메뉴 건너뛰기




Volumn 19, Issue 4, 2000, Pages 359-365

Tip-mediated fusion involving unipolar collagen fibrils accounts for rapid fibril elongation, the occurrence of fibrillar branched networks in skin and the paucity of collagen fibril ends in vertebrates

Author keywords

Bipolar; Collagen; Electron microscopy; Fibrils; Proteoglycan; Unipolar

Indexed keywords

COLLAGEN FIBRIL; PROCOLLAGEN; PROTEOGLYCAN;

EID: 0034253758     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(00)00082-2     Document Type: Short Survey
Times cited : (63)

References (30)
  • 1
    • 0028923480 scopus 로고
    • Collagen fibrillogenesis in-situ - fibril segments undergo postdepositional 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 postdepositional modifications resulting in linear and lateral growth during matrix development. Dev. Dyn. 202:1995;229-243.
    • (1995) Dev. Dyn. , vol.202 , pp. 229-243
    • Birk, D.E.1    Nurminskaya, M.V.2    Zycband, E.I.3
  • 2
    • 0030198753 scopus 로고    scopus 로고
    • Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon
    • Birk D.E., Hahn R.A., Linsenmayer C.Y., Zycband E.I. Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon. Matrix Biol. 15:1996;111-118.
    • (1996) Matrix Biol. , vol.15 , pp. 111-118
    • Birk, D.E.1    Hahn, R.A.2    Linsenmayer, C.Y.3    Zycband, E.I.4
  • 3
    • 0031042279 scopus 로고    scopus 로고
    • Collagen fibrillogenesis in situ: Fibril segments become long fibrils as the developing tendon matures
    • Birk D.E., Zycband E.I., Woodruff S., Winkelmann D.A., Trelstad R.L. Collagen fibrillogenesis in situ: fibril segments become long fibrils as the developing tendon matures. Dev. Dyn. 208:1997;291-298.
    • (1997) Dev. Dyn. , vol.208 , pp. 291-298
    • Birk, D.E.1    Zycband, E.I.2    Woodruff, S.3    Winkelmann, D.A.4    Trelstad, R.L.5
  • 4
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: Skin fragility and corneal opacity in the absence of lumican
    • Chakravarti S., Magnuson T., Lass J.H., Jepsen K.J., LaMantia C., Carroll H. Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J. Cell Biol. 141:1998;1277-1286.
    • (1998) J. Cell Biol. , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnuson, T.2    Lass, J.H.3    Jepsen, K.J.4    Lamantia, C.5    Carroll, H.6
  • 5
    • 0024412103 scopus 로고
    • The regulation of size and form in the assembly of collagen fibrils in vivo
    • addition 28: 2201-2205
    • Chapman J.A. The regulation of size and form in the assembly of collagen fibrils in vivo. Biopolymer. 28:1989;1367-1382. addition 28: 2201-2205.
    • (1989) Biopolymer , vol.28 , pp. 1367-1382
    • Chapman, J.A.1
  • 6
    • 0029067409 scopus 로고
    • Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen
    • Colige A., Beschin A., Samyn B. et al. Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen. J. Biol. Chem. 270:1995;16724-16730.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16724-16730
    • Colige, A.1    Beschin, A.2    Samyn, B.3
  • 7
    • 0030959540 scopus 로고    scopus 로고
    • CDNA cloning and expression of bovine procollagen N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige A., Li S.-W., Sieron A., Nusgens B.V., Prockop D.J., Lapiere C.M. cDNA cloning and expression of bovine procollagen N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc. Natl. Acad. Sci. USA. 94:1997;2374-2379.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.-W.2    Sieron, A.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 8
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson K.G., Baribault H., Holmes D.F., Graham H., Kadler K.E., Iozzo R.V. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 136:1997;729-743.
    • (1997) J. Cell Biol. , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 9
    • 0034723148 scopus 로고    scopus 로고
    • Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on molecular recognition sequences in unipolar fibrils and is regulated by collagen-proteoglycan interaction
    • Graham H.K., Holmes D.F., Watson R.B., Kadler K.E. Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on molecular recognition sequences in unipolar fibrils and is regulated by collagen-proteoglycan interaction. J. Mol. Biol. 295:2000;891-902.
    • (2000) J. Mol. Biol. , vol.295 , pp. 891-902
    • Graham, H.K.1    Holmes, D.F.2    Watson, R.B.3    Kadler, K.E.4
  • 10
    • 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. PNAS (USA). 89:1992;9855-9859.
    • (1992) PNAS (USA) , vol.89 , pp. 9855-9859
    • Holmes, D.F.1    Chapman, J.A.2    Prockop, D.J.3    Kadler, K.E.4
  • 11
    • 0027291184 scopus 로고
    • Ehlers Danlos syndrome type VIIB. Morphology of type I collagen fibrils is determined by the conformation of the N-propeptide
    • Holmes D.F., Watson R.B., Steinmann B., Kadler K.E. Ehlers Danlos syndrome type VIIB. Morphology of type I collagen fibrils is determined by the conformation of the N-propeptide. J. Biol. Chem. 268:1993;15758-15765.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15758-15765
    • Holmes, D.F.1    Watson, R.B.2    Steinmann, B.3    Kadler, K.E.4
  • 12
    • 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
  • 14
    • 0032515195 scopus 로고    scopus 로고
    • Collagen fibrils forming in developing tendon show an early and abrupt limitation in diameter at the growing tips unobserved in cell-free systems
    • Holmes D.F., Graham H.K., Kadler K.E. Collagen fibrils forming in developing tendon show an early and abrupt limitation in diameter at the growing tips unobserved in cell-free systems. J. Mol. Biol. 283:1998;1049-1058.
    • (1998) J. Mol. Biol. , vol.283 , pp. 1049-1058
    • Holmes, D.F.1    Graham, H.K.2    Kadler, K.E.3
  • 15
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans - Functional network of interactive proteins
    • Iozzo R.V. The biology of the small leucine-rich proteoglycans - Functional network of interactive proteins. J. Biol. Chem. 274:1999;18843-18846.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18843-18846
    • Iozzo, R.V.1
  • 16
    • 0029041275 scopus 로고
    • Procollagen C-peptidase: Procollagen C-proteinase
    • Kadler K.E., Watson R.B. Procollagen C-peptidase: procollagen C-proteinase. Methods Enzymol. 248:1995;771-781.
    • (1995) Methods Enzymol. , vol.248 , pp. 771-781
    • Kadler, K.E.1    Watson, R.B.2
  • 17
    • 0023656926 scopus 로고
    • Assembly of collagen fibrils de novo by enzymic cleavage of the type I pCcollagen by procollagen C-proteinase. Assay of critical concentration demonstrates that the process is an example of classical entropy-driven self assembly
    • Kadler K.E., Hojima Y., Prockop D.J. Assembly of collagen fibrils de novo by enzymic cleavage of the type I pCcollagen by procollagen C-proteinase. Assay of critical concentration demonstrates that the process is an example of classical entropy-driven self assembly. 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
    • 0023748662 scopus 로고
    • Assembly of collagen fibrils de novo. Between 37 and 41°C the process is limited by micro-unfolding of monomers
    • Kadler K.E., Hojima Y., Prockop D.J. Assembly of collagen fibrils de novo. Between 37 and 41°C the process is limited by micro-unfolding of monomers. J. Biol. Chem. 263:1988;10517-10523.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10517-10523
    • 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 pCcollagen. The fibrils formed at about 37°C are similar in diameter, roundness and apparent flexibility to the collagen fibrils seen in connective tissue
    • R. Fleischmajer, B.R. Olsen, & K. Kühn.
    • Kadler K.E., Hulmes D.J.S., Hojima Y., Prockop D.J. Assembly of Type I collagen fibrils de novo by the specific enzymic cleavage of pCcollagen. The fibrils formed at about 37°C are similar in diameter, roundness and apparent flexibility to the collagen fibrils seen in connective tissue. Fleischmajer R., Olsen B.R., Kühn K. Structure, Molecular Biology and Pathology of Collagen, Annals of the New York Academy of Sciences, vol. 580. 1990;214-224.
    • (1990) Structure, Molecular Biology and Pathology of Collagen, Annals of the New York Academy of Sciences, Vol. 580 , pp. 214-224
    • Kadler, K.E.1    Hulmes, D.J.S.2    Hojima, Y.3    Prockop, D.J.4
  • 20
    • 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. 268:1990;339-343.
    • (1990) Biochem. J. , vol.268 , pp. 339-343
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 21
    • 0029022720 scopus 로고
    • Procollagen N-peptidases: Procollagen N-proteinases
    • Kadler K.E., Lightfoot S.J., Watson R.B. Procollagen N-peptidases: procollagen N-proteinases. Methods Enzymol. 248:1995;756-771.
    • (1995) Methods Enzymol , vol.248 , pp. 756-771
    • Kadler, K.E.1    Lightfoot, S.J.2    Watson, R.B.3
  • 24
    • 0029906315 scopus 로고    scopus 로고
    • The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenetic protein-1
    • Li S.-W., Sieron A.L., Fertala A., Hojima Y., Arnold W.V., Prockop D.J. The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenetic protein-1. PNAS (USA). 93:1996;5127-5130.
    • (1996) PNAS (USA) , vol.93 , pp. 5127-5130
    • Li, S.-W.1    Sieron, A.L.2    Fertala, A.3    Hojima, Y.4    Arnold, W.V.5    Prockop, D.J.6
  • 25
    • 0002458019 scopus 로고
    • Growth and development of collagen fibrils in connective tissue
    • A. Ruggeri, & P.M. Motta. Martinus Nijhoff Publishers
    • Parry D.A.D., Craig A.S. Growth and development of collagen fibrils in connective tissue. Ruggeri A., Motta P.M. Ultastructure of the connective tissue matrix. 1984;34-64 Martinus Nijhoff Publishers.
    • (1984) Ultastructure of the Connective Tissue Matrix , pp. 34-64
    • Parry, D.A.D.1    Craig, A.S.2
  • 26
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • Svensson L., Aszodi A., Reinholt F.P., Fässler R., Heinegard D., Oldberg A. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J. Biol. Chem. 274:1999;9636-9647.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fässler, R.4    Heinegard, D.5    Oldberg, A.6
  • 27
    • 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
  • 28
    • 0032545170 scopus 로고    scopus 로고
    • The collagen fibrils in sea cucumber dermis grow from two identical paraboloidal tips and have no constant diameter shaft regions
    • Trotter J.A., Chapman J.A., Kadler K.E., Holmes D.F. The collagen fibrils in sea cucumber dermis grow from two identical paraboloidal tips and have no constant diameter shaft regions. J. Mol. Biol. 284:1998;1417-1424.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1417-1424
    • Trotter, J.A.1    Chapman, J.A.2    Kadler, K.E.3    Holmes, D.F.4
  • 29
    • 0034647432 scopus 로고    scopus 로고
    • Echinoderm collagen fibrils grow by surface-nucleation-propagation from both centres and ends
    • in press
    • Trotter, J.A., Kadler, K.E., Holmes, D.F., 2000. Echinoderm collagen fibrils grow by surface-nucleation-propagation from both centres and ends. J. Mol. Biol., in press.
    • (2000) J. Mol. Biol.
    • Trotter, J.A.1    Kadler, K.E.2    Holmes, D.F.3
  • 30
    • 0033535331 scopus 로고    scopus 로고
    • Type IIA procollagen containing the cysteine-rich amino propeptide is deposited in the extracellular matrix of prechondrogenic tissue and binds to TGF-beta 1 and BMP-2
    • Zhu Y., Oganesian A., Keene D.R., Sandell L.J. Type IIA procollagen containing the cysteine-rich amino propeptide is deposited in the extracellular matrix of prechondrogenic tissue and binds to TGF-beta 1 and BMP-2. J. Cell Biol. 144:1999;1069-1080.
    • (1999) J. Cell Biol. , vol.144 , pp. 1069-1080
    • Zhu, Y.1    Oganesian, A.2    Keene, D.R.3    Sandell, L.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.