메뉴 건너뛰기




Volumn 25, Issue 8, 2006, Pages 475-483

The lysyl hydroxylase isoforms are widely expressed during mouse embryogenesis, but obtain tissue- and cell-specific patterns in the adult

Author keywords

Collagen biosynthesis; Hydroxylysine; Lysyl hydroxylase

Indexed keywords

ISOENZYME; LYSYL HYDROXYLASE 1; LYSYL HYDROXYLASE 2; LYSYL HYDROXYLASE 3; PROCOLLAGEN LYSINE 2 OXOGLUTARATE 5 DIOXYGENASE; UNCLASSIFIED DRUG;

EID: 33750976345     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2006.08.260     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 0028851516 scopus 로고
    • Rat lysyl hydroxylase: molecular cloning, mRNA distribution and expression in a baculovirus system
    • Armstrong L.C., and Last J.A. Rat lysyl hydroxylase: molecular cloning, mRNA distribution and expression in a baculovirus system. Biochim. Biophys. Acta 1264 (1995) 93-102
    • (1995) Biochim. Biophys. Acta , vol.1264 , pp. 93-102
    • Armstrong, L.C.1    Last, J.A.2
  • 2
    • 0001843220 scopus 로고
    • Collagen superfamily
    • Comper W.D. (Ed), Harwood Academic Publishers, Amsterdam, The Netherlands
    • Bateman J.F., Lamande S.R., and Ramshaw J.A.M. Collagen superfamily. In: Comper W.D. (Ed). Extracellular Matrix (1995), Harwood Academic Publishers, Amsterdam, The Netherlands 22-67
    • (1995) Extracellular Matrix , pp. 22-67
    • Bateman, J.F.1    Lamande, S.R.2    Ramshaw, J.A.M.3
  • 3
    • 26644440414 scopus 로고    scopus 로고
    • Interleukin 4 and prolonged hypoxia induce a higher gene expression of lysyl hydroxylase 2 and an altered cross-link pattern: important pathogenetic steps in early and late stage of systemic scleroderma?
    • Brinckmann J., Kim S., Wu J., Reinhardt D.P., Batmunkh C., Metzen E., Notbohm H., Bank R.A., Krieg T., and Hunzelmann N. Interleukin 4 and prolonged hypoxia induce a higher gene expression of lysyl hydroxylase 2 and an altered cross-link pattern: important pathogenetic steps in early and late stage of systemic scleroderma?. Matrix Biol. 24 (2005) 459-468
    • (2005) Matrix Biol. , vol.24 , pp. 459-468
    • Brinckmann, J.1    Kim, S.2    Wu, J.3    Reinhardt, D.P.4    Batmunkh, C.5    Metzen, E.6    Notbohm, H.7    Bank, R.A.8    Krieg, T.9    Hunzelmann, N.10
  • 4
    • 0000838834 scopus 로고    scopus 로고
    • Disorders of collagen biosynthesis and structure
    • Scriver C.R., et al. (Ed), McGraw-Hill
    • Byers P.H. Disorders of collagen biosynthesis and structure. In: Scriver C.R., et al. (Ed). The Metabolic and Molecular Bases of Inherited Disease (2001), McGraw-Hill
    • (2001) The Metabolic and Molecular Bases of Inherited Disease
    • Byers, P.H.1
  • 5
    • 0025732094 scopus 로고
    • Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development
    • Cheah K.S., Lau E.T., Au P.K., and Tam P.P. Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development. Development 111 (1991) 945-953
    • (1991) Development , vol.111 , pp. 945-953
    • Cheah, K.S.1    Lau, E.T.2    Au, P.K.3    Tam, P.P.4
  • 6
    • 0030218990 scopus 로고    scopus 로고
    • Deposition of collagen VI in the extracellular matrix during mouse embryogenesis correlates with expression of the alpha 3(VI) subunit gene
    • Dziadek M., Darling P., Bakker M., Overall M., Zhang R.Z., Pan T.C., Tillet E., Timpl R., and Chu M.L. Deposition of collagen VI in the extracellular matrix during mouse embryogenesis correlates with expression of the alpha 3(VI) subunit gene. Exp. Cell Res. 226 (1996) 302-315
    • (1996) Exp. Cell Res. , vol.226 , pp. 302-315
    • Dziadek, M.1    Darling, P.2    Bakker, M.3    Overall, M.4    Zhang, R.Z.5    Pan, T.C.6    Tillet, E.7    Timpl, R.8    Chu, M.L.9
  • 7
    • 33748854428 scopus 로고    scopus 로고
    • Collagen cross-links
    • Eyre D.R., and Wu J.-J. Collagen cross-links. Top. Curr. Chem. 247 (2005) 207-229
    • (2005) Top. Curr. Chem. , vol.247 , pp. 207-229
    • Eyre, D.R.1    Wu, J.-J.2
  • 8
    • 0026507897 scopus 로고
    • Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2
    • Hautala T., Byers M.G., Eddy R.L., Shows T.B., Kivirikko K.I., and Myllylä R. Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2. Genomics 13 (1992) 62-69
    • (1992) Genomics , vol.13 , pp. 62-69
    • Hautala, T.1    Byers, M.G.2    Eddy, R.L.3    Shows, T.B.4    Kivirikko, K.I.5    Myllylä, R.6
  • 9
    • 0027535453 scopus 로고
    • A large duplication in the gene for lysyl hydroxylase accounts for the type VI variant of Ehlers-Danlos syndrome in two siblings
    • Hautala T., Heikkinen J., Kivirikko K.I., and Myllyla R. A large duplication in the gene for lysyl hydroxylase accounts for the type VI variant of Ehlers-Danlos syndrome in two siblings. Genomics 15 (1993) 399-404
    • (1993) Genomics , vol.15 , pp. 399-404
    • Hautala, T.1    Heikkinen, J.2    Kivirikko, K.I.3    Myllyla, R.4
  • 10
    • 9644303423 scopus 로고    scopus 로고
    • Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2
    • Ha-Vinh R., Alanay Y., Bank R.A., Campos-Xavier A.B., Zankl A., Superti-Furga A., and Bonafe L. Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2. Am. J. Med. Genet. 131A (2004) 115-120
    • (2004) Am. J. Med. Genet. , vol.131 A , pp. 115-120
    • Ha-Vinh, R.1    Alanay, Y.2    Bank, R.A.3    Campos-Xavier, A.B.4    Zankl, A.5    Superti-Furga, A.6    Bonafe, L.7
  • 11
    • 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., Valtavaara M., and Myllylä R. Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J. Biol. Chem. 275 (2000) 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    Valtavaara, M.6    Myllylä, R.7
  • 12
    • 0028679665 scopus 로고
    • Extracellular matrix: 1. Fibril-forming collagens
    • Kadler K. Extracellular matrix: 1. Fibril-forming collagens. Protein Profile 1 (1994) 519-638
    • (1994) Protein Profile , vol.1 , pp. 519-638
    • Kadler, K.1
  • 13
    • 0027943512 scopus 로고
    • Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum
    • Kellokumpu S., Sormunen R., Heikkinen J., and Myllylä R. Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum. J. Biol. Chem. 269 (1994) 30524-30529
    • (1994) J. Biol. Chem. , vol.269 , pp. 30524-30529
    • Kellokumpu, S.1    Sormunen, R.2    Heikkinen, J.3    Myllylä, R.4
  • 14
    • 0002097152 scopus 로고
    • Collagen: the collagen family: structure, assembly, and organization in the extracellular matrix
    • Royce P.M., et al. (Ed), Wiley-Liss, New York
    • Kielty C.M., Hopkinson I., and Grant M.E. Collagen: the collagen family: structure, assembly, and organization in the extracellular matrix. In: Royce P.M., et al. (Ed). Connective Tissue and Its Heritable Disorders (1993), Wiley-Liss, New York 103-147
    • (1993) Connective Tissue and Its Heritable Disorders , pp. 103-147
    • Kielty, C.M.1    Hopkinson, I.2    Grant, M.E.3
  • 15
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • Harding J.J., et al. (Ed), CRC Press, Inc., Boca Raton, FL
    • Kivirikko K.I., Myllylä R., and Pihlajaniemi T. Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In: Harding J.J., et al. (Ed). Post-translational Modifications of Proteins (1992), CRC Press, Inc., Boca Raton, FL 1-51
    • (1992) Post-translational Modifications of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 16
    • 0018849399 scopus 로고
    • Appearance and distribution of collagens and laminin in the early mouse embryo
    • Leivo I., Vaheri A., Timpl R., and Wartiovaara J. Appearance and distribution of collagens and laminin in the early mouse embryo. Dev. Biol. 76 (1980) 100-114
    • (1980) Dev. Biol. , vol.76 , pp. 100-114
    • Leivo, I.1    Vaheri, A.2    Timpl, R.3    Wartiovaara, J.4
  • 17
    • 0038106229 scopus 로고    scopus 로고
    • Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms
    • Mercer D.K., Nicol P.F., Kimbembe C., and Robins S.P. 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
  • 20
    • 0025764613 scopus 로고
    • Recycling of proteins between the endoplasmic reticulum and Golgi complex
    • Pelham H.R. Recycling of proteins between the endoplasmic reticulum and Golgi complex. Curr. Opin. Cell Biol. 3 (1991) 585-591
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 585-591
    • Pelham, H.R.1
  • 21
    • 21644439471 scopus 로고    scopus 로고
    • Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization
    • Pornprasertsuk S., Duarte W.R., Mochida Y., and Yamauchi M. Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization. J. Bone Miner. Res. 20 (2005) 81-87
    • (2005) J. Bone Miner. Res. , vol.20 , pp. 81-87
    • Pornprasertsuk, S.1    Duarte, W.R.2    Mochida, Y.3    Yamauchi, M.4
  • 22
    • 0029006974 scopus 로고
    • Collagens: molecular biology, diseases, and potentials for therapy
    • Prockop D.J., and Kivirikko K.I. Collagens: molecular biology, diseases, and potentials for therapy. Ann. Rev. Biochem. 64 (1995) 403-434
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 23
    • 0024546078 scopus 로고
    • Peptide production from proteins separated by sodium dodecyl-sulfate polyacrylamide gel electrophoresis
    • Prussak C.E., Almazan M.T., and Tseng B.Y. Peptide production from proteins separated by sodium dodecyl-sulfate polyacrylamide gel electrophoresis. Anal. Biochem. 178 (1989) 233-238
    • (1989) Anal. Biochem. , vol.178 , pp. 233-238
    • Prussak, C.E.1    Almazan, M.T.2    Tseng, B.Y.3
  • 25
    • 4444245754 scopus 로고    scopus 로고
    • Characterization of collagenous peptides bound to lysyl hydroxylase isoforms
    • Risteli M., Niemitalo O., Lankinen H., Juffer A.H., and Myllylä R. Characterization of collagenous peptides bound to lysyl hydroxylase isoforms. J. Biol. Chem. 279 (2004) 37535-37543
    • (2004) J. Biol. Chem. , vol.279 , pp. 37535-37543
    • Risteli, M.1    Niemitalo, O.2    Lankinen, H.3    Juffer, A.H.4    Myllylä, R.5
  • 26
    • 84882491717 scopus 로고    scopus 로고
    • Collagen cross-linking and metabolism
    • Academic Press
    • Robins S.P., and Brady J.D. Collagen cross-linking and metabolism. Principles of Bone Biology vol. 1 (2002), Academic Press
    • (2002) Principles of Bone Biology , vol.1
    • Robins, S.P.1    Brady, J.D.2
  • 27
    • 0032808005 scopus 로고    scopus 로고
    • Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse
    • Ruotsalainen H., Sipilä L., Kerkelä E., Pospiech H., and Myllylä R. Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their phylogenetic analysis and tissue-specific expression in the mouse. Matrix Biol. 18 (1999) 325-329
    • (1999) Matrix Biol. , vol.18 , pp. 325-329
    • Ruotsalainen, H.1    Sipilä, L.2    Kerkelä, E.3    Pospiech, H.4    Myllylä, R.5
  • 28
    • 0035033415 scopus 로고    scopus 로고
    • Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase
    • Ruotsalainen H., Vanhatupa S., Tampio M., Sipilä L., Valtavaara M., and Myllylä R. Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase. Matrix Biol. 20 (2001) 137-146
    • (2001) Matrix Biol. , vol.20 , pp. 137-146
    • Ruotsalainen, H.1    Vanhatupa, S.2    Tampio, M.3    Sipilä, L.4    Valtavaara, M.5    Myllylä, R.6
  • 31
    • 33646848764 scopus 로고    scopus 로고
    • The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration
    • Schneider V.A., and Granato M. The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration. Neuron 50 (2006) 683-695
    • (2006) Neuron , vol.50 , pp. 683-695
    • Schneider, V.A.1    Granato, M.2
  • 32
    • 0021806048 scopus 로고
    • A new method of preparing gold probes for multiple-labeling cytochemistry
    • Slot J.W., and Geuze H.J. A new method of preparing gold probes for multiple-labeling cytochemistry. Eur. J. Cell Biol. 38 (1985) 87-93
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 34
    • 0034625345 scopus 로고    scopus 로고
    • A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum
    • Suokas M., Myllylä R., and Kellokumpu S. A single C-terminal peptide segment mediates both membrane association and localization of lysyl hydroxylase in the endoplasmic reticulum. J. Biol. Chem. 275 (2000) 17863-17868
    • (2000) J. Biol. Chem. , vol.275 , pp. 17863-17868
    • Suokas, M.1    Myllylä, R.2    Kellokumpu, S.3
  • 35
    • 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 W.J., Nishiura T., Kuznetsov S.A., Robey P.G., Brenner D.A., and Yamauchi M. 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
  • 36
    • 13444309266 scopus 로고    scopus 로고
    • Tissue-specific expression and regulation of the alternatively-spliced forms of lysyl hydroxylase 2 (LH2) in human kidney cells and skin fibroblasts
    • Walker L.C., Overstreet M.A., and Yeowell H.N. Tissue-specific expression and regulation of the alternatively-spliced forms of lysyl hydroxylase 2 (LH2) in human kidney cells and skin fibroblasts. Matrix Biol. 23 (2005) 515-523
    • (2005) Matrix Biol. , vol.23 , pp. 515-523
    • Walker, L.C.1    Overstreet, M.A.2    Yeowell, H.N.3
  • 37
    • 33751017427 scopus 로고    scopus 로고
    • Oulu University Press, Oulu Acta Universitatis Ouluensis A334
    • Valtavaara M. Novel Lysyl Hydroxylase Isoforms (1999), Oulu University Press, Oulu Acta Universitatis Ouluensis A334
    • (1999) Novel Lysyl Hydroxylase Isoforms
    • Valtavaara, M.1
  • 38
    • 0030972003 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle
    • Valtavaara M., Papponen H., Pirttilä A.M., Hiltunen K., Helander H., and Myllylä R. Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J. Biol. Chem. 272 (1997) 6831-6834
    • (1997) J. Biol. Chem. , vol.272 , pp. 6831-6834
    • Valtavaara, M.1    Papponen, H.2    Pirttilä, A.M.3    Hiltunen, K.4    Helander, H.5    Myllylä, R.6
  • 39
    • 0032557436 scopus 로고    scopus 로고
    • Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3)
    • Valtavaara M., Szpirer C., Szpirer J., and Myllylä R. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3). J. Biol. Chem. 273 (1998) 12881-12886
    • (1998) J. Biol. Chem. , vol.273 , pp. 12881-12886
    • Valtavaara, M.1    Szpirer, C.2    Szpirer, J.3    Myllylä, R.4
  • 43
    • 0036861267 scopus 로고    scopus 로고
    • The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro
    • Wang C., Luosujärvi H., Heikkinen J., Risteli M., Uitto L., and Myllylä R. The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. Matrix Biol. 21 (2002) 559-566
    • (2002) Matrix Biol. , vol.21 , pp. 559-566
    • Wang, C.1    Luosujärvi, H.2    Heikkinen, J.3    Risteli, M.4    Uitto, L.5    Myllylä, R.6
  • 44
    • 0034104470 scopus 로고    scopus 로고
    • Lack of collagen type specificity for lysyl hydroxylase isoforms
    • Wang C., Valtavaara M., and Myllylä R. Lack of collagen type specificity for lysyl hydroxylase isoforms. DNA Cell Biol. 19 (2000) 71-77
    • (2000) DNA Cell Biol. , vol.19 , pp. 71-77
    • Wang, C.1    Valtavaara, M.2    Myllylä, R.3
  • 45
    • 0033844260 scopus 로고    scopus 로고
    • Collagen structure regulates fibril mineralization in osteogenesis as revealed by cross-link patterns in calcifying callus
    • Wassen M.H., Lammens J., Tekoppele J.M., Sakkers R.J., Liu Z., Verbout A.J., and Bank R.A. Collagen structure regulates fibril mineralization in osteogenesis as revealed by cross-link patterns in calcifying callus. J. Bone Miner. Res. 15 (2000) 1776-1785
    • (2000) J. Bone Miner. Res. , vol.15 , pp. 1776-1785
    • Wassen, M.H.1    Lammens, J.2    Tekoppele, J.M.3    Sakkers, R.J.4    Liu, Z.5    Verbout, A.J.6    Bank, R.A.7
  • 48
    • 0032940558 scopus 로고    scopus 로고
    • Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene
    • Yeowell H.N., and Walker L.C. Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 18 (1999) 179-187
    • (1999) Matrix Biol. , vol.18 , pp. 179-187
    • Yeowell, H.N.1    Walker, L.C.2
  • 49
    • 0033812976 scopus 로고    scopus 로고
    • Mutations in the lysyl hydroxylase 1 gene that result in enzyme deficiency and the clinical phenotype of Ehlers-Danlos syndrome type VI
    • Yeowell H.N., and Walker L.C. Mutations in the lysyl hydroxylase 1 gene that result in enzyme deficiency and the clinical phenotype of Ehlers-Danlos syndrome type VI. Mol. Genet. Metab. 71 (2000) 212-224
    • (2000) Mol. Genet. Metab. , vol.71 , pp. 212-224
    • Yeowell, H.N.1    Walker, L.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.