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Volumn 34, Issue 2, 2009, Pages 97-104

Expression of prolyl 3-hydroxylase genes in embryonic and adult mouse tissues

Author keywords

3 hydroxyproline; Collagen; Posttranslational modifications; Prolyl hydroxylase

Indexed keywords

ANIMAL EXPERIMENT; ANIMAL TISSUE; AORTA ARCH; ARTICLE; CARTILAGE; EMBRYO; EMBRYONAL TISSUE; GENE; GENE EXPRESSION; HEART; IN SITU HYBRIDIZATION; KIDNEY; LENS CAPSULE; MOUSE; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROLYL 3 HYDROXYLASE 1 GENE; PROLYL 3 HYDROXYLASE 2 GENE; PROLYL 3 HYDROXYLASE 3 GENE; QUANTITATIVE ANALYSIS; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; VERTEBRA BODY;

EID: 70350680484     PISSN: 03867196     EISSN: 13473700     Source Type: Journal    
DOI: 10.1247/csf.09002     Document Type: Article
Times cited : (29)

References (30)
  • 1
    • 33845866114 scopus 로고    scopus 로고
    • Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta
    • Barnes, A.M., Chang, W., Morello, R. 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
  • 2
    • 0036668567 scopus 로고    scopus 로고
    • Quantification of mRNA using real-time reverse transcription PCR (RT-PCR): Trends and problems
    • Bustin, S.A. 2002. Quantification of mRNA using real-time reverse transcription PCR (RT-PCR): trends and problems. J. Mol. Endocrinol., 29: 23-39.
    • (2002) J. Mol. Endocrinol. , vol.29 , pp. 23-39
    • Bustin, S.A.1
  • 3
    • 14044265394 scopus 로고    scopus 로고
    • Pitfalls of quantitative real-time reverse-transcription polymerase chain reaction
    • Bustin, S.A. and Nolan, T. 2004. Pitfalls of quantitative real-time reverse-transcription polymerase chain reaction. J. Biomol. Tech., 15: 155-166.
    • (2004) J. Biomol. Tech. , vol.15 , pp. 155-166
    • Bustin, S.A.1    Nolan, T.2
  • 4
    • 33847321022 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta
    • Cabral, W.A., Chang, W., Barnes, A.M. 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
  • 5
    • 63349103256 scopus 로고    scopus 로고
    • Conservation of notochord gene expression across chordates: Insights from the Leprecan gene family
    • Capellini, T.D., Dunn, M.P., Passamaneck, Y.J., Selleri, L., and Di Gregorio, A. 2008. Conservation of notochord gene expression across chordates: insights from the Leprecan gene family. Genesis, 46: 683-696.
    • (2008) Genesis , vol.46 , pp. 683-696
    • Capellini, T.D.1    Dunn, M.P.2    Passamaneck, Y.J.3    Selleri, L.4    Di Gregorio, A.5
  • 6
    • 0027249799 scopus 로고
    • Loss of Hox-A1 (Hox-1.6) function results in the reorganization of the murine hindbrain
    • Carpenter, E.M., Goddard, J.M., Chisaka, O., Manley, N.R., and Capecchi, M.R. 1993. Loss of Hox-A1 (Hox-1.6) function results in the reorganization of the murine hindbrain. Development, 118: 1063-1075. (Pubitemid 23252397)
    • (1993) Development , vol.118 , Issue.4 , pp. 1063-1075
    • Carpenter, E.M.1    Goddard, J.M.2    Chisaka, O.3    Manley, N.R.4    Capecchi, M.R.5
  • 7
    • 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. 1991. Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development. Development, 111: 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
  • 8
    • 0015895003 scopus 로고
    • The covalent structure of collagen. 2. The amino-acid sequence of alpha1-CB7 from calf-skin collagen
    • Fietzek, P.P., Rexrodt, F.W., Hopper, K.E., and Kühn, K. 1973. The covalent structure of collagen. 2. The amino-acid sequence of alpha1-CB7 from calf-skin collagen. Eur. J. Biochem., 38: 396-400.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 396-400
    • Fietzek, P.P.1    Rexrodt, F.W.2    Hopper, K.E.3    Kühn, K.4
  • 9
    • 0015408717 scopus 로고
    • The covalent structure of collagen: Amino acid sequence of 1-CB3 from calf skin collagen
    • Fietzek, P.P., Wendt, P., Kell, I., and Kühn, K. 1972. The covalent structure of collagen: amino acid sequence of 1-CB3 from calf skin collagen. FEBS Lett., 26: 74-76.
    • (1972) FEBS Lett. , vol.26 , pp. 74-76
    • Fietzek, P.P.1    Wendt, P.2    Kell, I.3    Kühn, K.4
  • 11
    • 0034721088 scopus 로고    scopus 로고
    • Gros1, a potential growth suppressor on chromosome 1: Its identity to basement membrane-associated proteoglycan, leprecan
    • Kaul, S.C., Sugihara, T., Yoshida, A., Nomura, H., and Wadhwa, R. 2000. Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan. Oncogene, 19: 3576-3583. (Pubitemid 30608478)
    • (2000) Oncogene , vol.19 , Issue.32 , pp. 3576-3583
    • Kaul, S.C.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Wadhwa, R.5
  • 12
    • 0015499039 scopus 로고
    • Isolation and characterization of cyanogen bromide peptides from basement membrane collagen
    • Kefalides, N.A. 1972. Isolation and characterization of cyanogen bromide peptides from basement membrane collagen. Biochem. Biophys. Res. Commun., 47: 1151-1158.
    • (1972) Biochem. Biophys. Res. Commun. , vol.47 , pp. 1151-1158
    • Kefalides, N.A.1
  • 13
    • 0015694644 scopus 로고
    • Structure and biosynthesis of basement membranes
    • Kefalides, N.A. 1973. Structure and biosynthesis of basement membranes. Int. Rev. Connect. Tissue Res., 6: 63-104.
    • (1973) Int. Rev. Connect. Tissue Res. , vol.6 , pp. 63-104
    • Kefalides, N.A.1
  • 16
    • 0029030722 scopus 로고
    • The role of Hoxa-3 in mouse thymus and thyroid development
    • Manley, N.R. and Capecchi, M.R. 1995. The role of Hoxa-3 in mouse thymus and thyroid development. Development, 121: 1989-2003.
    • (1995) Development , vol.121 , pp. 1989-2003
    • Manley, N.R.1    Capecchi, M.R.2
  • 17
    • 33750207868 scopus 로고    scopus 로고
    • CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta
    • Morello, R., Bertin, T.K., Chen, Y. 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
  • 18
    • 0032805509 scopus 로고    scopus 로고
    • CDNA cloning, characterization and chromosome mapping of Crtap encoding the mouse cartilage associated protein
    • DOI 10.1016/S0945-053X(99)00002-5, PII S0945053X99000025
    • Morello, R., Tonachini, L., Monticone, M., Viggiano, L., Rocchi, M., Cancedda, R., and Castagnola, P. 1999. cDNA cloning, characterization and chromosome mapping of Crtap encoding the mouse cartilage associated protein. Matrix Biol., 18: 319-324. (Pubitemid 29324746)
    • (1999) Matrix Biology , vol.18 , Issue.3 , pp. 319-324
    • Morello, R.1    Tonachini, L.2    Monticone, M.3    Viggiano, L.4    Rocchi, M.5    Cancedda, R.6    Castagnola, P.7
  • 19
    • 0041669549 scopus 로고    scopus 로고
    • Loss of Bmp7 and Fgf8 signaling in Hoxa 13-mutant mice causes hypospadia
    • Morgan, E.A., Nguyen, S.B., Scott, V., and Stadler, H.S. 2003. Loss of Bmp7 and Fgf8 signaling in Hoxa13-mutant mice causes hypospadia. Development, 130: 3095-3109. (Pubitemid 36926949)
    • (2003) Development , vol.130 , Issue.14 , pp. 3095-3109
    • Morgan, E.A.1    Nguyen, S.B.2    Scott, V.3    Stadler, H.S.4
  • 20
    • 0027420497 scopus 로고
    • Preferential expression of alternatively spliced mRNAs encoding type II procollagen with a cysteine-rich amino-propeptide in differentiating cartilage and nonchondrogenic tissues during early mouse development
    • Ng, L.J., Tam, P.P., and Cheah, K.S. 1993. Preferential expression of alternatively spliced mRNAs encoding type II procollagen with a cysteine-rich amino-propeptide in differentiating cartilage and nonchondrogenic tissues during early mouse development. Dev. Biol., 159: 403-417.
    • (1993) Dev. Biol. , vol.159 , pp. 403-417
    • Ng, L.J.1    Tam, P.P.2    Cheah, K.S.3
  • 22
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • DOI 10.1242/dev.01037
    • Pöschl, E., Schlotzer-Schrehardt, U., Brachvogel, B., Saito, K., Ninomiya, Y., and Mayer, U. 2004. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development, 131: 1619-1628. (Pubitemid 38559288)
    • (2004) Development , vol.131 , Issue.7 , pp. 1619-1628
    • Poschl, E.1    Schlotzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 23
    • 0016827228 scopus 로고
    • The covalent structure of collagen. The chymotrypsin, trypsin and hydroxylamine peptides derived from alpha2-CB4 of calf-skin collagen
    • Rexrodt, F.W., Fietzek, P.P., and Kühn, K. 1975. The covalent structure of collagen. The chymotrypsin, trypsin and hydroxylamine peptides derived from alpha2-CB4 of calf-skin collagen. Eur. J. Biochem., 59: 105-112.
    • (1975) Eur. J. Biochem. , vol.59 , pp. 105-112
    • Rexrodt, F.W.1    Fietzek, P.P.2    Kühn, K.3
  • 24
    • 0017850092 scopus 로고
    • Physicochemical characterization and molecular organization of the collagen a and B chains
    • Rhodes, R.K. and Miller, E.J. 1978. Physicochemical characterization and molecular organization of the collagen A and B chains. Biochemistry, 17: 3442-3448. (Pubitemid 8405365)
    • (1978) Biochemistry , vol.17 , Issue.17 , pp. 3442-3448
    • Rhodes, R.K.1    Miller, E.J.2
  • 25
    • 0035136701 scopus 로고    scopus 로고
    • Stage-and tissue-specific expression of a Col2a1-Cre fusion gene in transgenic mice
    • DOI 10.1016/S0945-053X(00)00122-0, PII S0945053X00001220
    • Sakai, K., Hiripi, L., Glumoff, V., Brandau, O., Eerola, R., Vuorio, E., Bösze, Z., Fässler, R., and Aszódi, A. 2001. Stage-and tissue-specific expression of a Col2a1-Cre fusion gene in transgenic mice. Matrix Biol., 19: 761-767. (Pubitemid 32153833)
    • (2001) Matrix Biology , vol.19 , Issue.8 , pp. 761-767
    • Sakai, K.1    Hiripi, L.2    Glumoff, V.3    Brandau, O.4    Eerola, R.5    Vuorio, E.6    Bosze, Z.7    Fassler, R.8    Aszodi, A.9
  • 26
    • 33644891305 scopus 로고    scopus 로고
    • Developmental expression profiles of Xenopus laevis reference genes
    • Sindelka, R., Ferjentsik, Z., and Jonak, J. 2006. Developmental expression profiles of Xenopus laevis reference genes. Dev. Dyn., 235: 754-758.
    • (2006) Dev. Dyn. , vol.235 , pp. 754-758
    • Sindelka, R.1    Ferjentsik, Z.2    Jonak, J.3
  • 27
    • 50349089712 scopus 로고    scopus 로고
    • Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV
    • Tiainen, P., Pasanen, A., Sormunen, R., and Myllyharju, J. 2008. Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV. J. Biol. Chem., 283: 19432-19439.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19432-19439
    • Tiainen, P.1    Pasanen, A.2    Sormunen, R.3    Myllyharju, J.4
  • 28
    • 0033384624 scopus 로고    scopus 로고
    • CDNA cloning, characterization and chromosome mapping of the gene encoding human cartilage associated protein (CRTAP)
    • Tonachini, L., Morello, R., Monticone, M., Skaug, J., Scherer, S.W., Cancedda, R., and Castagnola, P. 1999. cDNA cloning, characterization and chromosome mapping of the gene encoding human cartilage associated protein (CRTAP). Cytogenet. Cell Genet., 87: 191-194. (Pubitemid 30103085)
    • (1999) Cytogenetics and Cell Genetics , vol.87 , Issue.3-4 , pp. 191-194
    • Tonachini, L.1    Morello, R.2    Monticone, M.3    Skaug, J.4    Scherer, S.W.5    Cancedda, R.6    Castagnola, P.7
  • 29
    • 2542497037 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
    • Vranka, J.A., Sakai, L.Y., and Bächinger, H.P. 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    Bächinger, H.P.3
  • 30
    • 65949109910 scopus 로고    scopus 로고
    • Recessive Osteogenesis Imperfecta caused by LEPRE1 mutations: Clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation
    • Willaert, A., Malfait, F., Symoens, S., Gevaert, K., Kayserili, H., Megarbane, A., Mortier, G., Leroy, J.G., Coucke, P.J., and De Paepe, A. 2008. Recessive Osteogenesis Imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation. J. Med. Genet., 46: 233-241.
    • (2008) J. Med. Genet. , vol.46 , pp. 233-241
    • Willaert, A.1    Malfait, F.2    Symoens, S.3    Gevaert, K.4    Kayserili, H.5    Megarbane, A.6    Mortier, G.7    Leroy, J.G.8    Coucke, P.J.9    De Paepe, A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.