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Volumn 38, Issue 5, 2007, Pages 513-521

Influence of saline and pH on collagen type I fibrillogenesis in vitro: Fibril polymorphism and colloidal gold labelling

Author keywords

Collgen type I; Gold labelling; In vitro fibrillogenesis; Negative staining; Polymorphic forms

Indexed keywords

ACETIC ACID; COLLOIDS; GOLD; MOLECULAR ORIENTATION; PH EFFECTS; SODIUM CHLORIDE; TRANSMISSION ELECTRON MICROSCOPY;

EID: 33947101363     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2006.07.026     Document Type: Article
Times cited : (80)

References (41)
  • 1
    • 0028923480 scopus 로고
    • Collagen fibrillogenesis in situ: fibril segments undergo post-depositational modifications resulting in linear and lateral growth during matrix development
    • Birk D.E., Nurminskaya M.V., and Zycband E.I. Collagen fibrillogenesis in situ: fibril segments undergo post-depositational modifications resulting in linear and lateral growth during matrix development. Develop. Dyn. 202 (1995) 229-243
    • (1995) Develop. Dyn. , vol.202 , pp. 229-243
    • Birk, D.E.1    Nurminskaya, M.V.2    Zycband, E.I.3
  • 2
    • 2542553125 scopus 로고
    • Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly
    • Birk D.E., Zycband E.I., Winkelmann D.A., and Trelstad R.L. Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 4549-4553
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4549-4553
    • Birk, D.E.1    Zycband, E.I.2    Winkelmann, D.A.3    Trelstad, R.L.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., Winklemann D.A., and Trelstad R.L. Collagen fibrillogenesis in situ: fibril segments become long fibrils as the developing tendon matures. Develop. Dyn. 208 (1997) 291-298
    • (1997) Develop. Dyn. , vol.208 , pp. 291-298
    • Birk, D.E.1    Zycband, E.I.2    Woodruff, S.3    Winklemann, D.A.4    Trelstad, R.L.5
  • 4
    • 0017276132 scopus 로고
    • Supramolecular structure of polymorphic collagen fibrils
    • Bruns R.R. Supramolecular structure of polymorphic collagen fibrils. J. Cell Biol. 68 (1976) 521-538
    • (1976) J. Cell Biol. , vol.68 , pp. 521-538
    • Bruns, R.R.1
  • 5
    • 0007152183 scopus 로고
    • Procollagen segment-long-spacing crystallites: their role in collagen fibrillogenesis
    • Bruns R.R., Hulmes D.J.S., Therrien S.F., and Gross J. Procollagen segment-long-spacing crystallites: their role in collagen fibrillogenesis. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 313-317
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 313-317
    • Bruns, R.R.1    Hulmes, D.J.S.2    Therrien, S.F.3    Gross, J.4
  • 6
    • 11144241634 scopus 로고    scopus 로고
    • Noble-metal nanoparticles directly conjugated to globular proteins
    • Burt J.L., Gutierrez-Wing C., Miki-Yoshida M., and Jose-Yacaman M. Noble-metal nanoparticles directly conjugated to globular proteins. Langmuir 20 (2004) 11778-11783
    • (2004) Langmuir , vol.20 , pp. 11778-11783
    • Burt, J.L.1    Gutierrez-Wing, C.2    Miki-Yoshida, M.3    Jose-Yacaman, M.4
  • 7
    • 17844373840 scopus 로고    scopus 로고
    • Procollalglen trafficking, processing and fibrillogenesis
    • Canty E.G., and Kadler K.E. Procollalglen trafficking, processing and fibrillogenesis. J. Cell Sci. 118 (2005) 1341-1353
    • (2005) J. Cell Sci. , vol.118 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 8
    • 0028278071 scopus 로고
    • Clustering of fibronectin adhesins toward Treponema denticola tipsupon contact with immobilized fibronectin
    • Dawson J.R., and Ellen R.P. Clustering of fibronectin adhesins toward Treponema denticola tipsupon contact with immobilized fibronectin. Infect. Immun. 62 (1994) 2214-2221
    • (1994) Infect. Immun. , vol.62 , pp. 2214-2221
    • Dawson, J.R.1    Ellen, R.P.2
  • 9
    • 21444454716 scopus 로고    scopus 로고
    • Collagen-silica hybrid materials: sodium silicate and sodium chloride effects on type I collagen fibrillogenesis
    • Eglin D., Coradin T., Guille M.M.G., Helary C., and Livage J. Collagen-silica hybrid materials: sodium silicate and sodium chloride effects on type I collagen fibrillogenesis. Biomed. Mater. Eng. 15 (2005) 43-50
    • (2005) Biomed. Mater. Eng. , vol.15 , pp. 43-50
    • Eglin, D.1    Coradin, T.2    Guille, M.M.G.3    Helary, C.4    Livage, J.5
  • 10
    • 0016804150 scopus 로고
    • Oblique banding pattern in collagen fibrils reconstituted in vitro after trypsin treatment
    • Ghosh S.K., and Mitra H.P. Oblique banding pattern in collagen fibrils reconstituted in vitro after trypsin treatment. Biochim. Biophys. Acta 405 (1975) 340-346
    • (1975) Biochim. Biophys. Acta , vol.405 , pp. 340-346
    • Ghosh, S.K.1    Mitra, H.P.2
  • 11
    • 28544442717 scopus 로고    scopus 로고
    • Bone matrix like assemblies of collagen: from liquid crystals to gels and biomimetic materials
    • Giraud Guille M.M., Mosser G., Helary C., and Eglin E. Bone matrix like assemblies of collagen: from liquid crystals to gels and biomimetic materials. Micron 36 (2005) 602-608
    • (2005) Micron , vol.36 , pp. 602-608
    • Giraud Guille, M.M.1    Mosser, G.2    Helary, C.3    Eglin, E.4
  • 12
    • 0034723148 scopus 로고    scopus 로고
    • Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction
    • Graham H.K., Holmes D.F., Watson R.B., and Kadler K.E. Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on 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
  • 13
    • 0035059735 scopus 로고    scopus 로고
    • Sequestration of aggregated LDL by macrophages studied with freeze-etch electron microscopy
    • Haberland M.E., Mottino G., Le M., and Frank J.S. Sequestration of aggregated LDL by macrophages studied with freeze-etch electron microscopy. J. Lipid Res. 42 (2001) 605-619
    • (2001) J. Lipid Res. , vol.42 , pp. 605-619
    • Haberland, M.E.1    Mottino, G.2    Le, M.3    Frank, J.S.4
  • 15
    • 0001439498 scopus 로고
    • Negative staining
    • Harris J.R. (Ed), IRL Press at Oxford University Press, Oxford
    • Harris J.R., and Horne R.W. Negative staining. In: Harris J.R. (Ed). Electron Microscopy: A Practical Approach (1991), IRL Press at Oxford University Press, Oxford 203-228
    • (1991) Electron Microscopy: A Practical Approach , pp. 203-228
    • Harris, J.R.1    Horne, R.W.2
  • 16
    • 20144384111 scopus 로고    scopus 로고
    • Molybdenum blue: binding to collagen fibres and microcrystal formation
    • Harris J.R., Reiber A., Therese H.A., and Tremel W. Molybdenum blue: binding to collagen fibres and microcrystal formation. Micron 36 (2005) 387-391
    • (2005) Micron , vol.36 , pp. 387-391
    • Harris, J.R.1    Reiber, A.2    Therese, H.A.3    Tremel, W.4
  • 17
    • 0026756620 scopus 로고
    • Growing tips of type I collagen fibrils formed in vitro are near-parabolic in shape, implying a reciprocal relationship between accretion and diameter
    • Holmes D.F., Chapman J.A., Prockop D.J., and Kadler K.E. Growing tips of type I collagen fibrils formed in vitro are near-parabolic in shape, implying a reciprocal relationship between accretion and diameter. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 9855-9859
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9855-9859
    • Holmes, D.F.1    Chapman, J.A.2    Prockop, D.J.3    Kadler, K.E.4
  • 19
    • 33947147481 scopus 로고    scopus 로고
    • Collagen fibril assembly in vitro
    • Harris J.R., Graham J., and Rickwood D. (Eds), John Wiley and Sons Ltd., Chichester
    • Holmes D.F., and Kadler K.E. Collagen fibril assembly in vitro. In: Harris J.R., Graham J., and Rickwood D. (Eds). Cell Biology Protocols (2006), John Wiley and Sons Ltd., Chichester 375-378
    • (2006) Cell Biology Protocols , pp. 375-378
    • Holmes, D.F.1    Kadler, K.E.2
  • 20
  • 22
    • 0010570561 scopus 로고    scopus 로고
    • Structural relations between collagen and mineral in bone as determined by high voltage electron microscopic tomography
    • Landis W.J., Hodgens K.J., Arena J., Song M.J., and McEwan B.F. Structural relations between collagen and mineral in bone as determined by high voltage electron microscopic tomography. Microsc. Res. Tech. 33 (1996) 192-202
    • (1996) Microsc. Res. Tech. , vol.33 , pp. 192-202
    • Landis, W.J.1    Hodgens, K.J.2    Arena, J.3    Song, M.J.4    McEwan, B.F.5
  • 23
    • 10644251951 scopus 로고    scopus 로고
    • Recruitment of multiple cell lines by collagen-synthetic copolymer matrices in corneal regeneration
    • Li F., Griffith M., Li Z., Tanodekaew S., Sheardown H., Hakim M., and Carlsson D.J. Recruitment of multiple cell lines by collagen-synthetic copolymer matrices in corneal regeneration. Biomaterials 26 (2005) 3093-3104
    • (2005) Biomaterials , vol.26 , pp. 3093-3104
    • Li, F.1    Griffith, M.2    Li, Z.3    Tanodekaew, S.4    Sheardown, H.5    Hakim, M.6    Carlsson, D.J.7
  • 24
    • 4244164513 scopus 로고
    • Relation of ionising groups to the structure of the collagen fibril
    • Martin G.R., Mergenhagen S.E., and Scott D.B. Relation of ionising groups to the structure of the collagen fibril. Biochim. Biophys. Acta 49 (1961) 245-250
    • (1961) Biochim. Biophys. Acta , vol.49 , pp. 245-250
    • Martin, G.R.1    Mergenhagen, S.E.2    Scott, D.B.3
  • 26
    • 0035218932 scopus 로고    scopus 로고
    • Collagen structure and functional implications
    • Ottani V., Raspanti M., and Ruggeri A. Collagen structure and functional implications. Micron 32 (2001) 251-260
    • (2001) Micron , vol.32 , pp. 251-260
    • Ottani, V.1    Raspanti, M.2    Ruggeri, A.3
  • 27
    • 0031049878 scopus 로고    scopus 로고
    • Two distinct mechanisms regulate luteovirus transmission efficiency and specificity at the aphid salivary gland
    • Peiffer M.L., Gidlow F.E., and Gray S.M. Two distinct mechanisms regulate luteovirus transmission efficiency and specificity at the aphid salivary gland. J. Gen. Virol. 78 (1997) 495-503
    • (1997) J. Gen. Virol. , vol.78 , pp. 495-503
    • Peiffer, M.L.1    Gidlow, F.E.2    Gray, S.M.3
  • 28
    • 33947144987 scopus 로고    scopus 로고
    • Reiber, A., Harris, J.R., Conrad, J., Markl, J., Tremel, W., Wegner, G., 2007. Nanowires obtained by metallization of type I collagen fibres. Micron, submitted for publication.
  • 29
    • 0037416907 scopus 로고    scopus 로고
    • Biologically inspired growth of hydroxyapatite nanocrystals inside self-assembled collagen fibres
    • Roveri N., Falmi G., Sidoti M.C., Tampieri A., Landi E., Sandri M., and Parma B. Biologically inspired growth of hydroxyapatite nanocrystals inside self-assembled collagen fibres. Mater. Sci. Eng. C 23 (2003) 441-446
    • (2003) Mater. Sci. Eng. C , vol.23 , pp. 441-446
    • Roveri, N.1    Falmi, G.2    Sidoti, M.C.3    Tampieri, A.4    Landi, E.5    Sandri, M.6    Parma, B.7
  • 30
    • 0345868864 scopus 로고    scopus 로고
    • Mineralization behaviour of collagen type OI immobilized on different substrates
    • Scharnweber D., Born R., Flade K., Roessler S., Stoelzel M., and Worch H. Mineralization behaviour of collagen type OI immobilized on different substrates. Biomaterials 25 (2004) 2371-2380
    • (2004) Biomaterials , vol.25 , pp. 2371-2380
    • Scharnweber, D.1    Born, R.2    Flade, K.3    Roessler, S.4    Stoelzel, M.5    Worch, H.6
  • 31
    • 0141453852 scopus 로고    scopus 로고
    • Collagen self-assembly and the development of tendon mechanical properties
    • Silver F.H., Freeman J.W., and Seehra G.P. Collagen self-assembly and the development of tendon mechanical properties. J. Biomech. 36 (2003) 1529-1553
    • (2003) J. Biomech. , vol.36 , pp. 1529-1553
    • Silver, F.H.1    Freeman, J.W.2    Seehra, G.P.3
  • 32
    • 0030974903 scopus 로고    scopus 로고
    • Use of gold-labeled ovalbumin to correlate antigen deposition and localization with tissue response
    • Tengowski M.W., Bjorlilng D.E., Albrecht R.M., and Saban R. Use of gold-labeled ovalbumin to correlate antigen deposition and localization with tissue response. J. Pharmacol. Toxicol. Meth. 37 (1997) 15-21
    • (1997) J. Pharmacol. Toxicol. Meth. , vol.37 , pp. 15-21
    • Tengowski, M.W.1    Bjorlilng, D.E.2    Albrecht, R.M.3    Saban, R.4
  • 34
    • 0011886102 scopus 로고
    • Collagen fibrillogenesis: intermediate aggregates and suprafibrillar order
    • Trelstad R.L., Hayashi K., and Gross J. Collagen fibrillogenesis: intermediate aggregates and suprafibrillar order. Proc. Natl. Acad. Sci. U.S.A. 73 (1976) 4027-4031
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 4027-4031
    • Trelstad, R.L.1    Hayashi, K.2    Gross, J.3
  • 35
    • 0019956379 scopus 로고
    • A study of positive staining for electron microscopykusing collagen as a model system. II. Staining by uranyl ions
    • Tzaphlidou M., Chapman J.A., and Al-Samman M.H. A study of positive staining for electron microscopykusing collagen as a model system. II. Staining by uranyl ions. Micron 13 (1982) 133-145
    • (1982) Micron , vol.13 , pp. 133-145
    • Tzaphlidou, M.1    Chapman, J.A.2    Al-Samman, M.H.3
  • 36
    • 0036013790 scopus 로고    scopus 로고
    • Electron microscopic determination of silver incorporation in collagen fibres as a model of organic-metal chiral supramolecular structure with optical anisotropic properties
    • Vidal B.D.C., and Joazeiro P. Electron microscopic determination of silver incorporation in collagen fibres as a model of organic-metal chiral supramolecular structure with optical anisotropic properties. Micron 33 (2002) 507-509
    • (2002) Micron , vol.33 , pp. 507-509
    • Vidal, B.D.C.1    Joazeiro, P.2
  • 37
    • 0016789527 scopus 로고
    • Anisotropic properties of silver plus gold-impregnated collagen bundles: ADB and form birefringence curves
    • Vidal B.C., Mello M.L., Godo C., Casiero A.C., and Abujadi J.M. Anisotropic properties of silver plus gold-impregnated collagen bundles: ADB and form birefringence curves. Ann. Histochem. 20 (1975) 15-26
    • (1975) Ann. Histochem. , vol.20 , pp. 15-26
    • Vidal, B.C.1    Mello, M.L.2    Godo, C.3    Casiero, A.C.4    Abujadi, J.M.5
  • 38
    • 17444374661 scopus 로고    scopus 로고
    • Collagen fibril form and function
    • Wess T.J. Collagen fibril form and function. Adv. Protein Chem. 70 (2005) 341-374
    • (2005) Adv. Protein Chem. , vol.70 , pp. 341-374
    • Wess, T.J.1
  • 40
    • 10444269418 scopus 로고    scopus 로고
    • Aspects of collagen mineralization in hard tissue formation
    • Wiesmann H.P., Meyer U., Plate U., and Höhling H.J. Aspects of collagen mineralization in hard tissue formation. Int. Rev. Cytol. 242 (2004) 121-156
    • (2004) Int. Rev. Cytol. , vol.242 , pp. 121-156
    • Wiesmann, H.P.1    Meyer, U.2    Plate, U.3    Höhling, H.J.4


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