메뉴 건너뛰기




Volumn 126, Issue 1, 1996, Pages 51-60

Modulation of lysyl oxidase by dietary copper in rats

Author keywords

collagen; copper; elastin; lysyl oxidase; rats

Indexed keywords

COLLAGEN; COPPER; EGG WHITE; ELASTIN; MESSENGER RNA; PROTEIN LYSINE 6 OXIDASE; TRITIUM; TROPOELASTIN;

EID: 9044249316     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/126.1.51     Document Type: Article
Times cited : (41)

References (51)
  • 1
    • 0025932841 scopus 로고
    • Induction of lung lysyl oxidase activity and lysyl oxidase protein by exposure of rats to cadmium chloride: Properties of the induced enzyme
    • Almassian, B. J., Trackman, P. C., Iguchi, H., Boak, A., Calvaresi, D. & Kagan, H. M. (1990) Induction of lung lysyl oxidase activity and lysyl oxidase protein by exposure of rats to cadmium chloride: properties of the induced enzyme. Connect. Tissue Res. 25: 197-208.
    • (1990) Connect. Tissue Res. , vol.25 , pp. 197-208
    • Almassian, B.J.1    Trackman, P.C.2    Iguchi, H.3    Boak, A.4    Calvaresi, D.5    Kagan, H.M.6
  • 2
    • 0024786570 scopus 로고
    • Localization of human placenta lysyl oxidase on human placenta, skin and aorta by immunoelectronmicroscopy
    • Baccarani-Contri, M., Vincenzi, D., Quaglino, J. R., Mori, G. & Pasquali-Ronchetti, I. (1989) Localization of human placenta lysyl oxidase on human placenta, skin and aorta by immunoelectronmicroscopy. Matrix 9: 428-436.
    • (1989) Matrix , vol.9 , pp. 428-436
    • Baccarani-Contri, M.1    Vincenzi, D.2    Quaglino, J.R.3    Mori, G.4    Pasquali-Ronchetti, I.5
  • 4
    • 0019551730 scopus 로고
    • "Western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide I gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein
    • Burnette, W. N. (1981) "Western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide I gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein. Anal. Biochem. 112: 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 7
    • 0019777268 scopus 로고
    • Lung lysyl oxidase and prolyl hydroxylase: Increases induced by cadmium chloride inhalation and the effect of β-aminopropionitrile in rats
    • Chichester, C. O., Palmer, K. C., Hayes, J. A. & Kagan, H. M. (1981) Lung lysyl oxidase and prolyl hydroxylase: increases induced by cadmium chloride inhalation and the effect of β-aminopropionitrile in rats. Am. Rev. Respir. Dis. 124: 709-713.
    • (1981) Am. Rev. Respir. Dis. , vol.124 , pp. 709-713
    • Chichester, C.O.1    Palmer, K.C.2    Hayes, J.A.3    Kagan, H.M.4
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 84963016322 scopus 로고
    • Relation of monoamine oxidase activity and collagen crosslinking in copper-deficient and control tissues
    • Chou, W. S., Savage, J. E. & O'Dell, B. L. (1968) Relation of monoamine oxidase activity and collagen crosslinking in copper-deficient and control tissues. Proc. Soc. Exp. Biol. Med. 128: 948-952.
    • (1968) Proc. Soc. Exp. Biol. Med. , vol.128 , pp. 948-952
    • Chou, W.S.1    Savage, J.E.2    O'Dell, B.L.3
  • 10
    • 0023888613 scopus 로고
    • Role of copper in the regulation and accumulation of Superoxide dismutase and metallothionein in rat liver
    • Chung, K., Romero, N., Tinker, D., Keen, C. L., Amemiya, K. & Rucker, R. B. (1988) Role of copper in the regulation and accumulation of Superoxide dismutase and metallothionein in rat liver. J. Nutr. 118: 859-864.
    • (1988) J. Nutr. , vol.118 , pp. 859-864
    • Chung, K.1    Romero, N.2    Tinker, D.3    Keen, C.L.4    Amemiya, K.5    Rucker, R.B.6
  • 11
    • 0019177807 scopus 로고
    • In vivo inhibition of lysyl oxidase by high dose of zinc
    • Chvapil, M. & Misiorowski, R. (1980) In vivo inhibition of lysyl oxidase by high dose of zinc. Proc. Soc. Exp. Biol. Med. 164: 137-141.
    • (1980) Proc. Soc. Exp. Biol. Med. , vol.164 , pp. 137-141
    • Chvapil, M.1    Misiorowski, R.2
  • 12
    • 0027246376 scopus 로고
    • Structure of the mouse lysyl oxidase gene
    • Contente, S., Csiszar, K. & Kenyon, K. (1993) Structure of the mouse lysyl oxidase gene. Genomics 16: 395-400.
    • (1993) Genomics , vol.16 , pp. 395-400
    • Contente, S.1    Csiszar, K.2    Kenyon, K.3
  • 13
    • 0022487922 scopus 로고
    • Comparison of lysyl oxidase of bovine aorta and lung
    • Cronlund, A. L. & Kagan, H. M. (1986) Comparison of lysyl oxidase of bovine aorta and lung. Connect. Tissue Res. 15: 173-182.
    • (1986) Connect. Tissue Res. , vol.15 , pp. 173-182
    • Cronlund, A.L.1    Kagan, H.M.2
  • 15
    • 0022416361 scopus 로고
    • Elastin metabolism during perinatal lung development in the copper deficient rat
    • Dubick, M. A., Keen, C. L. & Rucker, R. B. (1985) Elastin metabolism during perinatal lung development in the copper deficient rat. Exp. Lung Res. 8: 227-241.
    • (1985) Exp. Lung Res. , vol.8 , pp. 227-241
    • Dubick, M.A.1    Keen, C.L.2    Rucker, R.B.3
  • 18
    • 0025279437 scopus 로고
    • Efficient production of chicken egg yolk antibodies against a conserved mammalian protein
    • Gassmann, M., Thömmes, S., Weiser, T. & Hübscher, U. (1990) Efficient production of chicken egg yolk antibodies against a conserved mammalian protein. FASEB J. 4: 2528-2532.
    • (1990) FASEB J. , vol.4 , pp. 2528-2532
    • Gassmann, M.1    Thömmes, S.2    Weiser, T.3    Hübscher, U.4
  • 19
    • 0021731952 scopus 로고
    • 2 collagen mRNA and their use in studying the regulation of Type I collagen synthesis by 1,25-dihydrocholecalciferol
    • 2 collagen mRNA and their use in studying the regulation of Type I collagen synthesis by 1,25-dihydrocholecalciferol. Biochem. 23: 6210-6216.
    • (1984) Biochem. , vol.23 , pp. 6210-6216
    • Genovese, C.1    Rowe, D.2    Kream, B.3
  • 20
    • 0020577769 scopus 로고
    • Isolation and characterization of full-length cDNA clones for human α, β, γ-actin mRNAs: Skeletal but not cytoplasmic actin have an amino terminal cysteine that is subsequently removed
    • Gunning, P., Parie, P., Ohayama, H., Engel, J., Blau, H. & Kedes, L. (1983) Isolation and characterization of full-length cDNA clones for human α, β, γ-actin mRNAs: skeletal but not cytoplasmic actin have an amino terminal cysteine that is subsequently removed. Mol. Cell Biol. 3: 787-795.
    • (1983) Mol. Cell Biol. , vol.3 , pp. 787-795
    • Gunning, P.1    Parie, P.2    Ohayama, H.3    Engel, J.4    Blau, H.5    Kedes, L.6
  • 21
    • 0025990715 scopus 로고
    • Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2
    • Hämäläinen, E., Jones, T. A., Sheer, D., Taskinen, K., Pihlajaniemi, T. & Kivirikko, K. I. (1991) Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2. Genomics 11: 508-516.
    • (1991) Genomics , vol.11 , pp. 508-516
    • Hämäläinen, E.1    Jones, T.A.2    Sheer, D.3    Taskinen, K.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 22
    • 0016160914 scopus 로고
    • Connective tissue amine oxidase. II. Purification and partial characterization of lysyl oxidase from chick aorta
    • Harris, E. D., Gonnerman, W. A., Savage, J. E. & O'Dell, B. L. (1974) Connective tissue amine oxidase. II. Purification and partial characterization of lysyl oxidase from chick aorta. Biochim. Biophys. Acta 341: 332-344.
    • (1974) Biochim. Biophys. Acta , vol.341 , pp. 332-344
    • Harris, E.D.1    Gonnerman, W.A.2    Savage, J.E.3    O'Dell, B.L.4
  • 23
    • 0020018910 scopus 로고
    • Lysyl oxidase: Preparation and role in elastin biosynthesis
    • [Cunningham, L. W. & Frederikson, D. W., eds., Structural and Contractile Proteins Academic Press, New York, NY
    • Kagan, H. M. & Sullivan, K. A. (1982) Lysyl oxidase: preparation and role in elastin biosynthesis. In: Methods in Enzymology [Cunningham, L. W. & Frederikson, D. W., eds.), Vol. 82, Structural and Contractile Proteins part A, pp. 637-649. Academic Press, New York, NY.
    • (1982) Methods in Enzymology , vol.82 , Issue.PART A , pp. 637-649
    • Kagan, H.M.1    Sullivan, K.A.2
  • 25
    • 0023039150 scopus 로고
    • Ultrastructural immunolocalization of lysyl oxidase in vascular connective tissue
    • Kagan, H. M., Vaccaro, C. A., Bronson, R. E., Tang, S. S. & Brody, J. S. (1986) Ultrastructural immunolocalization of lysyl oxidase in vascular connective tissue. J. Cell Biol. 103: 1121-1128.
    • (1986) J. Cell Biol. , vol.103 , pp. 1121-1128
    • Kagan, H.M.1    Vaccaro, C.A.2    Bronson, R.E.3    Tang, S.S.4    Brody, J.S.5
  • 27
    • 0027178650 scopus 로고
    • A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q 24-q25
    • Kenyon, K., Modi, W. S., Contente, S. & Friedman, R. M. (1993) A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q 24-q25. J. Biol. Chem. 268: 18435-18437.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18435-18437
    • Kenyon, K.1    Modi, W.S.2    Contente, S.3    Friedman, R.M.4
  • 28
    • 0022405587 scopus 로고
    • Partial characterization of lysyl oxidase from several human tissues
    • Kuivaniemi, H. (1985) Partial characterization of lysyl oxidase from several human tissues. Biochem. J. 230: 639-641.
    • (1985) Biochem. J. , vol.230 , pp. 639-641
    • Kuivaniemi, H.1
  • 29
    • 0021191522 scopus 로고
    • Human placental lysyl oxidase. Purification, partial characterization and preparation of two specific antisera to the enzyme
    • Kuivaniemi, H., Savolainen, E. R. & Kivirikko, K. I. (1984) Human placental lysyl oxidase. Purification, partial characterization and preparation of two specific antisera to the enzyme. J. Biol. Chem. 259: 6996-7003.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6996-7003
    • Kuivaniemi, H.1    Savolainen, E.R.2    Kivirikko, K.I.3
  • 30
    • 0026780248 scopus 로고
    • The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5. Extensive sequence homology with the murine ras recision gene
    • Mariani, T. J., Trackman, P. C, Kagan, H. M., Eddy, R. L., Shows, T. B., Boyd, C. D. & Deak, S. B. (1992) The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5. Extensive sequence homology with the murine ras recision gene. Matrix 12: 242-248.
    • (1992) Matrix , vol.12 , pp. 242-248
    • Mariani, T.J.1    Trackman, P.C.2    Kagan, H.M.3    Eddy, R.L.4    Shows, T.B.5    Boyd, C.D.6    Deak, S.B.7
  • 31
    • 0022186671 scopus 로고
    • Sensitive spectrophotometric method for the quantitative estimation of collagen
    • Marotta, M. & Martino, G. (1985) Sensitive spectrophotometric method for the quantitative estimation of collagen. Anal. Biochem. 150: 86-90.
    • (1985) Anal. Biochem. , vol.150 , pp. 86-90
    • Marotta, M.1    Martino, G.2
  • 32
    • 0026353388 scopus 로고
    • Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin
    • Murawaki, Y., Kusakabe, Y. & Hirayama, C. (1991) Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin. Hepatology 14: 1167-1173.
    • (1991) Hepatology , vol.14 , pp. 1167-1173
    • Murawaki, Y.1    Kusakabe, Y.2    Hirayama, C.3
  • 33
    • 0021819879 scopus 로고
    • Effect of vitamin B-6 (pyridoxine) deficiency on lung elastin crosslinking in perinatal and weanling rat pups
    • Myers, B. A., Dubick, M. A., Reynolds, R. D. & Rucker, R. B. (1985) Effect of vitamin B-6 (pyridoxine) deficiency on lung elastin crosslinking in perinatal and weanling rat pups. Biochem. J. 229: 153-160.
    • (1985) Biochem. J. , vol.229 , pp. 153-160
    • Myers, B.A.1    Dubick, M.A.2    Reynolds, R.D.3    Rucker, R.B.4
  • 35
    • 0020321343 scopus 로고
    • Role of copper in collagen crosslinking and its influence on selected mechanical properties of chick bone and tendon
    • Opsahl, W., Zeronian, H., Ellison, M., Lewis, D. & Rucker, R. B. (1982) Role of copper in collagen crosslinking and its influence on selected mechanical properties of chick bone and tendon. J. Nutr. 112: 708-716.
    • (1982) J. Nutr. , vol.112 , pp. 708-716
    • Opsahl, W.1    Zeronian, H.2    Ellison, M.3    Lewis, D.4    Rucker, R.B.5
  • 36
    • 0019441999 scopus 로고
    • Lysyl oxidase activity in the mouse uterine cervix is physiolgically regulated by estrogen
    • Ozasa, H., Tominaga, T., Nishmura, T. & Takeda, T. (1981) Lysyl oxidase activity in the mouse uterine cervix is physiolgically regulated by estrogen. Endocrinology 109: 618-621.
    • (1981) Endocrinology , vol.109 , pp. 618-621
    • Ozasa, H.1    Tominaga, T.2    Nishmura, T.3    Takeda, T.4
  • 38
    • 0014348347 scopus 로고
    • The crosslinking of collagen and elastin: Enzymatic conversion of lysine in peptide linkage to α-amino-adipic-S-semialdehyde (allysine) by an extract of bone
    • Pinnell, S. R. & Martin, G. R. (1968) The crosslinking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to α-amino-adipic-S-semialdehyde (allysine) by an extract of bone. Proc. Natl. Acad. Sci. U.S.A. 61: 708-718.
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.61 , pp. 708-718
    • Pinnell, S.R.1    Martin, G.R.2
  • 39
    • 0018387649 scopus 로고
    • Induction of lysyl oxidase with copper
    • Rayton, J. K. & Harris, E. D. (1979) Induction of lysyl oxidase with copper. J. Biol. Chem. 254: 621-626.
    • (1979) J. Biol. Chem. , vol.254 , pp. 621-626
    • Rayton, J.K.1    Harris, E.D.2
  • 40
    • 0025830332 scopus 로고
    • Lysyl oxidase-mediated crosslinking in granulation tissue collagen in two models of hyperglycemia
    • Reiser, K. M., Crouch, E. C., Chang, K. & Williamson, J. R. (1991) Lysyl oxidase-mediated crosslinking in granulation tissue collagen in two models of hyperglycemia. Biochim. Biophys. Acta 1097: 55-61.
    • (1991) Biochim. Biophys. Acta , vol.1097 , pp. 55-61
    • Reiser, K.M.1    Crouch, E.C.2    Chang, K.3    Williamson, J.R.4
  • 41
    • 0026643352 scopus 로고
    • Enzymatic and nonenzymatic cross-linking of collagen and elastin
    • Reiser, K., McCormick, R. & Rucker, R. (1992) Enzymatic and nonenzymatic cross-linking of collagen and elastin. FASEB J. 6: 2439-2449.
    • (1992) FASEB J. , vol.6 , pp. 2439-2449
    • Reiser, K.1    McCormick, R.2    Rucker, R.3
  • 42
    • 0025800963 scopus 로고
    • Purification, properties and influence of dietary copper on accumulation and functional activity of lysyl oxidase in rat skin
    • Romero-Chapman, N., Lee, J., Tinker, D., Uriu-Hare, J-Y, Keen, C. L. & Rucker, R. B. (1991) Purification, properties and influence of dietary copper on accumulation and functional activity of lysyl oxidase in rat skin. Biochem. J. 275: 657-662.
    • (1991) Biochem. J. , vol.275 , pp. 657-662
    • Romero-Chapman, N.1    Lee, J.2    Tinker, D.3    Uriu-Hare, J.-Y.4    Keen, C.L.5    Rucker, R.B.6
  • 43
    • 0015321637 scopus 로고
    • Isolation and properties of soluble elastin from copper-deficient chicks
    • Rucker, R. B. & Goettlich-Riemann, W. (1972) Isolation and properties of soluble elastin from copper-deficient chicks. J. Nutr. 102: 563-570.
    • (1972) J. Nutr. , vol.102 , pp. 563-570
    • Rucker, R.B.1    Goettlich-Riemann, W.2
  • 44
    • 0025344739 scopus 로고
    • Purification of lysyl oxidase from piglet skin by selective interaction with Sephacryl S-200
    • Shackleton, D. R .& Hulmes, D. J. S. (1990) Purification of lysyl oxidase from piglet skin by selective interaction with Sephacryl S-200. Biochem. J. 266: 917-919.
    • (1990) Biochem. J. , vol.266 , pp. 917-919
    • Shackleton, D.R.1    Hulmes, D.J.S.2
  • 45
    • 0017138099 scopus 로고
    • Properties of highly purified lysyl oxidase from embryonic chick cartilage
    • Stassen, F. L. H. (1976) Properties of highly purified lysyl oxidase from embryonic chick cartilage. Biochim. Biophys. Acta 438: 49-60.
    • (1976) Biochim. Biophys. Acta , vol.438 , pp. 49-60
    • Stassen, F.L.H.1
  • 48
    • 0026666773 scopus 로고
    • Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor
    • Trackman, P. C., Bedell-Hogan, D., Tang, J. & Kagan, H. M. (1992) Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor. J. Biol. Chem. 267: 8666-8671.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8666-8671
    • Trackman, P.C.1    Bedell-Hogan, D.2    Tang, J.3    Kagan, H.M.4
  • 50
    • 0019831250 scopus 로고
    • Development of peroxidase-coupled fluorometric assay for lysyl oxidase
    • Trackman, P. C., Zoski, C. G. & Kagan, H. M. (1981) Development of peroxidase-coupled fluorometric assay for lysyl oxidase. Anal. Biochem. 113: 336-342.
    • (1981) Anal. Biochem. , vol.113 , pp. 336-342
    • Trackman, P.C.1    Zoski, C.G.2    Kagan, H.M.3
  • 51
    • 0025121968 scopus 로고
    • Synthesis of lysyl oxidase in experimental hepatic fibrosis
    • Wakasaki, H. & Ooshima, A. (1990) Synthesis of lysyl oxidase in experimental hepatic fibrosis. Biochem. Biophys. Res. Commun. 166: 1201-1204.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1201-1204
    • Wakasaki, H.1    Ooshima, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.