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Volumn 10, Issue 6, 2014, Pages

Abnormal Type I Collagen Post-translational Modification and Crosslinking in a Cyclophilin B KO Mouse Model of Recessive Osteogenesis Imperfecta

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; CYCLOPHILIN B; CYCLOSPORIN A; PROCOLLAGEN LYSINE 2 OXOGLUTARATE 5 DIOXYGENASE; COLLAGEN; CYCLOPHILIN; GLYCOSYLATED COLLAGEN; MEMBRANE PROTEIN;

EID: 84903481605     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004465     Document Type: Article
Times cited : (101)

References (75)
  • 1
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J, Kivirikko KI, (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20: 33-43.
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 2
    • 0032032089 scopus 로고    scopus 로고
    • Collagen cross-links in mineralizing tissues: a review of their chemistry, function, and clinical relevance
    • Knott L, Bailey AJ, (1998) Collagen cross-links in mineralizing tissues: a review of their chemistry, function, and clinical relevance. Bone 22: 181-187.
    • (1998) Bone , vol.22 , pp. 181-187
    • Knott, L.1    Bailey, A.J.2
  • 3
    • 33748854428 scopus 로고    scopus 로고
    • Collagen Cross-Links
    • In: Brinckmann J, Notbohm H, Muller PK, Eds. Berlin: Springer Berlin Heidelberg
    • Eyre DR, Wu J (2005) Collagen Cross-Links. In: Brinckmann J, Notbohm H, Muller PK, Eds. Collagen: Primer in Structure, Processing and Assembly. Berlin: Springer Berlin Heidelberg. pp. 207-229.
    • (2005) Collagen: Primer in Structure, Processing and Assembly , pp. 207-229
    • Eyre, D.R.1    Wu, J.2
  • 4
    • 33847227672 scopus 로고    scopus 로고
    • Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans
    • Marini JC, Forlino A, Cabral WA, Barnes AM, San Antonio JD, et al. (2007) Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum Mutat 28: 209-221.
    • (2007) Hum Mutat , vol.28 , pp. 209-221
    • Marini, J.C.1    Forlino, A.2    Cabral, W.A.3    Barnes, A.M.4    San Antonio, J.D.5
  • 6
    • 34548240257 scopus 로고    scopus 로고
    • Components of the collagen prolyl 3-hydroxylation complex are crucial for normal bone development
    • Marini JC, Cabral WA, Barnes AM, Chang W, (2007) Components of the collagen prolyl 3-hydroxylation complex are crucial for normal bone development. Cell Cycle 6: 1675-1681.
    • (2007) Cell Cycle , vol.6 , pp. 1675-1681
    • Marini, J.C.1    Cabral, W.A.2    Barnes, A.M.3    Chang, W.4
  • 7
    • 2542497037 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
    • Vranka JA, Sakai LY, Bachinger HP, (2004) Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J Biol Chem 279: 23615-23621.
    • (2004) J Biol Chem , vol.279 , pp. 23615-23621
    • Vranka, J.A.1    Sakai, L.Y.2    Bachinger, H.P.3
  • 8
    • 33750207868 scopus 로고    scopus 로고
    • CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta
    • Morello R, Bertin TK, Chen Y, Hicks J, Tonachini L, et al. (2006) CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell 127: 291-304.
    • (2006) Cell , vol.127 , pp. 291-304
    • Morello, R.1    Bertin, T.K.2    Chen, Y.3    Hicks, J.4    Tonachini, L.5
  • 9
    • 67650522903 scopus 로고    scopus 로고
    • Biochemical characterization of the prolyl 3-hydroxylase 1/CRTAP/cyclophilin B complex
    • Ishikawa Y, Wirz J, Vranka JA, Nagata K, Bachinger HP, (2009) Biochemical characterization of the prolyl 3-hydroxylase 1/CRTAP/cyclophilin B complex. J Biol Chem 284: 17641-17647.
    • (2009) J Biol Chem , vol.284 , pp. 17641-17647
    • Ishikawa, Y.1    Wirz, J.2    Vranka, J.A.3    Nagata, K.4    Bachinger, H.P.5
  • 10
    • 33847321022 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta
    • Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, et al. (2007) Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat Genet 39: 359-365.
    • (2007) Nat Genet , vol.39 , pp. 359-365
    • Cabral, W.A.1    Chang, W.2    Barnes, A.M.3    Weis, M.4    Scott, M.A.5
  • 12
    • 77949442552 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex
    • Chang W, Barnes AM, Cabral WA, Bodurtha JN, Marini JC, (2009) Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex. Hum Mol Genet 19: 223-234.
    • (2009) Hum Mol Genet , vol.19 , pp. 223-234
    • Chang, W.1    Barnes, A.M.2    Cabral, W.A.3    Bodurtha, J.N.4    Marini, J.C.5
  • 13
    • 0141707715 scopus 로고    scopus 로고
    • Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions
    • Galat A, (2003) Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions. Curr Top Med Chem 3: 1315-1347.
    • (2003) Curr Top Med Chem , vol.3 , pp. 1315-1347
    • Galat, A.1
  • 14
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Gothel SF, Marahiel MA, (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol Life Sci 55: 423-436.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 15
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM, (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 17
    • 0025968746 scopus 로고
    • Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase
    • Steinmann B, Bruckner P, Superti-Furga A, (1991) Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. J Biol Chem 266: 1299-1303.
    • (1991) J Biol Chem , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 18
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization
    • Bachinger HP, Bruckner P, Timpl R, Prockop DJ, Engel J, (1980) Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur J Biochem 106: 619-632.
    • (1980) Eur J Biochem , vol.106 , pp. 619-632
    • Bachinger, H.P.1    Bruckner, P.2    Timpl, R.3    Prockop, D.J.4    Engel, J.5
  • 19
    • 76649130557 scopus 로고    scopus 로고
    • Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding
    • Barnes AM, Carter EM, Cabral WA, Weis M, Chang W, et al. (2010) Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N Engl J Med 362: 521-528.
    • (2010) N Engl J Med , vol.362 , pp. 521-528
    • Barnes, A.M.1    Carter, E.M.2    Cabral, W.A.3    Weis, M.4    Chang, W.5
  • 20
    • 79953087965 scopus 로고    scopus 로고
    • Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes
    • Pyott SM, Schwarze U, Christiansen HE, Pepin MG, Leistritz DF, et al. (2011) Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Hum Mol Genet 20: 1595-1609.
    • (2011) Hum Mol Genet , vol.20 , pp. 1595-1609
    • Pyott, S.M.1    Schwarze, U.2    Christiansen, H.E.3    Pepin, M.G.4    Leistritz, D.F.5
  • 21
    • 84862691109 scopus 로고    scopus 로고
    • Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding
    • Ishikawa Y, Vranka JA, Boudko SP, Pokidysheva E, Mizuno K, et al. (2012) Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin B-protein interactions and affects collagen folding. J Biol Chem 287: 22253-22265.
    • (2012) J Biol Chem , vol.287 , pp. 22253-22265
    • Ishikawa, Y.1    Vranka, J.A.2    Boudko, S.P.3    Pokidysheva, E.4    Mizuno, K.5
  • 22
    • 77952756514 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones
    • Vranka JA, Pokidysheva E, Hayashi L, Zientek K, Mizuno K, et al. (2010) Prolyl 3-hydroxylase 1 null mice display abnormalities in fibrillar collagen-rich tissues such as tendons, skin, and bones. J Biol Chem 285: 17253-17262.
    • (2010) J Biol Chem , vol.285 , pp. 17253-17262
    • Vranka, J.A.1    Pokidysheva, E.2    Hayashi, L.3    Zientek, K.4    Mizuno, K.5
  • 23
    • 33845866114 scopus 로고    scopus 로고
    • Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta
    • Barnes AM, Chang W, Morello R, Cabral WA, Weis M, et al. (2006) Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta. N Engl J Med 355: 2757-2764.
    • (2006) N Engl J Med , vol.355 , pp. 2757-2764
    • Barnes, A.M.1    Chang, W.2    Morello, R.3    Cabral, W.A.4    Weis, M.5
  • 24
    • 79953225159 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture
    • Sricholpech M, Perdivara I, Nagaoka H, Yokoyama M, Tomer KB, et al. (2011) Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture. J Biol Chem 286: 8846-8856.
    • (2011) J Biol Chem , vol.286 , pp. 8846-8856
    • Sricholpech, M.1    Perdivara, I.2    Nagaoka, H.3    Yokoyama, M.4    Tomer, K.B.5
  • 25
    • 84863328693 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance
    • Sricholpech M, Perdivara I, Yokoyama M, Nagaoka H, Terajima M, et al. (2012) Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance. J Biol Chem 287: 22998-23009.
    • (2012) J Biol Chem , vol.287 , pp. 22998-23009
    • Sricholpech, M.1    Perdivara, I.2    Yokoyama, M.3    Nagaoka, H.4    Terajima, M.5
  • 26
    • 59449103217 scopus 로고    scopus 로고
    • Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases
    • Schegg B, Hulsmeier AJ, Rutschmann C, Maag C, Hennet T, (2009) Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases. Mol Cell Biol 29: 943-952.
    • (2009) Mol Cell Biol , vol.29 , pp. 943-952
    • Schegg, B.1    Hulsmeier, A.J.2    Rutschmann, C.3    Maag, C.4    Hennet, T.5
  • 27
    • 0034680898 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity
    • Heikkinen J, Risteli M, Wang C, Latvala J, Rossi M, et al. (2000) Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J Biol Chem 275: 36158-36163.
    • (2000) J Biol Chem , vol.275 , pp. 36158-36163
    • Heikkinen, J.1    Risteli, M.2    Wang, C.3    Latvala, J.4    Rossi, M.5
  • 28
    • 53049110420 scopus 로고    scopus 로고
    • A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene
    • Salo AM, Cox H, Farndon P, Moss C, Grindulis H, et al. (2008) A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene. Am J Hum Genet 83: 495-503.
    • (2008) Am J Hum Genet , vol.83 , pp. 495-503
    • Salo, A.M.1    Cox, H.2    Farndon, P.3    Moss, C.4    Grindulis, H.5
  • 29
    • 34347382592 scopus 로고    scopus 로고
    • Expanding the lysyl hydroxylase toolbox: new insights into the localization and activities of lysyl hydroxylase 3 (LH3)
    • Myllyla R, Wang C, Heikkinen J, Juffer A, Lampela O, et al. (2007) Expanding the lysyl hydroxylase toolbox: new insights into the localization and activities of lysyl hydroxylase 3 (LH3). J Cell Physiol 212: 323-329.
    • (2007) J Cell Physiol , vol.212 , pp. 323-329
    • Myllyla, R.1    Wang, C.2    Heikkinen, J.3    Juffer, A.4    Lampela, O.5
  • 32
    • 84883190404 scopus 로고    scopus 로고
    • Posttranslational Modifications in Type I Collagen from Different Tissues extracted from wild type and Prolyl 3-hydroxylase 1 Null Mice
    • Pokidysheva E, Zientek KD, Ishikawa Y, Mizuno K, Vranka JA, et al. (2013) Posttranslational Modifications in Type I Collagen from Different Tissues extracted from wild type and Prolyl 3-hydroxylase 1 Null Mice. J Biol Chem 288: 24742-24752.
    • (2013) J Biol Chem , vol.288 , pp. 24742-24752
    • Pokidysheva, E.1    Zientek, K.D.2    Ishikawa, Y.3    Mizuno, K.4    Vranka, J.A.5
  • 33
    • 0028220202 scopus 로고
    • Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
    • Raghunath M, Bruckner P, Steinmann B, (1994) Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J Mol Biol 236: 940-949.
    • (1994) J Mol Biol , vol.236 , pp. 940-949
    • Raghunath, M.1    Bruckner, P.2    Steinmann, B.3
  • 34
    • 0027389056 scopus 로고
    • Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen
    • Bachinger HP, Morris NP, Davis JM, (1993) Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen. Am J Med Genet 45: 152-162.
    • (1993) Am J Med Genet , vol.45 , pp. 152-162
    • Bachinger, H.P.1    Morris, N.P.2    Davis, J.M.3
  • 35
    • 0032520161 scopus 로고    scopus 로고
    • Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506
    • Zeng B, MacDonald JR, Bann JG, Beck K, Gambee JE, et al. (1998) Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506. Biochem J 330 (Pt 1):: 109-114.
    • (1998) Biochem J , vol.330 , Issue.Pt 1 , pp. 109-114
    • Zeng, B.1    MacDonald, J.R.2    Bann, J.G.3    Beck, K.4    Gambee, J.E.5
  • 36
    • 84867455169 scopus 로고    scopus 로고
    • Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix
    • Barnes AM, Cabral WA, Weis M, Makareeva E, Mertz EL, et al. (2012) Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix. Hum Mutat 33: 1589-1598.
    • (2012) Hum Mutat , vol.33 , pp. 1589-1598
    • Barnes, A.M.1    Cabral, W.A.2    Weis, M.3    Makareeva, E.4    Mertz, E.L.5
  • 37
    • 84871243967 scopus 로고    scopus 로고
    • Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen
    • Schwarze U, Cundy T, Pyott SM, Christiansen HE, Hegde MR, et al. (2013) Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen. Hum Mol Genet 22: 1-17.
    • (2013) Hum Mol Genet , vol.22 , pp. 1-17
    • Schwarze, U.1    Cundy, T.2    Pyott, S.M.3    Christiansen, H.E.4    Hegde, M.R.5
  • 38
    • 84881616173 scopus 로고    scopus 로고
    • Kuskokwim Syndrome, a Recessive Congenital Contracture Disorder, Extends the Phenotype of FKBP10 Mutations
    • Barnes AM, Duncan G, Weis M, Paton W, Cabral WA, et al. (2013) Kuskokwim Syndrome, a Recessive Congenital Contracture Disorder, Extends the Phenotype of FKBP10 Mutations. Hum Mutat 34: 1279-1288.
    • (2013) Hum Mutat , vol.34 , pp. 1279-1288
    • Barnes, A.M.1    Duncan, G.2    Weis, M.3    Paton, W.4    Cabral, W.A.5
  • 39
    • 84862780507 scopus 로고    scopus 로고
    • Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss
    • Baumann M, Giunta C, Krabichler B, Ruschendorf F, Zoppi N, et al. (2012) Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss. Am J Hum Genet 90: 201-216.
    • (2012) Am J Hum Genet , vol.90 , pp. 201-216
    • Baumann, M.1    Giunta, C.2    Krabichler, B.3    Ruschendorf, F.4    Zoppi, N.5
  • 40
    • 0036377858 scopus 로고    scopus 로고
    • The kyphoscoliotic type of Ehlers-Danlos syndrome (type VI): differential effects on the hydroxylation of lysine in collagens I and II revealed by analysis of cross-linked telopeptides from urine
    • Eyre D, Shao P, Weis MA, Steinmann B, (2002) The kyphoscoliotic type of Ehlers-Danlos syndrome (type VI): differential effects on the hydroxylation of lysine in collagens I and II revealed by analysis of cross-linked telopeptides from urine. Mol Genet Metab 76: 211-216.
    • (2002) Mol Genet Metab , vol.76 , pp. 211-216
    • Eyre, D.1    Shao, P.2    Weis, M.A.3    Steinmann, B.4
  • 41
    • 0032772689 scopus 로고    scopus 로고
    • Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro
    • Uzawa K, Grzesik WJ, Nishiura T, Kuznetsov SA, Robey PG, et al. (1999) Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro. J Bone Miner Res 14: 1272-1280.
    • (1999) J Bone Miner Res , vol.14 , pp. 1272-1280
    • Uzawa, K.1    Grzesik, W.J.2    Nishiura, T.3    Kuznetsov, S.A.4    Robey, P.G.5
  • 43
    • 17044454221 scopus 로고    scopus 로고
    • Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis
    • van der Slot AJ, Zuurmond AM, Bardoel AF, Wijmenga C, Pruijs HE, et al. (2003) Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J Biol Chem 278: 40967-40972.
    • (2003) J Biol Chem , vol.278 , pp. 40967-40972
    • van der Slot, A.J.1    Zuurmond, A.M.2    Bardoel, A.F.3    Wijmenga, C.4    Pruijs, H.E.5
  • 44
    • 0015396145 scopus 로고
    • Reducible crosslinks in hydroxylysine-deficient collagens of a heritable disorder of connective tissue
    • Eyre DR, Glimcher MJ, (1972) Reducible crosslinks in hydroxylysine-deficient collagens of a heritable disorder of connective tissue. Proc Natl Acad Sci U S A 69: 2594-2598.
    • (1972) Proc Natl Acad Sci U S A , vol.69 , pp. 2594-2598
    • Eyre, D.R.1    Glimcher, M.J.2
  • 45
    • 0030937637 scopus 로고    scopus 로고
    • Abnormal formation of collagen cross-links in skin fibroblasts cultured from patients with Ehlers-Danlos syndrome type VI
    • Pasquali M, Still MJ, Vales T, Rosen RI, Evinger JD, et al. (1997) Abnormal formation of collagen cross-links in skin fibroblasts cultured from patients with Ehlers-Danlos syndrome type VI. Proc Assoc Am Physicians 109: 33-41.
    • (1997) Proc Assoc Am Physicians , vol.109 , pp. 33-41
    • Pasquali, M.1    Still, M.J.2    Vales, T.3    Rosen, R.I.4    Evinger, J.D.5
  • 46
    • 0015502702 scopus 로고
    • A heritable disorder of connective tissue. Hydroxylysine-deficient collagen disease
    • Pinnell SR, Krane SM, Kenzora JE, Glimcher MJ, (1972) A heritable disorder of connective tissue. Hydroxylysine-deficient collagen disease. N Engl J Med 286: 1013-1020.
    • (1972) N Engl J Med , vol.286 , pp. 1013-1020
    • Pinnell, S.R.1    Krane, S.M.2    Kenzora, J.E.3    Glimcher, M.J.4
  • 48
    • 0036861267 scopus 로고    scopus 로고
    • The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro
    • Wang C, Luosujarvi H, Heikkinen J, Risteli M, Uitto L, et al. (2002) The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. Matrix Biol 21: 559-566.
    • (2002) Matrix Biol , vol.21 , pp. 559-566
    • Wang, C.1    Luosujarvi, H.2    Heikkinen, J.3    Risteli, M.4    Uitto, L.5
  • 49
    • 4444245754 scopus 로고    scopus 로고
    • Characterization of collagenous peptides bound to lysyl hydroxylase isoforms
    • Risteli M, Niemitalo O, Lankinen H, Juffer AH, Myllyla R, (2004) Characterization of collagenous peptides bound to lysyl hydroxylase isoforms. J Biol Chem 279: 37535-37543.
    • (2004) J Biol Chem , vol.279 , pp. 37535-37543
    • Risteli, M.1    Niemitalo, O.2    Lankinen, H.3    Juffer, A.H.4    Myllyla, R.5
  • 50
    • 36349032945 scopus 로고    scopus 로고
    • Secretion and assembly of type IV and VI collagens depend on glycosylation of hydroxylysines
    • Sipila L, Ruotsalainen H, Sormunen R, Baker NL, Lamande SR, et al. (2007) Secretion and assembly of type IV and VI collagens depend on glycosylation of hydroxylysines. J Biol Chem 282: 33381-33388.
    • (2007) J Biol Chem , vol.282 , pp. 33381-33388
    • Sipila, L.1    Ruotsalainen, H.2    Sormunen, R.3    Baker, N.L.4    Lamande, S.R.5
  • 51
    • 0027394821 scopus 로고
    • Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta
    • Vetter U, Weis MA, Morike M, Eanes ED, Eyre DR, (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
  • 52
    • 0034048541 scopus 로고    scopus 로고
    • Pyridinium cross-links in bone of patients with osteogenesis imperfecta: evidence of a normal intrafibrillar collagen packing
    • Bank RA, Tekoppele JM, Janus GJ, Wassen MH, Pruijs HE, et al. (2000) Pyridinium cross-links in bone of patients with osteogenesis imperfecta: evidence of a normal intrafibrillar collagen packing. J Bone Miner Res 15: 1330-1336.
    • (2000) J Bone Miner Res , vol.15 , pp. 1330-1336
    • Bank, R.A.1    Tekoppele, J.M.2    Janus, G.J.3    Wassen, M.H.4    Pruijs, H.E.5
  • 53
    • 0017736223 scopus 로고
    • Osteogenesis imperfecta: biochemical studies of bone collagen
    • Fujii K, Tanzer ML, (1977) Osteogenesis imperfecta: biochemical studies of bone collagen. Clin Orthop Relat Res pp. 271-277.
    • (1977) Clin Orthop Relat Res , pp. 271-277
    • Fujii, K.1    Tanzer, M.L.2
  • 54
    • 84886095231 scopus 로고    scopus 로고
    • Bone Collagen: New Clues to Its Mineralization Mechanism from Recessive Osteogenesis Imperfecta
    • Eyre DR, Weis MA, (2013) Bone Collagen: New Clues to Its Mineralization Mechanism from Recessive Osteogenesis Imperfecta. Calcif Tissue Int 93: 338-347.
    • (2013) Calcif Tissue Int , vol.93 , pp. 338-347
    • Eyre, D.R.1    Weis, M.A.2
  • 55
    • 84859198543 scopus 로고    scopus 로고
    • Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly
    • Hudson DM, Kim LS, Weis M, Cohn DH, Eyre DR, (2012) Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly. Biochemistry 51: 2417-2424.
    • (2012) Biochemistry , vol.51 , pp. 2417-2424
    • Hudson, D.M.1    Kim, L.S.2    Weis, M.3    Cohn, D.H.4    Eyre, D.R.5
  • 56
    • 34249652649 scopus 로고    scopus 로고
    • Tissue-specific changes in the hydroxylysine content and cross-links of collagens and alterations in fibril morphology in lysyl hydroxylase 1 knock-out mice
    • Takaluoma K, Hyry M, Lantto J, Sormunen R, Bank RA, et al. (2007) Tissue-specific changes in the hydroxylysine content and cross-links of collagens and alterations in fibril morphology in lysyl hydroxylase 1 knock-out mice. J Biol Chem 282: 6588-6596.
    • (2007) J Biol Chem , vol.282 , pp. 6588-6596
    • Takaluoma, K.1    Hyry, M.2    Lantto, J.3    Sormunen, R.4    Bank, R.A.5
  • 57
    • 0028841268 scopus 로고
    • Urinary pyridinoline cross-links in Ehlers-Danlos syndrome type VI
    • Steinmann B, Eyre DR, Shao P, (1995) Urinary pyridinoline cross-links in Ehlers-Danlos syndrome type VI. Am J Hum Genet 57: 1505-1508.
    • (1995) Am J Hum Genet , vol.57 , pp. 1505-1508
    • Steinmann, B.1    Eyre, D.R.2    Shao, P.3
  • 58
    • 0010606157 scopus 로고
    • Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen
    • Yamauchi M, Noyes C, Kuboki Y, Mechanic GL, (1982) Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen. Proc Natl Acad Sci U S A 79: 7684-7688.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 7684-7688
    • Yamauchi, M.1    Noyes, C.2    Kuboki, Y.3    Mechanic, G.L.4
  • 59
    • 0015846875 scopus 로고
    • Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink
    • Eyre DR, Glimcher MJ, (1973) Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink. Biochem Biophys Res Commun 52: 663-671.
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 663-671
    • Eyre, D.R.1    Glimcher, M.J.2
  • 60
    • 0345732115 scopus 로고    scopus 로고
    • Lower bone cellular activities in male and female mature C3H/HeJ mice are associated with higher bone mass and different pyridinium crosslink profiles compared to C57BL/6J mice
    • Amblard D, Lafage-Proust MH, Chamson A, Rattner A, Collet P, et al. (2003) Lower bone cellular activities in male and female mature C3H/HeJ mice are associated with higher bone mass and different pyridinium crosslink profiles compared to C57BL/6J mice. J Bone Miner Metab 21: 377-387.
    • (2003) J Bone Miner Metab , vol.21 , pp. 377-387
    • Amblard, D.1    Lafage-Proust, M.H.2    Chamson, A.3    Rattner, A.4    Collet, P.5
  • 61
    • 0036313556 scopus 로고    scopus 로고
    • Cross-link profile of bone collagen correlates with structural organization of trabeculae
    • Banse X, Devogelaer JP, Lafosse A, Sims TJ, Grynpas M, et al. (2002) Cross-link profile of bone collagen correlates with structural organization of trabeculae. Bone 31: 70-76.
    • (2002) Bone , vol.31 , pp. 70-76
    • Banse, X.1    Devogelaer, J.P.2    Lafosse, A.3    Sims, T.J.4    Grynpas, M.5
  • 62
    • 0036708153 scopus 로고    scopus 로고
    • Mechanical properties of adult vertebral cancellous bone: correlation with collagen intermolecular cross-links
    • Banse X, Sims TJ, Bailey AJ, (2002) Mechanical properties of adult vertebral cancellous bone: correlation with collagen intermolecular cross-links. J Bone Miner Res 17: 1621-1628.
    • (2002) J Bone Miner Res , vol.17 , pp. 1621-1628
    • Banse, X.1    Sims, T.J.2    Bailey, A.J.3
  • 63
    • 0037260993 scopus 로고    scopus 로고
    • BayGenomics: a resource of insertional mutations in mouse embryonic stem cells
    • Stryke D, Kawamoto M, Huang CC, Johns SJ, King LA, et al. (2003) BayGenomics: a resource of insertional mutations in mouse embryonic stem cells. Nucleic Acids Res 31: 278-281.
    • (2003) Nucleic Acids Res , vol.31 , pp. 278-281
    • Stryke, D.1    Kawamoto, M.2    Huang, C.C.3    Johns, S.J.4    King, L.A.5
  • 64
    • 0019126423 scopus 로고
    • Differential staining of cartilage and bone in whole mouse fetuses by alcian blue and alizarin red S
    • McLeod MJ, (1980) Differential staining of cartilage and bone in whole mouse fetuses by alcian blue and alizarin red S. Teratology 22: 299-301.
    • (1980) Teratology , vol.22 , pp. 299-301
    • McLeod, M.J.1
  • 65
    • 84872844733 scopus 로고    scopus 로고
    • Sclerostin antibody improves skeletal parameters in a Brtl/+ mouse model of osteogenesis imperfecta
    • Sinder BP, Eddy MM, Ominsky MS, Caird MS, Marini JC, et al. (2013) Sclerostin antibody improves skeletal parameters in a Brtl/+ mouse model of osteogenesis imperfecta. J Bone Miner Res 28: 73-80.
    • (2013) J Bone Miner Res , vol.28 , pp. 73-80
    • Sinder, B.P.1    Eddy, M.M.2    Ominsky, M.S.3    Caird, M.S.4    Marini, J.C.5
  • 66
    • 84555195940 scopus 로고    scopus 로고
    • Osteoblast isolation from murine calvaria and long bones
    • Bakker AD, Klein-Nulend J, (2012) Osteoblast isolation from murine calvaria and long bones. Methods Mol Biol 816: 19-29.
    • (2012) Methods Mol Biol , vol.816 , pp. 19-29
    • Bakker, A.D.1    Klein-Nulend, J.2
  • 67
    • 0021996663 scopus 로고
    • Altered triple helical structure of type I procollagen in lethal perinatal osteogenesis imperfecta
    • Bonadio J, Holbrook KA, Gelinas RE, Jacob J, Byers PH, (1985) Altered triple helical structure of type I procollagen in lethal perinatal osteogenesis imperfecta. J Biol Chem 260: 1734-1742.
    • (1985) J Biol Chem , vol.260 , pp. 1734-1742
    • Bonadio, J.1    Holbrook, K.A.2    Gelinas, R.E.3    Jacob, J.4    Byers, P.H.5
  • 68
    • 41949119604 scopus 로고    scopus 로고
    • Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta
    • Makareeva E, Mertz EL, Kuznetsova NV, Sutter MB, DeRidder AM, et al. (2008) Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta. J Biol Chem 283: 4787-4798.
    • (2008) J Biol Chem , vol.283 , pp. 4787-4798
    • Makareeva, E.1    Mertz, E.L.2    Kuznetsova, N.V.3    Sutter, M.B.4    DeRidder, A.M.5
  • 69
    • 0027353094 scopus 로고
    • The post-translational chemistry and molecular packing of mineralizing tendon collagens
    • Yamauchi M, Katz EP, (1993) The post-translational chemistry and molecular packing of mineralizing tendon collagens. Connect Tissue Res 29: 81-98.
    • (1993) Connect Tissue Res , vol.29 , pp. 81-98
    • Yamauchi, M.1    Katz, E.P.2
  • 70
    • 84934436741 scopus 로고    scopus 로고
    • Lysine hydroxylation and cross-linking of collagen
    • Yamauchi M, Shiiba M, (2008) Lysine hydroxylation and cross-linking of collagen. Methods Mol Biol 446: 95-108.
    • (2008) Methods Mol Biol , vol.446 , pp. 95-108
    • Yamauchi, M.1    Shiiba, M.2
  • 71
    • 0023075941 scopus 로고
    • Collagen cross-linking amino acids
    • Eyre D, (1987) Collagen cross-linking amino acids. Methods Enzymol 144: 115-139.
    • (1987) Methods Enzymol , vol.144 , pp. 115-139
    • Eyre, D.1
  • 72
    • 0031258359 scopus 로고    scopus 로고
    • Phenotypic comparison of an osteogenesis imperfecta type IV proband with a de novo alpha2(I) Gly922 → Ser substitution in type I collagen and an unrelated patient with an identical mutation
    • Forlino A, D'Amato E, Valli M, Camera G, Hopkins E, et al. (1997) Phenotypic comparison of an osteogenesis imperfecta type IV proband with a de novo alpha2(I) Gly922 → Ser substitution in type I collagen and an unrelated patient with an identical mutation. Biochem Mol Med 62: 26-35.
    • (1997) Biochem Mol Med , vol.62 , pp. 26-35
    • Forlino, A.1    D'Amato, E.2    Valli, M.3    Camera, G.4    Hopkins, E.5
  • 73
    • 0038193527 scopus 로고    scopus 로고
    • Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix
    • Cabral WA, Mertts MV, Makareeva E, Colige A, Tekin M, et al. (2003) Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix. J Biol Chem 278: 10006-10012.
    • (2003) J Biol Chem , vol.278 , pp. 10006-10012
    • Cabral, W.A.1    Mertts, M.V.2    Makareeva, E.3    Colige, A.4    Tekin, M.5
  • 74
    • 0028328909 scopus 로고
    • Deposition and selective degradation of structurally-abnormal type I collagen in a collagen matrix produced by osteogenesis imperfecta fibroblasts in vitro
    • Bateman JF, Golub SB, (1994) Deposition and selective degradation of structurally-abnormal type I collagen in a collagen matrix produced by osteogenesis imperfecta fibroblasts in vitro. Matrix Biol 14: 251-262.
    • (1994) Matrix Biol , vol.14 , pp. 251-262
    • Bateman, J.F.1    Golub, S.B.2
  • 75
    • 21444439013 scopus 로고    scopus 로고
    • Mutations near amino end of alpha1(I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing
    • Cabral WA, Makareeva E, Colige A, Letocha AD, Ty JM, et al. (2005) Mutations near amino end of alpha1(I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing. J Biol Chem 280: 19259-19269.
    • (2005) J Biol Chem , vol.280 , pp. 19259-19269
    • Cabral, W.A.1    Makareeva, E.2    Colige, A.3    Letocha, A.D.4    Ty, J.M.5


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