메뉴 건너뛰기




Volumn 97, Issue 7, 2005, Pages 557-568

Collagen reorganization in leech wound healing

Author keywords

Atomic force microscopy (AFM); Collagen injury; Scanning electron microscopy (SEM); Transmission electron microscopy (TEM)

Indexed keywords

COLLAGEN FIBRIL; PROTEOGLYCAN;

EID: 21644470117     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1042/BC20040085     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 0021193618 scopus 로고
    • Structure of human basement membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha-I (IV) chain
    • Babel, W. and Glanville, R.W. (1984) Structure of human basement membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha-I (IV) chain. Eur. J. Biochem. 143, 545-556
    • (1984) Eur. J. Biochem. , vol.143 , pp. 545-556
    • Babel, W.1    Glanville, R.W.2
  • 3
    • 0036421529 scopus 로고    scopus 로고
    • The extracellular matrix as a scaffold for tissue reconstruction
    • Badylak, S.F. (2002) The extracellular matrix as a scaffold for tissue reconstruction. Semin. Cell Dev. Biol. 13, 377-383
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 377-383
    • Badylak, S.F.1
  • 5
    • 0021687083 scopus 로고
    • Extracellular compartments in matrix morphogenesis: Collagen fibril, bundle, and lamellar formation by corneal fibroblasts
    • Birk, D.E. and Trelstad, R.L. (1984) Extracellular compartments in matrix morphogenesis: collagen fibril, bundle, and lamellar formation by corneal fibroblasts. J. Cell Biol. 99, 2024-2033
    • (1984) J. Cell Biol. , vol.99 , pp. 2024-2033
    • Birk, D.E.1    Trelstad, R.L.2
  • 6
    • 0028235645 scopus 로고
    • Assembly of the tendon extracellular matrix during development
    • Birk, D.E. and Zycband, E. (1994) Assembly of the tendon extracellular matrix during development. J. Anat. 184, 457-463
    • (1994) J. Anat. , vol.184 , pp. 457-463
    • Birk, D.E.1    Zycband, E.2
  • 7
    • 0024351538 scopus 로고
    • Collagen fibril bundles: A branching assembly unit in tendon morphogenesis
    • Birk, D.E., Southern, J.F., Zycband, E., Fallon, J.T. and Trelstad, R.L. (1989) Collagen fibril bundles: a branching assembly unit in tendon morphogenesis. Development 107, 437-443
    • (1989) Development , vol.107 , pp. 437-443
    • Birk, D.E.1    Southern, J.F.2    Zycband, E.3    Fallon, J.T.4    Trelstad, R.L.5
  • 8
    • 0030198753 scopus 로고    scopus 로고
    • Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon
    • Birk, D.E., Hahn, R.A., Linsemayer, C.Y. and Zycband, E. (1996) Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon. Matrix Biol. 15, 111-118
    • (1996) Matrix Biol. , vol.15 , pp. 111-118
    • Birk, D.E.1    Hahn, R.A.2    Linsemayer, C.Y.3    Zycband, E.4
  • 9
    • 0037562793 scopus 로고    scopus 로고
    • Collagen fibrils appear more closely packed in the prepulpillary cornea: Optical and biomedical implications
    • Boote, C., Dennis, S., Newton, R.H., Puri, H. and Meek, K.M. (2003) Collagen fibrils appear more closely packed in the prepulpillary cornea: optical and biomedical implications. Invest. Ophthal. Vis. Sci. 44, 2941-2948
    • (2003) Invest. Ophthal. Vis. Sci. , vol.44 , pp. 2941-2948
    • Boote, C.1    Dennis, S.2    Newton, R.H.3    Puri, H.4    Meek, K.M.5
  • 10
    • 4344571831 scopus 로고
    • A cytological and histochemical study of the connective-tissue fibres of the leech, Hirudo medicinalis
    • Bradbury, S. (1958) A cytological and histochemical study of the connective-tissue fibres of the leech, Hirudo medicinalis. Q J. Microsc. Sci. 99, 131-142
    • (1958) Q. J. Microsc. Sci. , vol.99 , pp. 131-142
    • Bradbury, S.1
  • 11
    • 4344647265 scopus 로고
    • A study of fibrogenesis in the leech, Hirudo medicinalis
    • Bradbury, S. and Meek, G.A. (1958) A study of fibrogenesis in the leech, Hirudo medicinalis. Q. J. Microsc. Sci. 99, 143-148
    • (1958) Q. J. Microsc. Sci. , vol.99 , pp. 143-148
    • Bradbury, S.1    Meek, G.A.2
  • 12
    • 0002012699 scopus 로고
    • The choice of resins for electron immunocytochemistry
    • (Polack, J.M. and Varndell I.M., eds.), Elsevier, Amsterdam
    • Causton, B. E. (1984) The choice of resins for electron immunocytochemistry. In Immunolabelling for Electron Microscopy (Polack, J.M. and Varndell I.M., eds.), pp. 17-28, Elsevier, Amsterdam
    • (1984) Immunolabelling for Electron Microscopy , pp. 17-28
    • Causton, B.E.1
  • 13
    • 0025337123 scopus 로고
    • A highly specific and quantitative method for determining Type III-I collagen ratios in tissues
    • Cheung, D.T., Benya, P.D., Perelman, N., Dicesare, P.E. and Nimni, M.E. (1990) A highly specific and quantitative method for determining Type III-I collagen ratios in tissues. Matrix 10, 164-171
    • (1990) Matrix , vol.10 , pp. 164-171
    • Cheung, D.T.1    Benya, P.D.2    Perelman, N.3    Dicesare, P.E.4    Nimni, M.E.5
  • 15
    • 0037360165 scopus 로고    scopus 로고
    • How do fibroblasts translate mechanical signal into changes in extracellular matrix production?
    • Chiquet, M., Renedo, A.S., Huber, F. and Fluck, M. (2003) How do fibroblasts translate mechanical signal into changes in extracellular matrix production? Matrix Bol. 22, 73-80
    • (2003) Matrix Biol. , vol.22 , pp. 73-80
    • Chiquet, M.1    Renedo, A.S.2    Huber, F.3    Fluck, M.4
  • 16
    • 0033813556 scopus 로고    scopus 로고
    • Assembly of type I collagen: Fusion of fibril subunits and the influence of fibril diameter on mechanical properties
    • Christiansen, D.L., Huang, E.K. and Silver, F.H. (2000) Assembly of type I collagen: fusion of fibril subunits and the influence of fibril diameter on mechanical properties. Matrix Biol. 19, 409-420
    • (2000) Matrix Biol. , vol.19 , pp. 409-420
    • Christiansen, D.L.1    Huang, E.K.2    Silver, F.H.3
  • 22
    • 0011882463 scopus 로고
    • Collagen of Coelenterates
    • (Bairati, A. and Garrone, R., eds.), Plenum, New York
    • Franc, S. (1985) Collagen of Coelenterates. In Biology of Invertebrates and Lower Vertebrates Collagens (Bairati, A. and Garrone, R., eds.), pp. 197-210, Plenum, New York
    • (1985) Biology of Invertebrates and Lower Vertebrates Collagens , pp. 197-210
    • Franc, S.1
  • 24
    • 0029816069 scopus 로고    scopus 로고
    • Stimulation of fibroblast cell growth, matrix production and granulation tissue formation by connective tissue growth factor
    • Frazier, K., Williams, S., Kothapalli, D., Klapper, H. and Grotendorst, G.R. (1996) Stimulation of fibroblast cell growth, matrix production and granulation tissue formation by connective tissue growth factor. J. Invest. Dermatol. 107, 404-411
    • (1996) J. Invest. Dermatol. , vol.107 , pp. 404-411
    • Frazier, K.1    Williams, S.2    Kothapalli, D.3    Klapper, H.4    Grotendorst, G.R.5
  • 25
    • 0028577358 scopus 로고
    • Immunological properties and tissue localization of two different collagen types in annelid and vestimentifera species
    • Gaill, F., Hamraoui, L., Sicot, F.X. and Timpl, R. (1994) Immunological properties and tissue localization of two different collagen types in annelid and vestimentifera species. Eur. J. Cell Biol. 65, 392-401
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 392-401
    • Gaill, F.1    Hamraoui, L.2    Sicot, F.X.3    Timpl, R.4
  • 28
    • 0002817533 scopus 로고
    • Collagen and other matrix glycoproteins in embryogenesis
    • (Hay, E., ed.), Plenum Publishing, New York
    • Hay, E. (1991) Collagen and other matrix glycoproteins in embryogenesis. In Cell Biology of Extracellular Matrix (Hay, E., ed.), pp. 419-462, Plenum Publishing, New York
    • (1991) Cell Biology of Extracellular Matrix , pp. 419-462
    • Hay, E.1
  • 29
    • 0034781276 scopus 로고    scopus 로고
    • Three-dimensional supramolecular organization of the extracellular matrix in human and rabbit corneal stroma, as revealed by ultrarapid-freezing and deep-etching methods
    • Hirsch, M., Prenant, G. and Renard, G. (2001) Three-dimensional supramolecular organization of the extracellular matrix in human and rabbit corneal stroma, as revealed by ultrarapid-freezing and deep-etching methods. Exp. Eye Res. 72, 123-135
    • (2001) Exp. Eye Res. , vol.72 , pp. 123-135
    • Hirsch, M.1    Prenant, G.2    Renard, G.3
  • 30
    • 0028282547 scopus 로고
    • Cellular tensegrety: Exploring how mechanical changes in the cytoskeleton regulate cell growth, migration and tissue pattern during morphogenesis
    • Ingber, D. (1994) Cellular tensegrety: exploring how mechanical changes in the cytoskeleton regulate cell growth, migration and tissue pattern during morphogenesis. Int. Rev. Cytol. 150, 173-224
    • (1994) Int. Rev. Cytol. , vol.150 , pp. 173-224
    • Ingber, D.1
  • 31
    • 0038441495 scopus 로고    scopus 로고
    • Microstructure, mechanical and biomimetic properties of fish scales from Pagrus major
    • Ikoma, T., Kobayashi, H., Tanaka, J., Walsh, D. and Mann, S. (2003) Microstructure, mechanical and biomimetic properties of fish scales from Pagrus major. J. Struct. Biol. 142, 327-333
    • (2003) J. Struct. Biol. , vol.142 , pp. 327-333
    • Ikoma, T.1    Kobayashi, H.2    Tanaka, J.3    Walsh, D.4    Mann, S.5
  • 34
    • 0242290312 scopus 로고    scopus 로고
    • Collagen XXIV, a vertebrate fibrillar collagen with structural features of invertebrate collagens: Selective expression in developing cornea and bone
    • Koch, M., Laub, F., Zhou, P., Hahn, R.A., Tanaka, S., Burgeson, R.E., Gerecke, D.R., Ramirez, F. and Gordon, M.K. (2003) Collagen XXIV, a vertebrate fibrillar collagen with structural features of invertebrate collagens: selective expression in developing cornea and bone. J. Biochem. Chem. 278, 43236-43244
    • (2003) J. Biochem. Chem. , vol.278 , pp. 43236-43244
    • Koch, M.1    Laub, F.2    Zhou, P.3    Hahn, R.A.4    Tanaka, S.5    Burgeson, R.E.6    Gerecke, D.R.7    Ramirez, F.8    Gordon, M.K.9
  • 36
    • 2642600388 scopus 로고
    • Studies on the helical and paramiosinic muscles. VI. Submicroscopic organization and function of body wall muscle fibers in some leeches
    • Lanzavecchia, G., de Eguileor, M., Vailati, G. and Valvassori, R. (1977) Studies on the helical and paramiosinic muscles. VI. Submicroscopic organization and function of body wall muscle fibers in some leeches. Boll. Zool. 44, 311-326
    • (1977) Boll. Zool. , vol.44 , pp. 311-326
    • Lanzavecchia, G.1    de Eguileor, M.2    Vailati, G.3    Valvassori, R.4
  • 37
    • 0028180918 scopus 로고
    • Expression of α2 type I collagen in W8 cells increases cell adhesion and decreases colony formation in soft agar
    • Lim, A., Greenspan, D.S. and Smith, B.D. (1994) Expression of α2 type I collagen in W8 cells increases cell adhesion and decreases colony formation in soft agar. Matrix Biol. 14, 21-30
    • (1994) Matrix Biol. , vol.14 , pp. 21-30
    • Lim, A.1    Greenspan, D.S.2    Smith, B.D.3
  • 39
    • 0026433425 scopus 로고
    • Extracellular matrix molecules in development and regeneration of the leech CNS
    • Masuda-Nakagawa, L.M. and Nicholls, J.G. (1991) Extracellular matrix molecules in development and regeneration of the leech CNS. Philos. Trans. R. Soc. Lond. 331, 323-335
    • (1991) Philos. Trans. R. Soc. Lond. , vol.331 , pp. 323-335
    • Masuda-Nakagawa, L.M.1    Nicholls, J.G.2
  • 40
    • 0024294875 scopus 로고
    • Identification of molecules in leech extracellular matrix that promote neurite outgrowth
    • Masuda-Nakagawa, L.M., Beck, K. and Chiquet, M. (1988) Identification of molecules in leech extracellular matrix that promote neurite outgrowth. Proc. R. Soc. Lond. 235, 247-257
    • (1988) Proc. R. Soc. Lond. , vol.235 , pp. 247-257
    • Masuda-Nakagawa, L.M.1    Beck, K.2    Chiquet, M.3
  • 42
    • 0031033337 scopus 로고    scopus 로고
    • In situ localization of two fibrillar collagens in two compact connective tissues by immunoelectron microscopy after cryotechnical processing
    • Nicolas, G., Gaill, F. and Zylberberg, L. (1997) In situ localization of two fibrillar collagens in two compact connective tissues by immunoelectron microscopy after cryotechnical processing. J. Histochem. Cytochem. 45, 119-128
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 119-128
    • Nicolas, G.1    Gaill, F.2    Zylberberg, L.3
  • 44
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • Ottani, V., Raspanti, M. and Ruggeri, A. (2001) Collagen structure and functional implications. Micron 32, 251-260
    • (2001) Micron. , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 46
    • 0034908351 scopus 로고    scopus 로고
    • Platelet-derived growth factor and transforming growth factor-β in invertebrate immune and neuroendocrine interactions: Another sign of conservation in evolution
    • Ottaviani, E., Franchini, A. and Kletsas, D. (2001) Platelet-derived growth factor and transforming growth factor-β in invertebrate immune and neuroendocrine interactions: another sign of conservation in evolution. Comp. Biochem. Physiol. 129, 295-306
    • (2001) Comp. Biochem. Physiol. , vol.129 , pp. 295-306
    • Ottaviani, E.1    Franchini, A.2    Kletsas, D.3
  • 47
    • 0002458019 scopus 로고
    • Growth and development of collagen fibrils in connective tissue
    • (Ruggeri, A. and Motta, P.M., eds.), Martinus Nijhoff, The Hague
    • Parry, D.A.D. and Craig, A.S. (1984) Growth and development of collagen fibrils in connective tissue. In Ultrastructure of the Connective Tissue Matrix (Ruggeri, A. and Motta, P.M., eds.), pp. 34-64, Martinus Nijhoff, The Hague
    • (1984) Ultrastructure of the Connective Tissue Matrix , pp. 34-64
    • Parry, D.A.D.1    Craig, A.S.2
  • 48
    • 0036241448 scopus 로고    scopus 로고
    • Structural aspects of the extracellular matrix of tendon: An atomic force and scanning electron microscopy study
    • Raspanti, M., Congiu, T. and Guizzardi, S. (2002) Structural aspects of the extracellular matrix of tendon: an atomic force and scanning electron microscopy study. Arch. Histol. Cytol. 65, 37-43
    • (2002) Arch. Histol. Cytol. , vol.65 , pp. 37-43
    • Raspanti, M.1    Congiu, T.2    Guizzardi, S.3
  • 50
    • 0025075184 scopus 로고
    • A comparative biochemical and ultrastructural study of proteoglycan-collagen interactions in corneal stroma. Functional and metabolic implications
    • Scott, E.S. and Bosworth, T.R. (1990) A comparative biochemical and ultrastructural study of proteoglycan-collagen interactions in corneal stroma. Functional and metabolic implications. Biochem. J. 270, 491-497
    • (1990) Biochem. J. , vol.270 , pp. 491-497
    • Scott, E.S.1    Bosworth, T.R.2
  • 51
    • 0030970733 scopus 로고    scopus 로고
    • Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagen
    • Sicot, F.X., Exposito, J.Y., Masselot, M., Garrone, R., Deutsch, J. and Gaill, F. (1997) Cloning of an annelid fibrillar-collagen gene and phylogenetic analysis of vertebrate and invertebrate collagen. Eur. J. Biochem. 246, 50-58
    • (1997) Eur. J. Biochem. , vol.246 , pp. 50-58
    • Sicot, F.X.1    Exposito, J.Y.2    Masselot, M.3    Garrone, R.4    Deutsch, J.5    Gaill, F.6
  • 52
    • 0034731522 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces expression of connective tissue growth factor via KDR, Flt1, and phosphatidylinositol 3-kinase-Akt-dependent pathways in retinal vascular cells
    • Suzuma, K., Naruse, K., Suzuma, I., Takahara, N., Ueki, K., Aiello, L.P. and King, G. (2000) Vascular endothelial growth factor induces expression of connective tissue growth factor via KDR, Flt1, and phosphatidylinositol 3-kinase-Akt-dependent pathways in retinal vascular cells. J. Biol. Chem. 52, 40725-40731
    • (2000) J. Biol. Chem. , vol.52 , pp. 40725-40731
    • Suzuma, K.1    Naruse, K.2    Suzuma, I.3    Takahara, N.4    Ueki, K.5    Aiello, L.P.6    King, G.7
  • 54
  • 55
    • 0018762445 scopus 로고
    • Tendon collagen fibrillogenesis: Intracellular subassemblies and cell surface changes associated with fibril growth
    • Trelstad, R.L. and Hayashi, K. (1979) Tendon collagen fibrillogenesis: intracellular subassemblies and cell surface changes associated with fibril growth. Dev. Biol. 71, 228-242
    • (1979) Dev. Biol. , vol.71 , pp. 228-242
    • Trelstad, R.L.1    Hayashi, K.2
  • 56
    • 0034647432 scopus 로고    scopus 로고
    • Echinoderm collagen fibrils grow by surface-nucleation-propagation from both centres and ends
    • Trotter, J.A., Kadler, K.E. and Holmes, D.F. (2000) Echinoderm collagen fibrils grow by surface-nucleation-propagation from both centres and ends. J. Mol. Biol. 300, 531-540
    • (2000) J. Mol. Biol. , vol.300 , pp. 531-540
    • Trotter, J.A.1    Kadler, K.E.2    Holmes, D.F.3
  • 57
    • 0024493670 scopus 로고
    • Anisotropic and biochemical properties of tendons modified by exercise and denervation: Aggregation and macromolecular order in collagen bundles
    • Vilarta, R. and De Campos Vidal, B. (1989) Anisotropic and biochemical properties of tendons modified by exercise and denervation: aggregation and macromolecular order in collagen bundles. Matrix 9, 55-61
    • (1989) Matrix , vol.9 , pp. 55-61
    • Vilarta, R.1    De Campos Vidal, B.2
  • 58
    • 32644482406 scopus 로고
    • The basement lamella of amphibian skin. Its reconstruction after wounding
    • Weiss, P. and Ferris, W. (1956) The basement lamella of amphibian skin. Its reconstruction after wounding. J. Biophys. Biochem. Cytol. 2, 275-281
    • (1956) J. Biophys. Biochem. Cytol. , vol.2 , pp. 275-281
    • Weiss, P.1    Ferris, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.