경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

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MT5-MMP (MMP-24) is restricted to brain, while the other MT-MMPs are more widely expressed (Visse &Nagase 2003). For their pericellular fibrinolytic activity, MT-MMPs have an important role in angiogenesis (Sternlicht &Werb 2001). Seven MMPs are currently classified into the group of “other MMPs”. MMP-12 is mainly expressed in macrophages and it degrades a large variety of proteins (Shapiro et al. 1993). MMP-19 is a novel member identified from patients with rheumatoid arthritis, therefore initially named RASI-1 (Kolb et al. 1997). MMP-20 is currently considered a tooth-specific MMP, with the expression strictly restricted to dental cells in vivo (Palosaari et al. 2003). MMP-22 is known to be expressed in chicken embryo fibroblasts, and it seems to digest gelatine (Yang &Kurkinen 1998). MMP-23 is a transmembrane protein expressed in reproductive tissue (Visse &Nagase 2003). The expression patterns of the newest member of the MMP family, MMP-28, suggest functions in skin hemostasis and wound repair (Illman et al. 2003). The expression of MMPs is primarily regulated at the level of transcription, while the proteolytic activity is regulated by latent precursor activation and inhibition of activity. Cytokines, growth factors and corticosteroids are known to induce or repress the transcription of MMP genes (See Table 1 for details) (Windsor et al. 1993, Birkedal-Hansen 1995, Cimpean &Caloianu 1997, Morin et al. 1999, Singer et al. 1999, Feinberg et al. 2000, Li et al. 2000, Delany &Canalis 2001, Kang et al. 2001, Mauch et al. 2002). On the other hand, MMPs are known to regulate the activity of many cytokines and growth factors (Sternlicht &Werb 2002, Visse &Nagase - 26 -
2003). While plasmin is a potent activator of various MMPs, the zymogens can also be activated by other enzymes as well as other MMPs (Bassi et al. 2000, Kotra et al. 2001, Palosaari et al. 2002, Illman et al. 2003). In addition to its role in inhibition of MMPs, TIMP-2 also has a role in the activation of MMP-2 (Strongin et al. 1995). The modulators of the latest MMPs are presently unknown. MMP-1, MMP-2, MMP-9 and MMP-16 are expressed in bovine skeletal muscle on mRNA level (Balcerzak et al. 2001), and MMP-1, MMP-2 and MMP-9 proteins in human skeletal muscle (Singh et al. 2000). Although MMP-13 and MMP-15 expression are not observed in the bovine muscle, their mRNAs are found in the RNA extracted from skeletal muscle connective tissue cells (Balcerzak et al. 2001). Therefore it seems that MMP-13 and MMP-15 are expressed in skeletal muscle in tiny amounts. In muscle diseases, also MMP-3, MMP-7, MMP-10 and MMP-11 proteins have been reported in human skeletal muscle (Schoser &Blottner 1999, Kieseier et al. 2001). In skeletal muscle, MMPs are primarily expressed by fibroblasts, although some level of expression has been found to occur also in satellite cells (Guérin &Holland 1995, Balcerzak et al. 2001). MMP-9 is expressed in skeletal muscle mainly by infiltrating leukocytes (Kherif et al. 1999, Kieseier et al. 2001). Ⅰ-5.1.1. MMP inhibition by TIMPs MMP activity can be specifically inhibited by tissue inhibitors of metalloproteinases (TIMPs) as well as by non-specific inhibitors including e.g. α2-macroglobulin, RECK and tissue factor pathway inhibitor-2 (Baker et - 27 -
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: into collagenases, gelatinases, str
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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