경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

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One of the first modifications to take place is the very critical step of hydroxylation of selected proline and lysine amino acids in the newly synthesized procollagen protein (Figure 2). Specific enzymes called hydroxylases are responsible for these important reactions needed to form hydroxyproline and hydroxylysine. The hydroxylase enzymes require Vitamin C and Iron as cofactors.(Mussini E, Hutton JJ, Udenfriend S. 1967) If a patient is Vitamin C deficient, then this reaction will not occur. In the absence of hydroxyproline, the collagen chains cannot form a proper helical structure, and the resultant molecule is weak and quickly destroyed.(Bienkowski RS, Baum BJ, Crystal RG. 1978) The end result is poor wound healing, and the clinical condition is called scurvy.(Hirschmann JV, Raugi GJ. 1999) The current recommended daily allowance for Vitamin C is 60mg; however, 200mg may be optimal.(Gross RL. 2000; Ayello EA, Thomas DR, Litchford MA. 1999) Some of the newly formed hydroxylysine amino acids are glycosylated by the addition of sugars, such as galactose and glucose.(Anttinen H, Myllyla R, Kivirikko KI. 1978) The enzymes that catalyze the glycosylation step, galactosyl and glucosyl transferases, require the trace metal manganese (Mn 2+ ). The glycosylation step imparts unique chemical and structural characteristics to the newly formed collagen molecule and may influence fibril size.(Kivirikko KI, Myllyla R. 1979) It is of interest to note that the glycosylation enzymes are found with the highest activities in the very young and decrease as we age.(Anttinen H, Oikarinen A, Kivirikko KI. 1977) While inside the cell and when the procollagen peptides are intact, the molecule is about 1,000 times more soluble than it is at a latter stage when - 20 -
the extension peptides are removed.(Prockop DJ, Kivirikko KI, Tuderman L, Guzman NA. 1979) This high degree of solubility allows the procollagen molecule to be transported easily within the cell where it is moved by means of specialized structures called microtubules to the cell surface where it is secreted into the extracellular spaces.(Diegelmann RF, Peterkofsky B. 1972) As the procollagen is secreted from the cell, it is acted upon by specialized enzymes called procollagen proteinases that remove both of the extension peptides from the ends of the molecule.(Lapiere CM, Lenaers A, Kohn LD. 1971) Portions of these digested end pieces are thought to re-enter the cell and regulate the amount of collagen synthesis by a feed-back type of mechanism.(Lichtenstein JR, Martin GR, Kohn LD, Byers PH, McKusick VA. 1973; Wiestner M, Krieg T, Horlein D, Glanville RW, Fietzek P, Muller PK. 1979) The processed molecule is referred to as collagen and now begins to be involved in the important process of fiber formation. In the extracellular spaces, another post-translational modification takes place as the triple helical collagen molecules (Figure 1) line up and begin to form fibrils and then fibers. This step is called crosslink formation and is promoted by another specialized enzyme called lysyl oxidase (Figure 3).(Bailey AJ, Robins SP, Balian G. 1974) This reaction places stable crosslinks within (intramolecular crosslinks) and between the molecules (intermolecular crosslinks). This is the critical step that gives the collagen fibers such tremendous strength. On a per weight basis, the strength of collagen approaches the tensile strength of steel. - 21 -
Page 1 and 2: 석 사 학 위 논 문 Human derma
Page 3 and 4: 김선아의 의학영양학 석사
Page 5 and 6: Ⅱ. Collagen and ascorbic acid ·
Page 7 and 8: List of Figures Figure Page 1. The
Page 9 and 10: Chapter I. LITERATURE REVIEW - 1 -
Page 11 and 12: kinetic energy is constantly in mot
Page 13 and 14: Figure 1. Triple-stranded helical m
Page 15 and 16: Table 1. Collagen types α Chains T
Page 17 and 18: is contains three identical α chai
Page 19 and 20: incluede in this category because o
Page 21 and 22: Type IX collagen is expressed in ca
Page 23 and 24: most immunogenic regions of type I
Page 25 and 26: Figure 2. Formation of collagen A p
Page 27: Fig 3. Collagen synthesis - 19 -
Page 31 and 32: synthesis and remolding continue at
Page 33 and 34: into collagenases, gelatinases, str
Page 35 and 36: 2003). While plasmin is a potent ac
Page 37 and 38: Baker et al. 2002). Although TIMPs
Page 39 and 40: produce clealvage under physiologic
Page 41 and 42: dietary ascorbic acid, scurvy devel
Page 43 and 44: than those cultured in the absence
Page 45 and 46: triple helices into the fivers and
Page 47 and 48: which were restored upon the additi
Page 49 and 50: Ⅳ. Prolyl hydroxylase Collagen pr
Page 51 and 52: mechanism leading to this retention
Page 53 and 54: esulting hydroxylysine residues hav
Page 55 and 56: 1988 Burgeson RE. The collagens of
Page 57 and 58: egeneration. Matrix 11:63-8, 1991 M
Page 59 and 60: 1985 Wood G. The heterogeneity of c
Page 61 and 62: Human dermal fibroblast cell에서
Page 63 and 64: 1. 서론 피부는 탄력성을
Page 65 and 66: 1. 세포배양 2. 재료 및 방
Page 67 and 68: 3. 세포의 증식측정 Human fib
Page 69 and 70: 4.2 Polymerase Chain Reaction (PCR)
Page 71 and 72: Table 3.1. Proliferation of HS27 ce
Page 73 and 74: 3.2. HS27 cell에서 ascorbic acid,
Page 75 and 76: ascorbic acid silicon lysine prolin
Page 77 and 78: ascorbic acid silicon lysine prolin
Page 79 and 80:
3.3. HS27 cell에서 ascorbic acid,
Page 81 and 82:
- 73 - 2) The signal intensity from
Page 83 and 84:
4. 요약 및 결론 피부 진피
Page 85 and 86:
참고문헌 1. Ishikawa T, Ishikaw
Page 87 and 88:
19. Katsuhiro Uzawa, Heather N. Yeo
Page 89 and 90:
5일 처리에 의해 증가하였
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경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

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