경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

More documents

Recommendations

Info

Ⅰ-3.2.2. Short chain collagens This group involves type VIII collagen and X collagens, which have similar structure and assembly but different distribution and function. Type VIII collagen has been found in the Descemet's membrane of the eye, vascular endothelial cells, and some tumor-derived cells. The type VIII collagen molecule has a triple helical region of 135nm in length, with a globular region at the C-terminus and a smaller globular region at the N-terminus. The entire triple-helical domain is encoded by one single exon. The triple helices have interruptions in the same positions in α-1(VIII) and α -2(VIII) chains. The function of type VIII collagen is as yet unknown.(Vuorio E, de Crombugghe B. 1990; Hulmes D. 1992) Type X collagen is a homotrimeric disulfide-bonded collagen and is the product of hypertrophic chondrocytes. It is the most specialized of the collagens, hacing a function related to cartilage mineralization. Its molecular structure is similar to that of type VIII collagen, especially in the triple-helical and C-terminal globular regions. Its triple helical domain has eight interruptions in the gly-X-Y repeat structure. The entire triple helical domain is encoded by one single exon. The function of type X collagen has been suggested to play a role in the formation of a framework during replacement of cartilage by bone and guiding endothelial cells during angiogenesis.(Hulmes D. 1992) Ⅰ-3.2.3. Fibril-associated collagens This subgroup, fibril-associated collagens with interrupted triple-helices(FACIT), comprises type IX, XII, and XIV collagens. These collagens attach to the surface of pre-existing fibrils. - 12 -
Type IX collagen is expressed in cartilages (1-10% of total collagens). It is a heterotrimer, contains three short triple helical domains with interchain disulfide bonds, and has a large globular region at the N-terminus of cartilage α-1(I). The function of type IX collagen remains unknown although it may have a role in mediating the interaction between type II collagen and proteoglycans in cartilage. Type IX molecules have been localized on the surface of cartilage type II collagen fibrils in a periodic distribution.(Vaughan L, Mendler M, Huber S, et al. 1988) The interaction between type IX and II collagens is stabilized by covalent intermolecular cross-links.(Eyre D, Wu J. 1987; van der Rest M, Mayne R. 1988) Type XII collagen is found in dense collagen I-containing connective tissues such as tendons and ligaments.(Gordon M, Gerecke D, Dublet B, et al. 1989; Yamagata M, Yamagada K, Yamada S, et al. 1991). The molecule is a homotrimer of three α-1(XII) chains, where each chain has two triple-helical eomains. Because of the similarity with type IX collagen, an analogous function has been suggested: lateral association with type I collagen on the surfaces of fibrils.(Vuorio E, de Crombugghe B. 1990) Type XIV collagen is found in skin and tendon. Further studies are necessary to determine whether structural homology exists with type XII collagen. Ⅰ-3.3. Type I Collagen When the term collagen is used, it usually means type Ⅰ collagne, the most common of the collagens in vertebrates. It comprises up to 90% of the skeletons of the mammals and is also widespread all over the body: in addition to bones, it is found in skin, tendons, ligaments, cornea, - 13 -
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: incluede in this category because o
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 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
show all

경희대학교 동서의학대학원 의 학 영 양 학 과 김 선 아

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?