경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

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deposition of collagen type Ⅰ, which constitutes 90% of the total organic extracellular matrix in mature bone, by preosteoblasts or early undifferentiated osteoblast-like cells (Boskey AL, Wright TM, Blank RD. 1999). - 40 -
Ⅳ. Prolyl hydroxylase Collagen prolyl 4-hydroxylases (P4Hs, EC 1.14.11.2) are located within the lumen of the endoplasmic reticulum and catalyze the formation of 4-hydroxyproline by the hydroxylation of prolines in -X-Pro-Gly- sequences in collagens and more than 15 other proteins that have collagen-like domains (Kivirikko and Myllyharju, 1998; Kivirikko and Pihlajaniemi, 1998; Myllyharju and Kivirikko, 2001). P4Hs have a central role in the biosynthesis of collagens, as 4-hydroxyproline residues are essential for the formation of the collagen triple helix. In addition, a novel and distinct family of cytoplasmic prolyl 4-hydroxylases playing a critical role in the regulation of the hypoxia-inducible transcription factor HIF a has recently been identified (Bruick and Mc- Knight, 2001; Epstein et al., 2001). No overall amino acid sequence homology is detected between the collagen and HIF P4Hs, with the exception that the catalytically critical residues are conserved. Collagen P4Hs from all vertebrate sources studied are α2β2 tetramers in which the β subunit is identical to protein disulfide isomerase (PDI) (Kivirikko and Myllyharju, 1998; Kivirikko and Pihlajaniemi, 1998). Several isoforms of the catalytic a subunit are found in human and mouse tissues, Caenorhabditis elegans and Drosophila melanogaster (Veijola et al., 1994; Helaakoski et al., 1995; Annunen et al., 1997, 1999; Friedman et al., 2000; Hill et al., 2000; Winter and Page, 2000; Abrams and Andrew, 2002; Riihimaa et al., 2002). Successful production of active recombinant P4H by coexpression of the a and PDI/β subunits in insect cells (Vuori et al., 1992) - 41 -
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 and 28: Fig 3. Collagen synthesis - 19 -
Page 29 and 30: the extension peptides are removed.
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: which were restored upon the additi
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

경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

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