in human dermal fibroblast. J Ginseng Res 31: 86-92 https://doi.org/10.5142/JGR.2007.31.2.086
  7. Bauer E.A, Uitto J. 1982. Skin, collagen in health and disease. JB Weiss, MlV Jayson, eds. Churchill Livingston, Edinburgh, UK. p 474-487
  8. Pinnel S.R, Murad S, Darr D. 1987. Induction of collagen synthesis by ascorbic acid. A possible mechanism. Arch Dermatol 123: 1684-1686 https://doi.org/10.1001/archderm.123.12.1684
  9. Tinker D, Rucker R.B. 1985. Accumulation and chemical modification of connective tissue proteins. Physiol Rev 65: 607-657 https://doi.org/10.1152/physrev.1985.65.3.607
  10. Berg R.A, Kerr J.S. 1992. Nutritional aspects of collagen metabolism. Annu Rev Nutr 12: 369-390 https://doi.org/10.1146/annurev.nu.12.070192.002101
  11. Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko K.I. 1998. Cloning and characterization of a third human lysyl hydroxylase isoform. Proc Natl Acad Sci USA 95: 10482-10486 https://doi.org/10.1073/pnas.95.18.10482
  12. Seaborn CD, Nielsen FH. 2002. Silicon deprivation decreases collagen formation in wounds and bone, and ornithine transaminase enzyme activity in liver. Biol Trace Elem Res 89: 251-261 https://doi.org/10.1385/BTER:89:3:251
  13. Groff J.L, Gropper S.S. 1999. Advanced nutrition and human metabolism. 3rd ed. Peter Marshall Publisher, Wadsworth/ Thomson Learing, Belmont, USA. p 251
  14. Tajima S, Pinnell S.R. 1996. Ascorbic acid preferentially enhances type Ⅰ and Ⅲ collagen gene transcription in human skin fibroblasts. J Derm Sci 11: 250-253 https://doi.org/10.1016/0923-1811(95)00640-0
  15. Walingo K.M. 2005. Role of vitmin C (ascorbic acid) on human health-A review. African J Food Agric Nutr Develop (AJFAND) 5: 1-13
  16. Murad S, Grove D, Lindberg KA, Reynolds G, Sivarajah A, Pinnell S.R. 1981. Regulation of collagen synthesis by ascorbic acid. Proc Natl Acd Sci USA 78: 2879-2882 https://doi.org/10.1073/pnas.78.5.2879
  17. Reffitt D.M, Ogston N, Jugdaohsingh R, Cheung H.F, Evans B.A, Thompson R.P, Powell J.J, Hampson G.N. 2003. Orthosilicic acid stimulates collagen type Ⅰ synthesis and osteoblastic differentiation in human osteoblast-like cells in vitro. Bone 32: 127-135 https://doi.org/10.1016/S8756-3282(02)00950-X
  18. Che P, Xu J, Shi H, Ma Y. 1995. Quantitative determination of serum iron in human blood by high performance capillary electrophoresis. J Chromato B 669: 45-51 https://doi.org/10.1016/0378-4347(95)00041-G
  19. Dionisi Vici C, De Felice L, E.l Hachem M, Bottero S, Rizzo C, Paoloni A, Goffredo B, Sabetta G, Caniglia M. 1998. Intravenous immune globulin in lysinuric protein intolerance. J Inherit Metab Dis 21: 95-102 https://doi.org/10.1023/A:1005383307100
  20. Kang S.A, Jang K.H, Cho Y.H, Hong K.H, Kong S.H, Choue R.W. 2001. High performance liquid chromatographic analysis of isoflavones in soybean and blackbean. J Arache 8: 44-48
  21. Bernard M.P, Myers J.C, Chu M.L, Ramirez F, Eikenberry E.F, Prockop D.J. 1983. Structure of a cDNA for the pro alpha 2 chain of human type Ⅰ procollagen. Comparison with chick cDNA for pro alpha 2 (I) identifies structurally conserved features of the protein and the gene. Biochemistry 22: 1139-1145 https://doi.org/10.1021/bi00274a023
  22. Ala-Kokko L, Kontusaari S, Baldwin C.T, Kuivaniemi H, Prockop D.J. 1989. Structure of cDNA clones coding for the entire prepro alpha 1 (Ⅲ) chain of human type Ⅲ procollagen. Differences in protein structure from type Ⅰ procollagen and conservation of codon preferences. Biochem J 260: 509-516
  23. Shibayama H, Hisama M, Matsuda S, Ohtsuki M, Iwaki M. 2008. Effect of a novel ascorbic derivative, disodium isostearyl 2-O-L-ascorbyl phosphate on human dermal fibroblasts: increased collagen synthesis and inhibition of MMP-1. Biol Pharm Bull 31: 563-568 https://doi.org/10.1248/bpb.31.563
  24. Duarte T.L, Cooke M.S, Jones G.D. 2009. Gene expression profiling reveals new protective roles for vitamin C in human skin cells. Free Radic Biol Med 46: 78-87 https://doi.org/10.1016/j.freeradbiomed.2008.09.028
  25. Etienne-Manneville S, Hall A. 2001. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell 106: 489-498 https://doi.org/10.1016/S0092-8674(01)00471-8
  26. Carlisle E.M. 1981. Silicon: a requirement in bone formation independent of vitamin D1. Calcif Tissue Int 33: 27-34 https://doi.org/10.1007/BF02409409
  27. Ruiz I.G, de la Torre P, Diaz T, Esteban E, Morillas J.D, Munoz-Yague T, Solis-Herruzo J.A. 2000. Sp family of transcription factors is involved in iron-induced collagen alpha1 (I) gene expression. DNA Cell Biol 19: 167-178 https://doi.org/10.1089/104454900314555
  28. Gardi C, Arezzini B, Fortino V, Comporti M. 2002. Effect of free iron on collagen synthesis, cell proliferation and MMP-2 expression in rat hepatic stellate cells. Biochem Pharmacol 64: 1139-1145 https://doi.org/10.1016/S0006-2952(02)01257-1

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