메뉴 건너뛰기




Volumn 60, Issue 6, 1997, Pages 501-505

Alteration in the extent of collagen I hydroxylation, isolated from femoral heads of women with a femoral neck fracture caused by osteoporosis

Author keywords

Collagen I; Hip fracture; Lysyl hydroxylation; Osteoporosis; Prolyl hydroxylation

Indexed keywords

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; CLINICAL ARTICLE; COLLAGEN METABOLISM; FEMALE; FEMUR NECK FRACTURE; HIP FRACTURE; HUMAN; HUMAN TISSUE; HYDROXYLATION; OSTEOARTHRITIS; OSTEOPOROSIS; PRIORITY JOURNAL;

EID: 0343487763     PISSN: 0171967X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002239900271     Document Type: Article
Times cited : (44)

References (34)
  • 2
    • 0342983842 scopus 로고
    • The organic matrix of bone
    • Bourne GH (ed) Academic Press, New York
    • Eastol JE (1956) The organic matrix of bone. In: Bourne GH (ed) The biochemistry and physiology of bone. Academic Press, New York, p 91
    • (1956) The Biochemistry and Physiology of Bone , pp. 91
    • Eastol, J.E.1
  • 3
    • 0024351071 scopus 로고
    • Substitution of serine for α1(I) glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen
    • Pack M, Constantinou DC, Kalia K, Nielsen KB, Prockop DJ (1989) Substitution of serine for α1(I) glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. J Biol Chem 264:19694-19699
    • (1989) J Biol Chem , vol.264 , pp. 19694-19699
    • Pack, M.1    Constantinou, D.C.2    Kalia, K.3    Nielsen, K.B.4    Prockop, D.J.5
  • 4
    • 0025086974 scopus 로고
    • Substitution of arginine for glycine at position 847 in the triple-helicial domain of the α1(I) chain of type I collagen produces lethal osteogenesis imperfecta
    • Wallis GA, Starman BJ, Schwartz MF, Byers PH (1990) Substitution of arginine for glycine at position 847 in the triple-helicial domain of the α1(I) chain of type I collagen produces lethal osteogenesis imperfecta. J Biol Chem 265:18628-18633
    • (1990) J Biol Chem , vol.265 , pp. 18628-18633
    • Wallis, G.A.1    Starman, B.J.2    Schwartz, M.F.3    Byers, P.H.4
  • 5
    • 0024230293 scopus 로고
    • A substitution of cysteine for glycine 784 of the α1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away
    • Vogel BE, Doelz R, Kadler KE, Hojima Y, Engel J, Prockop DJ (1988) A substitution of cysteine for glycine 784 of the α1 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away. J Biol Chem 263:19249-19255
    • (1988) J Biol Chem , vol.263 , pp. 19249-19255
    • Vogel, B.E.1    Doelz, R.2    Kadler, K.E.3    Hojima, Y.4    Engel, J.5    Prockop, D.J.6
  • 6
    • 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, Müller PK (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
  • 7
    • 0015502702 scopus 로고
    • A heritable disorder of connective tissue hydroxylysine-deficient collagen disease
    • Pinell SR, Krane SM, Kenzora JE, Glimcher EJ (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
    • Pinell, S.R.1    Krane, S.M.2    Kenzora, J.E.3    Glimcher, E.J.4
  • 8
    • 0015407865 scopus 로고
    • Lysyl-protocollagen hydroxylase deficiency in fibroblasts from siblings with hydroxylysine-deficient collagen
    • Krane SM, Pinell SR, Erbe RW (1972) Lysyl-protocollagen hydroxylase deficiency in fibroblasts from siblings with hydroxylysine-deficient collagen. Proc Natl Acad Sci 69:2899-2903
    • (1972) Proc Natl Acad Sci , vol.69 , pp. 2899-2903
    • Krane, S.M.1    Pinell, S.R.2    Erbe, R.W.3
  • 9
    • 0018305846 scopus 로고
    • Biochemical characteristics of the Ehlers-Danlos syndrome type VI in a family with one affected child
    • Krieg T, Feldman U, Kessler W, Müller PK (1979) Biochemical characteristics of the Ehlers-Danlos syndrome type VI in a family with one affected child. Hum Genet 46:41-49
    • (1979) Hum Genet , vol.46 , pp. 41-49
    • Krieg, T.1    Feldman, U.2    Kessler, W.3    Müller, P.K.4
  • 10
    • 0026678191 scopus 로고
    • Compositional analysis of the collagenous bone matrix. a study on adult and osteopenic bone
    • Bätge B, Diebold J, Stein H, Bodo M, Müller PK (1992) Compositional analysis of the collagenous bone matrix. A study on adult and osteopenic bone. 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
  • 11
    • 0026681853 scopus 로고
    • Posttranslational modifications in the collagen of human osteoporotic femoral head
    • Bailey AK, Wotton SF, Simps TJ, Thompson PW (1992) Posttranslational modifications in the collagen of human osteoporotic femoral head. Biochem Biophys Res Comm 185:801-805
    • (1992) Biochem Biophys Res Comm , vol.185 , pp. 801-805
    • Bailey, A.K.1    Wotton, S.F.2    Simps, T.J.3    Thompson, P.W.4
  • 12
    • 0022510760 scopus 로고
    • Rapid fractionation of collagen chains and peptides by high-performance liquid chromatography
    • Bateman JF, Mascara T, Chan D, Cole WG (1986) Rapid fractionation of collagen chains and peptides by high-performance liquid chromatography. Anal Biochem 154:338-344
    • (1986) Anal Biochem , vol.154 , pp. 338-344
    • Bateman, J.F.1    Mascara, T.2    Chan, D.3    Cole, W.G.4
  • 13
    • 0000533290 scopus 로고
    • Determination of amino acids with 9-fluorenylmethylchloroformate and reversed-phase high-performance liquid chromatography
    • Einarsson S, Josefsson B, Lagerkvist S (1983) Determination of amino acids with 9-fluorenylmethylchloroformate and reversed-phase high-performance liquid chromatography. J Chromatogr 282:609-618
    • (1983) J Chromatogr , vol.282 , pp. 609-618
    • Einarsson, S.1    Josefsson, B.2    Lagerkvist, S.3
  • 16
    • 0025778486 scopus 로고
    • Mutations in collagen genes: Cause of rare and some common diseases in humans
    • Kuivaniemi H, Tromp K, Prockop DJ (1991) Mutations in collagen genes: cause of rare and some common diseases in humans. FASEB 5:2052-2060
    • (1991) FASEB , vol.5 , pp. 2052-2060
    • Kuivaniemi, H.1    Tromp, K.2    Prockop, D.J.3
  • 17
    • 0027196285 scopus 로고
    • Molecular basis of heritable connective tissue diseases
    • Vandenberg P (1993) Molecular basis of heritable connective tissue diseases. Biochem Med Metab Biol 49:1-12
    • (1993) Biochem Med Metab Biol , vol.49 , pp. 1-12
    • Vandenberg, P.1
  • 18
    • 0016777556 scopus 로고
    • Disturbance in the regulation of the type of collagen synthesized in a form of osteogenesis imperfecta
    • Müller PK, Lemmen C, Gay S, Meigel W (1975) Disturbance in the regulation of the type of collagen synthesized in a form of osteogenesis imperfecta. Eur J Biochem 59:97-104
    • (1975) Eur J Biochem , vol.59 , pp. 97-104
    • Müller, P.K.1    Lemmen, C.2    Gay, S.3    Meigel, W.4
  • 19
    • 0021181518 scopus 로고
    • Cysteine in the triple-helicial domain of one allelic product of the a1(I) gene of type I collagen produces a lethal form of osteogenesis imperfecta
    • Steinman B, Rao VH, Vogel A, Bruckner P, Gitzelman R, Byers P (1984) Cysteine in the triple-helicial domain of one allelic product of the a1(I) gene of type I collagen produces a lethal form of osteogenesis imperfecta. J Biol Chem 259: 11129-11138
    • (1984) J Biol Chem , vol.259 , pp. 11129-11138
    • Steinman, B.1    Rao, V.H.2    Vogel, A.3    Bruckner, P.4    Byers P, G.R.5
  • 20
    • 0020628753 scopus 로고
    • Analysis of cyanogen bromide peptides of type I collagen from a patient with lethal osteogenesis imperfecta
    • Kirsch E, Glanville RW, Krieg T, Müller P (1983) Analysis of cyanogen bromide peptides of type I collagen from a patient with lethal osteogenesis imperfecta. Biochem J 211:599-603
    • (1983) Biochem J , vol.211 , pp. 599-603
    • Kirsch, E.1    Glanville, R.W.2    Krieg, T.3    Müller, P.4
  • 21
    • 0343447454 scopus 로고
    • Bone quality and bone quantity in osteoporosis
    • Christiansen C, Johansen JS, Riisi BJ (eds) Osteopress, Copenhagen
    • Grynpas MD, Katz I, Pritzker KPH (1987) Bone quality and bone quantity in osteoporosis. In: Christiansen C, Johansen JS, Riisi BJ (eds) Osteoporosis. Osteopress, Copenhagen, p 364
    • (1987) Osteoporosis , pp. 364
    • Grynpas, M.D.1    Katz, I.2    Pritzker, K.P.H.3
  • 23
    • 0026000415 scopus 로고
    • Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: Evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta
    • Spotila L, Constantinou CD, Sereda L, Ganguly A, Riggs BL, Prockop DJ (1991) Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta. Proc Natl Acad Sci USA 88:5423-5427
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5423-5427
    • Spotila, L.1    Constantinou, C.D.2    Sereda, L.3    Ganguly, A.4    Riggs, B.L.5    Prockop, D.J.6
  • 24
  • 25
    • 0029092961 scopus 로고
    • Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias
    • Lehmann HW, Wolf E, Röser K, Bodo M, Delling G, Müller PK (1995) Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias. J Cancer Res Clin Oncol 121:413-418
    • (1995) J Cancer Res Clin Oncol , vol.121 , pp. 413-418
    • Lehmann, H.W.1    Wolf, E.2    Röser, K.3    Bodo, M.4    Delling, G.5    Müller, P.K.6
  • 26
    • 0018863356 scopus 로고
    • Changes in tissue morphology and collagen composition during the repair of cortical bone in the adult chicken
    • Glimcher MJ, Shapiro F, Ellis RD, Eyre DR (1980) Changes in tissue morphology and collagen composition during the repair of cortical bone in the adult chicken. J Bone Jt Surg [Am]62:964-973
    • (1980) J Bone Jt Surg [Am] , vol.62 , pp. 964-973
    • Glimcher, M.J.1    Shapiro, F.2    Ellis, R.D.3    Eyre, D.R.4
  • 27
    • 0023394028 scopus 로고
    • Polar-apolar characteristics and fibrillogenesis of glycosylated collagen
    • Amudeswari S, Liang N, Chakrabarti B (1987) Polar-apolar characteristics and fibrillogenesis of glycosylated collagen. Coll Relat Res 7:215-223
    • (1987) Coll Relat Res , vol.7 , pp. 215-223
    • Amudeswari, S.1    Liang, N.2    Chakrabarti, B.3
  • 29
    • 0026643352 scopus 로고
    • Enzymatic and nonenzymatic cross-linking of collagen and elastin
    • Reiser K, McCormick R, Rucker RB (1992) Enzymatic and nonenzymatic cross-linking of collagen and elastin. FASEB 6:2439-2448
    • (1992) FASEB , vol.6 , pp. 2439-2448
    • Reiser, K.1    McCormick, R.2    Rucker, R.B.3
  • 30
    • 0020531821 scopus 로고
    • The organization of crosslinking in collagen fibrils
    • Davison PF, Brennan M (1983) The organization of crosslinking in collagen fibrils. Connect Tissue Res 11:135-151
    • (1983) Connect Tissue Res , vol.11 , pp. 135-151
    • Davison, P.F.1    Brennan, M.2
  • 33
    • 0016163996 scopus 로고
    • Age-related variations in hydroxylation of lysine and proline in collagen
    • Barnes MJ, Constable BJ, Morton LF, Royce PM (1974) Age-related variations in hydroxylation of lysine and proline in collagen. Biochem J 139:461-468
    • (1974) Biochem J , vol.139 , pp. 461-468
    • Barnes, M.J.1    Constable, B.J.2    Morton, L.F.3    Royce, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.