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Volumn 15, Issue 2, 1996, Pages 111-118

Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon

Author keywords

Chicken; Collagen fibril; Cornea; Dermis; Development; Fibril assembly; Fibril segment; Tendon

Indexed keywords

COLLAGEN FIBRIL; SODIUM CHLORIDE;

EID: 0030198753     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(96)90152-3     Document Type: Article
Times cited : (67)

References (34)
  • 1
    • 0003054974 scopus 로고
    • Collagen fibril assembly, deposition, and organization into tissue-specific matrices
    • P.D. Yurchenco, D.E. Birk, Mecham R.P. New York: Academic Press
    • Birk D.E., Linsenmayer T.F. Collagen fibril assembly, deposition, and organization into tissue-specific matrices. Yurchenco P.D., Birk D.E., Mecham R.P. Extracellular Matrix Assembly and Structure. 1994;91-128 Academic Press, New York.
    • (1994) Extracellular Matrix Assembly and Structure , pp. 91-128
    • Birk, D.E.1    Linsenmayer, T.F.2
  • 2
    • 0028923480 scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments undergo post-depositional modifications resulting in linear and lateral growth during matrix development
    • Birk D.E., Nurminskaya M.V., Zycband E.I. Collagen fibrillogenesis in situ: fibril segments undergo post-depositional modifications resulting in linear and lateral growth during matrix development. Develop. Dynam. 202:1995;229-243.
    • (1995) Develop. Dynam. , vol.202 , pp. 229-243
    • Birk, D.E.1    Nurminskaya, M.V.2    Zycband, E.I.3
  • 4
  • 5
    • 0021687083 scopus 로고
    • Extracellular compartments in matrix morphogenesis: Collagen fibril, bundle, and lamellar formation by corneal fibroblasts
    • Birk D.E., Trelstad R.L. Extracellular compartments in matrix morphogenesis: collagen fibril, bundle, and lamellar formation by corneal fibroblasts. J. Cell Biol. 99:1984;2024-2033.
    • (1984) J. Cell Biol. , vol.99 , pp. 2024-2033
    • Birk, D.E.1    Trelstad, R.L.2
  • 6
    • 0022470549 scopus 로고
    • Extracellular compartments in tendon morphogenesis: Collagen fibril, bundle, and macroaggregate formation
    • Birk D.E., Trelstad R.L. Extracellular compartments in tendon morphogenesis: collagen fibril, bundle, and macroaggregate formation. J. Cell Biol. 103:1986;231-240.
    • (1986) J. Cell Biol. , vol.103 , pp. 231-240
    • Birk, D.E.1    Trelstad, R.L.2
  • 7
    • 2542553125 scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments are intermediates in matrix assembly
    • Birk D.E., Zycband E.I., Winkelmann D.A., Trelstad R.L. Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly. Proc. Natl. Acad. Sci. USA. 86:1989b;4549-4553.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4549-4553
    • Birk, D.E.1    Zycband, E.I.2    Winkelmann, D.A.3    Trelstad, R.L.4
  • 8
    • 0025292972 scopus 로고
    • Collagen fibrillogenesis in situ. Discontinuous segmental assembly in extracellular compartments
    • Birk D.E., Zycband E.I., Winkelmann D.A., Trelstad R.L. Collagen fibrillogenesis in situ. Discontinuous segmental assembly in extracellular compartments. Ann. N.Y. Acad. Sci. 580:1990;176-194.
    • (1990) Ann. N.Y. Acad. Sci. , vol.580 , pp. 176-194
    • Birk, D.E.1    Zycband, E.I.2    Winkelmann, D.A.3    Trelstad, R.L.4
  • 9
    • 0028235645 scopus 로고
    • Assembly of the tendon extracellular matrix during development
    • Birk D.E., Zycband E. Assembly of the tendon extracellular matrix during development. J. Anat. 184:1994;457-463.
    • (1994) J. Anat. , vol.184 , pp. 457-463
    • Birk, D.E.1    Zycband, E.2
  • 10
    • 0024412103 scopus 로고
    • The regulation of size and form in the assembly of collagen fibrils in vivo
    • Chapman J.A. The regulation of size and form in the assembly of collagen fibrils in vivo. Biopolymers. 28:1989;1367-1382.
    • (1989) Biopolymers , vol.28 , pp. 1367-1382
    • Chapman, J.A.1
  • 11
    • 0024313452 scopus 로고
    • An estimate of the mean length of collagen fibrils in rat tail-tendon as a function of age
    • Craig A.S., Birtles M.J., Conway J.F., Parry D.A. An estimate of the mean length of collagen fibrils in rat tail-tendon as a function of age. Connect. Tissue Res. 19:1989;51-62.
    • (1989) Connect. Tissue Res. , vol.19 , pp. 51-62
    • Craig, A.S.1    Birtles, M.J.2    Conway, J.F.3    Parry, D.A.4
  • 12
    • 84924926133 scopus 로고
    • A series of normal stages in development of the chick embroy
    • Hamburger V., Hamilton H.L. A series of normal stages in development of the chick embroy. J. Morphol. 88:1951;49-92.
    • (1951) J. Morphol. , vol.88 , pp. 49-92
    • Hamburger, V.1    Hamilton, H.L.2
  • 13
    • 0017409329 scopus 로고
    • A study of the growth of normal and iodinated collagen fibrils in vitro using electron microscope autoradiography
    • Haworth R.A., Chapman J.A. A study of the growth of normal and iodinated collagen fibrils in vitro using electron microscope autoradiography. Biopolymers. 16:1977;1895-1906.
    • (1977) Biopolymers , vol.16 , pp. 1895-1906
    • Haworth, R.A.1    Chapman, J.A.2
  • 14
    • 0026756620 scopus 로고
    • Growing tips of type I collagen fibrils formed in vitro are near-paraboloidal in shape, implying a reciprocal relationship between accretion and diameter
    • Holmes D.F., Chapman J.A., Prockop D.J., Kadler K.E. Growing tips of type I collagen fibrils formed in vitro are near-paraboloidal in shape, implying a reciprocal relationship between accretion and diameter. Proc. Natl. Acad. Sci. USA. 89:1992;9855-9859.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9855-9859
    • Holmes, D.F.1    Chapman, J.A.2    Prockop, D.J.3    Kadler, K.E.4
  • 15
    • 0028158454 scopus 로고
    • Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity
    • Holmes D.F., Lowe M.P., Chapman J.A. Vertebrate (chick) collagen fibrils formed in vivo can exhibit a reversal in molecular polarity. J. Mol. Biol. 235:1994;80-83.
    • (1994) J. Mol. Biol. , vol.235 , pp. 80-83
    • Holmes, D.F.1    Lowe, M.P.2    Chapman, J.A.3
  • 16
    • 0018802455 scopus 로고
    • Axial mass distributions of collagen fibrils grown in vitro: Results for the end regions of early fibrils
    • Holmes D.F., Chapman J.A. Axial mass distributions of collagen fibrils grown in vitro: results for the end regions of early fibrils. Biochem. Biophys. Res. Commun. 87:1979;993-999.
    • (1979) Biochem. Biophys. Res. Commun. , vol.87 , pp. 993-999
    • Holmes, D.F.1    Chapman, J.A.2
  • 17
    • 0023656926 scopus 로고
    • Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process
    • Kadler K.E., Hojima Y., Prockop D.J. Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process. J. Biol. Chem. 262:1987;15696-15701.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15696-15701
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 18
    • 0025358337 scopus 로고
    • Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction
    • Kadler K.E., Hojima Y., Prockop D.J. Collagen fibrils in vitro grow from pointed tips in the C- to N-terminal direction. Biochem. J. 268:1990a;339-343.
    • (1990) Biochem. J. , vol.268 , pp. 339-343
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 19
    • 0025316412 scopus 로고
    • Assembly of type I collagen fibrils de novo by the specific enzymic cleavage of pC collagen. The fibrils formed at about 37 degrees C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue
    • Kadler K.E., Hulmes D.J., Hojima Y., Prockop D.J. Assembly of type I collagen fibrils de novo by the specific enzymic cleavage of pC collagen. The fibrils formed at about 37 degrees C are similar in diameter, roundness, and apparent flexibility to the collagen fibrils seen in connective tissue. Ann. NY Acad. Sci. 580:1990b;214-224.
    • (1990) Ann. NY Acad. Sci. , vol.580 , pp. 214-224
    • Kadler, K.E.1    Hulmes, D.J.2    Hojima, Y.3    Prockop, D.J.4
  • 23
    • 0002458019 scopus 로고
    • Growth and development of collagen fibrils in connective tissue
    • A. Ruggeri, Morta P.M. Boston: Martinus Nijohoff
    • Parry D.A.D., Craig A.S. Growth and development of collagen fibrils in connective tissue. Ruggeri A., Morta P.M. Ultrastructure of the Connective Tissue Matrix. 1984;34-64 Martinus Nijohoff, Boston.
    • (1984) Ultrastructure of the Connective Tissue Matrix , pp. 34-64
    • Parry, D.A.D.1    Craig, A.S.2
  • 24
    • 0025827384 scopus 로고
    • Collagen fibril assembly and deposition in the developing dermis: Segmental deposition in extracellular compartments
    • Ploetz C., Zycband E.I., Birk D.E. Collagen fibril assembly and deposition in the developing dermis: segmental deposition in extracellular compartments. J. Struct. Biol. 106:1991;73-81.
    • (1991) J. Struct. Biol. , vol.106 , pp. 73-81
    • Ploetz, C.1    Zycband, E.I.2    Birk, D.E.3
  • 25
    • 0002751244 scopus 로고
    • Assembly of collagen fibrils de novo from soluble precursors; Polymerization and copolimerization of procollagen, pN-collagen, and mutated collagens
    • P.D. Yurchenco, D.E. Birk, Mecham R.P. New York: Academic Press
    • Prockop D.J., Hulmes D.J.S. Assembly of collagen fibrils de novo from soluble precursors; polymerization and copolimerization of procollagen, pN-collagen, and mutated collagens. Yurchenco P.D., Birk D.E., Mecham R.P. Extracellular Matrix Assembly and Structure. 1994;47-90 Academic Press, New York.
    • (1994) Extracellular Matrix Assembly and Structure , pp. 47-90
    • Prockop, D.J.1    Hulmes, D.J.S.2
  • 26
    • 0026545753 scopus 로고
    • Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic study
    • Romanic A.M., Adachi E., Hojima Y., Engel J., Prockop D.J. Polymerization of pNcollagen I and copolymerization of pNcollagen I with collagen I. A kinetic, thermodynamic, and morphologic study. J. Biol. Chem. 267:1992;22265-22271.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22265-22271
    • Romanic, A.M.1    Adachi, E.2    Hojima, Y.3    Engel, J.4    Prockop, D.J.5
  • 27
    • 0026599612 scopus 로고
    • Identification of chick corneal keratan sulfate proteoglycan precursor protein in whole corneas and in cultured corneal fibroblasts
    • Schrecengost P.K., Blochberger T.C., Hassell J.R. Identification of chick corneal keratan sulfate proteoglycan precursor protein in whole corneas and in cultured corneal fibroblasts. Arch. Biochem. Biophys. 292:1992;54-61.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 54-61
    • Schrecengost, P.K.1    Blochberger, T.C.2    Hassell, J.R.3
  • 28
    • 0021362952 scopus 로고
    • The periphery of the developing collagen fibril
    • Scott J.E. The periphery of the developing collagen fibril. Biochem. J. 195:1984;229-233.
    • (1984) Biochem. J. , vol.195 , pp. 229-233
    • Scott, J.E.1
  • 29
    • 0016360365 scopus 로고
    • Biosynthesis of collagen crosslinks: Increased activity of purified lysyl oxidase with reconstituted fibrils
    • Siegel R.C. Biosynthesis of collagen crosslinks: increased activity of purified lysyl oxidase with reconstituted fibrils. Proc. Natl. Acad. Sci. USA. 71:1974;4826-4830.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4826-4830
    • Siegel, R.C.1
  • 30
    • 0028047893 scopus 로고
    • Native collagen fibrils from echinoderms are molecularly bipolar
    • Thurmond F.A., Trotter J.A. Native collagen fibrils from echinoderms are molecularly bipolar. J. Mol. Biol. 235:1994;73-79.
    • (1994) J. Mol. Biol. , vol.235 , pp. 73-79
    • Thurmond, F.A.1    Trotter, J.A.2
  • 31
    • 0011886102 scopus 로고    scopus 로고
    • Collagen fibrillogenesis: Intermediate aggregates and suprafibrillar order
    • Trelstad R.L., Hayashi K., Gross J. Collagen fibrillogenesis: intermediate aggregates and suprafibrillar order. Proc. Natl. Acad. Sci. USA. 73:1996;4027-4031.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4027-4031
    • Trelstad, R.L.1    Hayashi, K.2    Gross, J.3
  • 32
    • 0027972703 scopus 로고
    • Molecular structure and functional morphology of echinoderm collagen fibrils
    • Trogger J.A., Thurmond F.A., Koob T.J. Molecular structure and functional morphology of echinoderm collagen fibrils. Cell Tissue. Res. 275:1994;451-458.
    • (1994) Cell Tissue. Res. , vol.275 , pp. 451-458
    • Trogger, J.A.1    Thurmond, F.A.2    Koob, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.