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Volumn 327, Issue 4, 2005, Pages 1042-1046

Expression of lysyl oxidase isoforms in MC3T3-E1 osteoblastic cells

Author keywords

Collagen; Collagen cross linking; Lysyl oxidase; Lysyl oxidase like proteins; Matrix mineralization; MC3T3 E1 cells

Indexed keywords

ISOENZYME; MESSENGER RNA; PROTEIN LYSINE 6 OXIDASE;

EID: 12344289271     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.12.119     Document Type: Article
Times cited : (33)

References (31)
  • 1
    • 0038104439 scopus 로고    scopus 로고
    • Collagen biochemistry: An overview
    • M. Yamauchi Collagen biochemistry: an overview Adv. Tissue Bank. 6 2002 445 500
    • (2002) Adv. Tissue Bank. , vol.6 , pp. 445-500
    • Yamauchi, M.1
  • 2
    • 0024214253 scopus 로고
    • Cross-linking and new bone collagen synthesis in immobilized and recovering primate osteoporosis
    • M. Yamauchi, D.R. Young, G.S. Chandler, and G.L. Mechanic Cross-linking and new bone collagen synthesis in immobilized and recovering primate osteoporosis Bone 9 1988 415 418
    • (1988) Bone , vol.9 , pp. 415-418
    • Yamauchi, M.1    Young, D.R.2    Chandler, G.S.3    Mechanic, G.L.4
  • 3
    • 0026536702 scopus 로고
    • Cross-linking connectivity in bone collagen fibrils: The COOH-terminal locus of free aldehyde
    • K. Otsubo, E.P. Katz, G.L. Mechanic, and M. Yamauchi Cross-linking connectivity in bone collagen fibrils: the COOH-terminal locus of free aldehyde Biochemistry 31 1992 396 402
    • (1992) Biochemistry , vol.31 , pp. 396-402
    • Otsubo, K.1    Katz, E.P.2    Mechanic, G.L.3    Yamauchi, M.4
  • 4
    • 0027353094 scopus 로고
    • The post-translational chemistry and molecular packing of mineralizing tendon collagens
    • M. Yamauchi, and E.P. Katz The post-translational chemistry and molecular packing of mineralizing tendon collagens Connect. Tissue Res. 29 1993 81 98
    • (1993) Connect. Tissue Res. , vol.29 , pp. 81-98
    • Yamauchi, M.1    Katz, E.P.2
  • 7
    • 0031081115 scopus 로고    scopus 로고
    • Alteration of mineral crystallinity and collagen cross-linking of bones in osteopetrotic toothless (tl/tl) rats and their improvement after treatment with colony stimulating factor-1
    • A. Wojtowicz, A. Dziedzic-Goclawska, A. Kaminski, W. Stachowicz, K. Wojtowicz, S.C. Marks Jr., and M. Yamauchi Alteration of mineral crystallinity and collagen cross-linking of bones in osteopetrotic toothless (tl/tl) rats and their improvement after treatment with colony stimulating factor-1 Bone 20 1997 127 132
    • (1997) Bone , vol.20 , pp. 127-132
    • Wojtowicz, A.1    Dziedzic-Goclawska, A.2    Kaminski, A.3    Stachowicz, W.4    Wojtowicz, K.5    Marks Jr., S.C.6    Yamauchi, M.7
  • 8
    • 0032032089 scopus 로고    scopus 로고
    • Collagen cross-links in mineralizing tissues: A review of their chemistry, function, and clinical relevance
    • L. Knott, and A.J. Bailey Collagen cross-links in mineralizing tissues: a review of their chemistry, function, and clinical relevance Bone 22 1998 181 187
    • (1998) Bone , vol.22 , pp. 181-187
    • Knott, L.1    Bailey, A.J.2
  • 9
    • 12344299783 scopus 로고    scopus 로고
    • Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells
    • S. Pornprasertsuk, W.R. Duarte, Y. Mochida, and M. Yamauchi Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells J. Bone Miner. Res. 19 2004 1349 1355
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 1349-1355
    • Pornprasertsuk, S.1    Duarte, W.R.2    Mochida, Y.3    Yamauchi, M.4
  • 10
    • 21644439471 scopus 로고    scopus 로고
    • Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization
    • in press
    • S. Pornprasertsuk, W.R. Duarte, Y. Mochida, M. Yamauchi, Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization, J. Bone Miner. Res. (2005), in press
    • (2005) J. Bone Miner. Res.
    • Pornprasertsuk, S.1    Duarte, W.R.2    Mochida, Y.3    Yamauchi, M.4
  • 11
    • 0014940673 scopus 로고
    • Cross-linking of collagen and elastin. Properties of lysyl oxidase
    • R.C. Siegel, S.R. Pinnell, and G.R. Martin Cross-linking of collagen and elastin. Properties of lysyl oxidase Biochemistry 9 1970 4486 4492
    • (1970) Biochemistry , vol.9 , pp. 4486-4492
    • Siegel, R.C.1    Pinnell, S.R.2    Martin, G.R.3
  • 12
    • 0037371153 scopus 로고    scopus 로고
    • Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell
    • H.M. Kagan, and W. Li Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell J. Cell. Biochem. 88 2003 660 672
    • (2003) J. Cell. Biochem. , vol.88 , pp. 660-672
    • Kagan, H.M.1    Li, W.2
  • 14
    • 85053589021 scopus 로고
    • Cross-linking of collagen
    • M. Nimni CRC Press Florida
    • M. Yamauchi, and G. Mechanic Cross-linking of collagen M. Nimni Collagen 1988 CRC Press Florida 157 172
    • (1988) Collagen , pp. 157-172
    • Yamauchi, M.1    Mechanic, G.2
  • 15
    • 0035374511 scopus 로고    scopus 로고
    • Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent
    • J.D. Brady, and S.P. Robins Structural characterization of pyrrolic cross-links in collagen using a biotinylated Ehrlich's reagent J. Biol. Chem. 276 2001 18812 18818
    • (2001) J. Biol. Chem. , vol.276 , pp. 18812-18818
    • Brady, J.D.1    Robins, S.P.2
  • 16
    • 0030888680 scopus 로고    scopus 로고
    • Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence
    • H. Saito, J. Papaconstantinou, H. Sato, and S. Goldstein Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence J. Biol. Chem. 272 1997 8157 8160
    • (1997) J. Biol. Chem. , vol.272 , pp. 8157-8160
    • Saito, H.1    Papaconstantinou, J.2    Sato, H.3    Goldstein, S.4
  • 17
    • 0027178650 scopus 로고
    • A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25
    • K. Kenyon, W.S. Modi, S. Contente, and R.M. Friedman A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25 J. Biol. Chem. 268 1993 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
  • 19
    • 0035968314 scopus 로고    scopus 로고
    • Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage
    • H. Ito, H. Akiyama, H. Iguchi, K. Iyama, M. Miyamoto, K. Ohsawa, and T. Nakamura Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage J. Biol. Chem. 276 2001 24023 24029
    • (2001) J. Biol. Chem. , vol.276 , pp. 24023-24029
    • Ito, H.1    Akiyama, H.2    Iguchi, H.3    Iyama, K.4    Miyamoto, M.5    Ohsawa, K.6    Nakamura, T.7
  • 20
    • 0035368087 scopus 로고    scopus 로고
    • Central nervous system, uterus, heart, and leukocyte expression of the LOXL3 gene, encoding a novel lysyl oxidase-like protein
    • C. Jourdan-Le Saux, A. Tomsche, A. Ujfalusi, L. Jia, and K. Csiszar Central nervous system, uterus, heart, and leukocyte expression of the LOXL3 gene, encoding a novel lysyl oxidase-like protein Genomics 74 2001 211 218
    • (2001) Genomics , vol.74 , pp. 211-218
    • Jourdan-Le Saux, C.1    Tomsche, A.2    Ujfalusi, A.3    Jia, L.4    Csiszar, K.5
  • 21
    • 0035871036 scopus 로고    scopus 로고
    • Cloning and characterization of a fourth human lysyl oxidase isoenzyme
    • J.M. Maki, and K.I. Kivirikko Cloning and characterization of a fourth human lysyl oxidase isoenzyme Biochem. J. 355 2001 381 387
    • (2001) Biochem. J. , vol.355 , pp. 381-387
    • Maki, J.M.1    Kivirikko, K.I.2
  • 22
    • 0034751557 scopus 로고    scopus 로고
    • Cloning and characterization of a fifth human lysyl oxidase isoenzyme: The third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains
    • J.M. Maki, H. Tikkanen, and K.I. Kivirikko Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains Matrix Biol. 20 2001 493 496
    • (2001) Matrix Biol. , vol.20 , pp. 493-496
    • Maki, J.M.1    Tikkanen, H.2    Kivirikko, K.I.3
  • 23
    • 0034749471 scopus 로고    scopus 로고
    • A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain
    • L. Asuncion, B. Fogelgren, K.S. Fong, S.F. Fong, Y. Kim, and K. Csiszar A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain Matrix Biol. 20 2001 487 491
    • (2001) Matrix Biol. , vol.20 , pp. 487-491
    • Asuncion, L.1    Fogelgren, B.2    Fong, K.S.3    Fong, S.F.4    Kim, Y.5    Csiszar, K.6
  • 24
    • 0032983542 scopus 로고    scopus 로고
    • Isolation and characterization of MC3T3-E1 preosteoblast subclones with distinct in vitro and in vivo differentiation/mineralization potential
    • D. Wang, K. Christensen, K. Chawla, G. Xiao, P.H. Krebsbach, and R.T. Franceschi Isolation and characterization of MC3T3-E1 preosteoblast subclones with distinct in vitro and in vivo differentiation/mineralization potential J. Bone Miner. Res. 14 1999 893 903
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 893-903
    • Wang, D.1    Christensen, K.2    Chawla, K.3    Xiao, G.4    Krebsbach, P.H.5    Franceschi, R.T.6
  • 25
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Δ Δ C(T)) method
    • K.J. Livak, and T.D. Schmittgen Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Δ Δ C(T)) method Methods 25 2001 402 408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 26
    • 0029960037 scopus 로고    scopus 로고
    • Regulation of lysyl oxidase by basic fibroblast growth factor in osteoblastic MC3T3-E1 cells
    • J.F. Eduardo, M.B. Gabriel, and P. Trackman Regulation of lysyl oxidase by basic fibroblast growth factor in osteoblastic MC3T3-E1 cells J. Biol. Chem. 271 1996 6411 6416
    • (1996) J. Biol. Chem. , vol.271 , pp. 6411-6416
    • Eduardo, J.F.1    Gabriel, M.B.2    Trackman, P.3
  • 27
    • 0347910356 scopus 로고
    • Pre- and post-translation regulation of lysyl oxidase by transforming growth factor-b1 in osteoblast MC3T3-E1 cells
    • J.F. Eduardo, J.C. Young, H.T. Xiaoyan, T. Takala, and P. Trackman Pre- and post-translation regulation of lysyl oxidase by transforming growth factor-b1 in osteoblast MC3T3-E1 cells J. Biol. Chem. 270 1995 30797 30803
    • (1995) J. Biol. Chem. , vol.270 , pp. 30797-30803
    • Eduardo, J.F.1    Young, J.C.2    Xiaoyan, H.T.3    Takala, T.4    Trackman, P.5
  • 29
    • 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
    • K. Uzawa, W.J. Grzesik, T. Nishiura, S.A. Kuznetsov, P.G. Robey, D.A. Brenner, and M. Yamauchi 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 1999 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    Brenner, D.A.6    Yamauchi, M.7
  • 31
    • 0038106229 scopus 로고    scopus 로고
    • Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms
    • D.K. Mercer, P.F. Nicol, C. Kimbembe, and S.P. Robins Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms Biochem. Biophys. Res. Commun. 307 2003 803 809
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 803-809
    • Mercer, D.K.1    Nicol, P.F.2    Kimbembe, C.3    Robins, S.P.4


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