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Volumn 122, Issue 1, 1997, Pages 109-115

Glycosylation of human bone collagen I in relation to lysylhydroxylation and fibril diameter

Author keywords

Bone; Collagen; Modification; Osteopenia

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 1; DEOXYPYRIDINOLINE; PYRIDINOLINE;

EID: 1842333330     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021717     Document Type: Article
Times cited : (38)

References (34)
  • 1
    • 0025719982 scopus 로고
    • Cytokines in context
    • Nathan, C. and Sporn, M. (1991) Cytokines in context. J. Cell Biol. 113, 981-986
    • (1991) J. Cell Biol. , vol.113 , pp. 981-986
    • Nathan, C.1    Sporn, M.2
  • 2
    • 0027222768 scopus 로고
    • Consensus development conference: Diagnosis, prophylaxis, and treatment of osteoporosis
    • Consensus development conference: diagnosis, prophylaxis, and treatment of osteoporosis (1993) Am. J. Med. 94, 646-650
    • (1993) Am. J. Med. , vol.94 , pp. 646-650
  • 3
    • 0026678191 scopus 로고
    • Compositional analysis of the collagenous bone matrix. A study on adult normal and osteopenic bone tissue
    • Bätge, B., Diebold, J., Stein, H., Bodo, M., and Müller, P.K. (1992) Compositional analysis of the collagenous bone matrix. A study on adult normal and osteopenic bone tissue. Eur. J. Clin. Invest. 22, 805-812
    • (1992) Eur. J. Clin. Invest. , vol.22 , pp. 805-812
    • Bätge, B.1    Diebold, J.2    Stein, H.3    Bodo, M.4    Müller, P.K.5
  • 4
    • 0026681853 scopus 로고
    • Post-translational modifications in the collagen of human osteoporotic femoral head
    • Bailey, A.J., Wotton, S.F., Sims, T.J., and Thompson, P.W. (1992) Post-translational modifications in the collagen of human osteoporotic femoral head. Biochem. Biophys. Res. Commun. 185, 801-805
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 801-805
    • Bailey, A.J.1    Wotton, S.F.2    Sims, T.J.3    Thompson, P.W.4
  • 5
    • 0029123770 scopus 로고
    • Biochemical changes in the collagenous matrix of osteoporotic avian bone
    • Knott, L., Whitehead, C.C., Fleming, R.H., and Bailey, A.J. (1995) Biochemical changes in the collagenous matrix of osteoporotic avian bone. Biochem. J. 310, 1045-1051
    • (1995) Biochem. J. , vol.310 , pp. 1045-1051
    • Knott, L.1    Whitehead, C.C.2    Fleming, R.H.3    Bailey, A.J.4
  • 7
    • 0027397099 scopus 로고
    • Fulvic acid supplementation and selenium deficiency disturb the structural integrity of mouse skeletal tissue. An animal model to study the molecular defects of Kashin-Beck disease
    • Yang, C., Niu, C., Bodo, M., Gabriel, E., Notbohm, H., Wolf, E., and Müller, P.K. (1993) Fulvic acid supplementation and selenium deficiency disturb the structural integrity of mouse skeletal tissue. An animal model to study the molecular defects of Kashin-Beck disease. Biochem. J. 289, 829-835
    • (1993) Biochem. J. , vol.289 , pp. 829-835
    • Yang, C.1    Niu, C.2    Bodo, M.3    Gabriel, E.4    Notbohm, H.5    Wolf, E.6    Müller, P.K.7
  • 8
    • 0029613827 scopus 로고
    • 1 influences lysylhydroxylation of collagen I and reduces steady-state levels of lysylhydroxylase mRNA in human osteoblast-like cells
    • 1 influences lysylhydroxylation of collagen I and reduces steady-state levels of lysylhydroxylase mRNA in human osteoblast-like cells. Eur. J. Clin. Invest. 25, 959-966
    • (1995) Eur. J. Clin. Invest. , vol.25 , pp. 959-966
    • Seitzer, U.1    Bätge, B.2    Acil, Y.3    Müller, P.K.4
  • 9
    • 0020509916 scopus 로고
    • Relationships between surface, volume, and thickness of iliac trabecular bone in aging and in osteoporosis. Implications for the microanatomic and cellular mechanisms of bone loss
    • Parfitt, A.M., Mathews, C.H., Villanueva, A.R., Kleerekoper, M., Frame, B., and Rao, D.S. (1983) Relationships between surface, volume, and thickness of iliac trabecular bone in aging and in osteoporosis. Implications for the microanatomic and cellular mechanisms of bone loss. J. Clin. Invest. 72, 1396-1409
    • (1983) J. Clin. Invest. , vol.72 , pp. 1396-1409
    • Parfitt, A.M.1    Mathews, C.H.2    Villanueva, A.R.3    Kleerekoper, M.4    Frame, B.5    Rao, D.S.6
  • 11
    • 0025182117 scopus 로고
    • A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95
    • Bätge, B., Notbohm, H., Diebold, J., Lehmann, H., Bodo, M., Deutzmann, R., and Müller, P.K. (1990) A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95. Eur. J. Biochem. 192, 153-159
    • (1990) Eur. J. Biochem. , vol.192 , pp. 153-159
    • Bätge, B.1    Notbohm, H.2    Diebold, J.3    Lehmann, H.4    Bodo, M.5    Deutzmann, R.6    Müller, P.K.7
  • 12
    • 0022510760 scopus 로고
    • Rapid fractionation of collagen chains and peptides by high-performance liquid chromatography
    • Bateman, J.F., Mascara, T., Chan, D., and Cole, W.G. (1986) Rapid fractionation of collagen chains and peptides by high-performance liquid chromatography. Ann. Biochem. 154, 338-344
    • (1986) Ann. Biochem. , vol.154 , pp. 338-344
    • Bateman, J.F.1    Mascara, T.2    Chan, D.3    Cole, W.G.4
  • 13
    • 0021136055 scopus 로고
    • Hydroxylysine glycosides: Preparation and analysis by reverse phase high performance liquid chromatography
    • Tenni, R., Rimoldi, D., Zanaboni, G., Cetta, G., and Castellani, A. A. (1984) Hydroxylysine glycosides: preparation and analysis by reverse phase high performance liquid chromatography. Ital. J. Biochem. 33, 117-127
    • (1984) Ital. J. Biochem. , vol.33 , pp. 117-127
    • Tenni, R.1    Rimoldi, D.2    Zanaboni, G.3    Cetta, G.4    Castellani, A.A.5
  • 14
    • 0028349129 scopus 로고
    • A rapid method for the isolation of the mature collagen cross-links hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP)
    • Acil, Y. and Müller, P.K. (1994) A rapid method for the isolation of the mature collagen cross-links hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP). J. Chromatogr. A664, 183-188
    • (1994) J. Chromatogr. , vol.A664 , pp. 183-188
    • Acil, Y.1    Müller, P.K.2
  • 15
    • 1842335940 scopus 로고
    • (Sachs, L., ed.) Springer Verlag, Berlin/Heidelberg
    • Sachs, L. (1992) in Angewandte Statistik (Sachs, L., ed.) pp. 245-248, Springer Verlag, Berlin/Heidelberg
    • (1992) Angewandte Statistik , pp. 245-248
    • Sachs, L.1
  • 16
    • 0028787166 scopus 로고
    • Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1 chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate cristalline hydroxyapatite
    • Culbert, A.A., Lowe, M., Atkinson, M., Byers, P., Wallis, A., and Kadler, K.E. (1995) Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1 chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate cristalline hydroxyapatite. Biochem. J. 311, 815-820
    • (1995) Biochem. J. , vol.311 , pp. 815-820
    • Culbert, A.A.1    Lowe, M.2    Atkinson, M.3    Byers, P.4    Wallis, A.5    Kadler, K.E.6
  • 18
    • 0023394028 scopus 로고
    • Polar-apolar characteristics and fibrillogenesis of glycosylated collagen
    • Amudeswari, S., Liang, J.N., and Chakrabarti, B. (1987) Polar-apolar characteristics and fibrillogenesis of glycosylated collagen. Collagen Relat. Res. 7, 215-223
    • (1987) Collagen Relat. Res. , vol.7 , pp. 215-223
    • Amudeswari, S.1    Liang, J.N.2    Chakrabarti, B.3
  • 19
    • 0026630061 scopus 로고
    • Copolymerization of normal type I collagen with three mutated type I collagens containing substitutions of cysteine at different glycine positions in the alpha 1 (I) chain
    • Torre Blanco, A., Adachi, E., Romanic, A.M., and Prockop, D.J. (1992) Copolymerization of normal type I collagen with three mutated type I collagens containing substitutions of cysteine at different glycine positions in the alpha 1 (I) chain. J. Biol. Chem. 267, 4968-4973
    • (1992) J. Biol. Chem. , vol.267 , pp. 4968-4973
    • Torre Blanco, A.1    Adachi, E.2    Romanic, A.M.3    Prockop, D.J.4
  • 21
    • 0019417315 scopus 로고
    • Disorder of collagen metabolism in a patient with osteogenesis imperfecta (lethal type): Increased degree of hydroxylation of lysine in collagen types I and III
    • Kirsch, E., Krieg, T., Remberger, K., Fendel, H., Bruckner, P., and Müller, P.K. (1981) Disorder of collagen metabolism in a patient with osteogenesis imperfecta (lethal type): increased degree of hydroxylation of lysine in collagen types I and III. Eur. J. Clin. Invest. 11, 39-47
    • (1981) Eur. J. Clin. Invest. , vol.11 , pp. 39-47
    • Kirsch, E.1    Krieg, T.2    Remberger, K.3    Fendel, H.4    Bruckner, P.5    Müller, P.K.6
  • 22
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • (Harding, J.J. and Crabbe, M.J.C., eds.) CRC Press, Boca Raton/Ann Arbor/London
    • Kivirikko, K.I., Myllylä, R., and Pihlajaniemi, T. (1992) Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins in Post-translational Modifications of Proteins (Harding, J.J. and Crabbe, M.J.C., eds.) pp. 53-104, CRC Press, Boca Raton/Ann Arbor/London
    • (1992) Post-translational Modifications of Proteins , pp. 53-104
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 24
    • 0024467522 scopus 로고
    • Biochemical analysis of callus tissue in osteogenesis imperfecta type IV. Evidence for transient overmodification in collagen types I and III
    • Brenner, R.E., Vetter, U., Nerlich, A., Wörsdorfer, O., Teller, W.M., and Müller, P.K. (1989) Biochemical analysis of callus tissue in osteogenesis imperfecta type IV. Evidence for transient overmodification in collagen types I and III. J. Clin. Invest. 84, 915-921
    • (1989) J. Clin. Invest. , vol.84 , pp. 915-921
    • Brenner, R.E.1    Vetter, U.2    Nerlich, A.3    Wörsdorfer, O.4    Teller, W.M.5    Müller, P.K.6
  • 25
    • 0029145151 scopus 로고
    • Microcallus formations of the cancellous bone: A quantitative analysis of the human spine
    • Hahn, M., Vogel, M., Amling, M., Ritzel, H., and Delling, G. (1995) Microcallus formations of the cancellous bone: a quantitative analysis of the human spine. J. Bone. Miner. Res. 10, 1410-1416
    • (1995) J. Bone. Miner. Res. , vol.10 , pp. 1410-1416
    • Hahn, M.1    Vogel, M.2    Amling, M.3    Ritzel, H.4    Delling, G.5
  • 27
    • 0003650943 scopus 로고
    • (Piez, K. and Reddi, A., eds.) Elsevier, New York
    • Miller, E.J. (1984) in Extracellular Matrix Biochemistry (Piez, K. and Reddi, A., eds.) pp. 83-118, Elsevier, New York
    • (1984) Extracellular Matrix Biochemistry , pp. 83-118
    • Miller, E.J.1
  • 28
    • 9344224950 scopus 로고
    • Pyridinium-Quervernetzungen im Knochengewebe: Vergleich mit Kollagenmodifikation und Morphometrie
    • Bätge, B., Acil, Y., Schlatterer, A., Seitzer, U., and Müller, P.K. (1994) Pyridinium-Quervernetzungen im Knochengewebe: Vergleich mit Kollagenmodifikation und Morphometrie. Osteologie 3, 119-124
    • (1994) Osteologie , vol.3 , pp. 119-124
    • Bätge, B.1    Acil, Y.2    Schlatterer, A.3    Seitzer, U.4    Müller, P.K.5
  • 29
    • 0028272120 scopus 로고
    • Urinary pyridinium cross-links: A noninvasive diagnostic test for Ehlers-Danlos syndrome type VI
    • Pasquali, M., Dembure, P., Still, M., and Elsas, L.J. (1994) Urinary pyridinium cross-links: a noninvasive diagnostic test for Ehlers-Danlos syndrome type VI. N. Engl. J. Med. 331, 132-133
    • (1994) N. Engl. J. Med. , vol.331 , pp. 132-133
    • Pasquali, M.1    Dembure, P.2    Still, M.3    Elsas, L.J.4
  • 30
    • 0027394821 scopus 로고
    • Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta
    • Vetter, U., Weis, M.A., Morike, M., Eanes, E.D., and Eyre, D.R. (1993) Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta. J. Bone. Miner. Res. 8, 133-137
    • (1993) J. Bone. Miner. Res. , vol.8 , pp. 133-137
    • Vetter, U.1    Weis, M.A.2    Morike, M.3    Eanes, E.D.4    Eyre, D.R.5
  • 31
    • 0022249249 scopus 로고
    • Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen
    • Royce, P.M. and Barnes, M.J. (1985) Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen. Biochem. J. 230, 475-480
    • (1985) Biochem. J. , vol.230 , pp. 475-480
    • Royce, P.M.1    Barnes, M.J.2
  • 32
    • 0027241887 scopus 로고
    • Collagen II from articular cartilage and annulus fibrosus. Structural and functional implication of tissue specific posttranslational modifications of collagen molecules
    • Yang, C.L., Rui, H., Mosler, S., Notbohm, H., Sawaryn, A., and Müller, P.K. (1993) Collagen II from articular cartilage and annulus fibrosus. Structural and functional implication of tissue specific posttranslational modifications of collagen molecules. Eur. J. Biochem. 213, 1297-1302
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1297-1302
    • Yang, C.L.1    Rui, H.2    Mosler, S.3    Notbohm, H.4    Sawaryn, A.5    Müller, P.K.6
  • 33
    • 0027355492 scopus 로고
    • Biochemical changes in the collagen of human osteoporotic bone matrix
    • Bailey, A.J., Wotton, S.F., Sims, T.J., and Thompson, P.W. (1993) Biochemical changes in the collagen of human osteoporotic bone matrix. Connect. Tissue Res. 29, 119-132
    • (1993) Connect. Tissue Res. , vol.29 , pp. 119-132
    • Bailey, A.J.1    Wotton, S.F.2    Sims, T.J.3    Thompson, P.W.4
  • 34
    • 0025343595 scopus 로고
    • Collagen fibrillogenesis in vitro: Interaction of types I and V collagen regulates fibril diameter
    • Birk, D.E., Fitch, J.M., Babiarz, J.P., Doane, K.J., and Linsenmayer, T.F. (1990) Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter. J. Cell Sci. 95, 649-657
    • (1990) J. Cell Sci. , vol.95 , pp. 649-657
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.P.3    Doane, K.J.4    Linsenmayer, T.F.5


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