메뉴 건너뛰기




Volumn 20, Issue 11, 2000, Pages 4084-4093

Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROCOLLAGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE;

EID: 0034111331     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.11.4084-4093.2000     Document Type: Article
Times cited : (96)

References (38)
  • 1
    • 0030807022 scopus 로고    scopus 로고
    • Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer - The alpha(I) and alpha(II) subunits do not form a mixed alpha(I) alpha(II)beta(2) tetramer
    • Annunen, P., T. Helaakoski, J. Myllyharju, J. Veijola, T. Pihlajaniemi, and K. I. Kivirikko. 1997. Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer - the alpha(I) and alpha(II) subunits do not form a mixed alpha(I) alpha(II)beta(2) tetramer. J. Biol. Chem. 272:17342-17348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17342-17348
    • Annunen, P.1    Helaakoski, T.2    Myllyharju, J.3    Veijola, J.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 2
    • 0033525689 scopus 로고    scopus 로고
    • Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties
    • Annunen, P., P. Koivunen, and K. I. Kivirikko. 1999. Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties. J. Biol. Chem. 274:6790-6796.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6790-6796
    • Annunen, P.1    Koivunen, P.2    Kivirikko, K.I.3
  • 3
    • 0025187795 scopus 로고
    • Properties of a class of genes required for ray morphogenesis in Caenorhabditis elegans
    • Baird, S. E., and S. W. Emmons. 1990. Properties of a class of genes required for ray morphogenesis in Caenorhabditis elegans. Genetics 126:335-344.
    • (1990) Genetics , vol.126 , pp. 335-344
    • Baird, S.E.1    Emmons, S.W.2
  • 4
    • 0024469811 scopus 로고
    • Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II
    • Bird, D. M., and D. L. Riddle. 1989. Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II. Mol. Cell. Biol. 9:4119-4130.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4119-4130
    • Bird, D.M.1    Riddle, D.L.2
  • 5
    • 0033542457 scopus 로고    scopus 로고
    • Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans
    • Blelloch, R., and J. Kimble. 1999. Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans. Nature 399:586-590.
    • (1999) Nature , vol.399 , pp. 586-590
    • Blelloch, R.1    Kimble, J.2
  • 6
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. 1974. The genetics of Caenorhabditis elegans. Genetics 77:71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 7
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • C. elegans Genome Consortium. 1998. Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282:2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 8
    • 0019596981 scopus 로고
    • Cuticle of Caenorhabditis elegans: Its isolation and partial characterisation
    • Cox, G. N., M. Kusch, and R. S. Edgar. 1981. Cuticle of Caenorhabditis elegans: its isolation and partial characterisation. J. Cell Biol. 90:7-17.
    • (1981) J. Cell Biol. , vol.90 , pp. 7-17
    • Cox, G.N.1    Kusch, M.2    Edgar, R.S.3
  • 9
    • 0032512878 scopus 로고    scopus 로고
    • The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency
    • Darby, N. J., E. Penka, and R. Vincentelli. 1998. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J. Mol. Biol. 276:239-247.
    • (1998) J. Mol. Biol. , vol.276 , pp. 239-247
    • Darby, N.J.1    Penka, E.2    Vincentelli, R.3
  • 10
    • 0025002190 scopus 로고
    • A modular set of lacZ fusion vectors for studying gene expression in Caenorhabditis elegans
    • Fire, A., S. White Harrison, and D. Dixon. 1990. A modular set of lacZ fusion vectors for studying gene expression in Caenorhabditis elegans. Gene 93:189-198.
    • (1990) Gene , vol.93 , pp. 189-198
    • Fire, A.1    White Harrison, S.2    Dixon, D.3
  • 11
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire, A., S. Xu, M. K. Montgomery, S. A. Kostas, S. E. Driver, and C. C. Mello. 1998. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391:806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 12
    • 0030612084 scopus 로고    scopus 로고
    • Characterization of alpha 1(IV) collagen mutations in Caenorhabditis elegans and the effects of alpha 1 and alpha 2(IV) mutations on type IV collagen distribution
    • Gupta, M., P. Graham, and J. M. Kramer. 1997. Characterization of alpha 1(IV) collagen mutations in Caenorhabditis elegans and the effects of alpha 1 and alpha 2(IV) mutations on type IV collagen distribution. J. Cell Biol. 137:1185-1196.
    • (1997) J. Cell Biol. , vol.137 , pp. 1185-1196
    • Gupta, M.1    Graham, P.2    Kramer, J.M.3
  • 13
    • 0026006199 scopus 로고
    • Prolyl 4-hydroxylase, a target enzyme for drug development - Design of suppressive agents and the in vitro effects of inhibitors and proinhibitors
    • Hanauske-Abel, H. 1991. Prolyl 4-hydroxylase, a target enzyme for drug development - design of suppressive agents and the in vitro effects of inhibitors and proinhibitors. J. Hepatol. 13:S8-S16.
    • (1991) J. Hepatol. , vol.13
    • Hanauske-Abel, H.1
  • 14
    • 0027415488 scopus 로고
    • Cell-free synthesis and assembly of prolyl 4-hydroxylase - The role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit
    • John, D. C. A., M. E. Grant, and N. J. Bulleid. 1993. Cell-free synthesis and assembly of prolyl 4-hydroxylase - the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit. EMBO J. 12: 1587-1595.
    • (1993) EMBO J. , vol.12 , pp. 1587-1595
    • John, D.C.A.1    Grant, M.E.2    Bulleid, N.J.3
  • 15
    • 0029898363 scopus 로고    scopus 로고
    • Temporal reiteration of a precise gene expression pattern during nematode development
    • Johnstone, I. L., and J. D. Barry. 1996. Temporal reiteration of a precise gene expression pattern during nematode development. EMBO J. 15:3633-3639.
    • (1996) EMBO J. , vol.15 , pp. 3633-3639
    • Johnstone, I.L.1    Barry, J.D.2
  • 16
    • 0026782145 scopus 로고
    • Molecular analysis of mutations in the Caenorhabditis elegans collagen gene dpy-7
    • Johnstone, I. L., Y. Shafi, and J. D. Barry. 1992. Molecular analysis of mutations in the Caenorhabditis elegans collagen gene dpy-7. EMBO J. 11: 3857-3863.
    • (1992) EMBO J. , vol.11 , pp. 3857-3863
    • Johnstone, I.L.1    Shafi, Y.2    Barry, J.D.3
  • 17
    • 0025965946 scopus 로고
    • Nematode collagen genes
    • Kingston, B. I. 1991. Nematode collagen genes. Parasitol. Today 7:11-15.
    • (1991) Parasitol. Today , vol.7 , pp. 11-15
    • Kingston, B.I.1
  • 18
    • 0031893340 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
    • Kivirikko, K. I., and J. Myllyharju. 1998. Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 16:357-368.
    • (1998) Matrix Biol. , vol.16 , pp. 357-368
    • Kivirikko, K.I.1    Myllyharju, J.2
  • 19
    • 0031616949 scopus 로고    scopus 로고
    • Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
    • Kivirikko, K. I., and T. Pihlajaniemi. 1998. Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases. Adv. Enzymol. Related Areas Mol. Biol. 72:325-400.
    • (1998) Adv. Enzymol. Related Areas Mol. Biol. , vol.72 , pp. 325-400
    • Kivirikko, K.I.1    Pihlajaniemi, T.2
  • 20
    • 0028300045 scopus 로고
    • Structures and functions of collagens in Caenorhabditis elegans
    • Kramer, J. M. 1994. Structures and functions of collagens in Caenorhabditis elegans. FASEB J. 8:329-336.
    • (1994) FASEB J. , vol.8 , pp. 329-336
    • Kramer, J.M.1
  • 21
    • 0001531616 scopus 로고    scopus 로고
    • Extracellular matrix
    • D. L. Riddle, T. Blumenthal, B. J. Meyer, and J. R. Priess (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Kramer, J. M. 1997. Extracellular matrix, p. 471-500. In D. L. Riddle, T. Blumenthal, B. J. Meyer, and J. R. Priess (ed.), C. elegans II. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) C. Elegans II , pp. 471-500
    • Kramer, J.M.1
  • 22
    • 0022509078 scopus 로고
    • Genetic studies of unusual loci that affect body shape of the nematode Caenorhabditis elegans and may code for cuticle structural proteins
    • Kusch, M., and R. S. Edgar. 1986. Genetic studies of unusual loci that affect body shape of the nematode Caenorhabditis elegans and may code for cuticle structural proteins. Genetics 113:621-639.
    • (1986) Genetics , vol.113 , pp. 621-639
    • Kusch, M.1    Edgar, R.S.2
  • 23
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase
    • Myllyharju, J., and K. I. Kivirikko. 1997. Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase. EMBO J. 16: 1173-1180.
    • (1997) EMBO J. , vol.16 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 24
    • 0031441989 scopus 로고    scopus 로고
    • Cyclophilin and protein disulphide isomerase genes are co-transcribed in a functionally related manner in Caenorhabditis elegans
    • Page, A. P. 1997. Cyclophilin and protein disulphide isomerase genes are co-transcribed in a functionally related manner in Caenorhabditis elegans. DNA Cell Biol. 16:1335-1343.
    • (1997) DNA Cell Biol. , vol.16 , pp. 1335-1343
    • Page, A.P.1
  • 25
    • 0033574727 scopus 로고    scopus 로고
    • A highly conserved nematode protein folding operon in Caenorhabditis elegans and Caenorhabditis briggsae
    • Page, A. P. 1999. A highly conserved nematode protein folding operon in Caenorhabditis elegans and Caenorhabditis briggsae. Gene 230:267-275.
    • (1999) Gene , vol.230 , pp. 267-275
    • Page, A.P.1
  • 26
    • 0029885634 scopus 로고    scopus 로고
    • Cloning and biochemical characterisation of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans
    • Page, A. P., K. MacNiven, and M. O. Hengartner. 1996. Cloning and biochemical characterisation of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans. Biochem. J. 317:179-185.
    • (1996) Biochem. J. , vol.317 , pp. 179-185
    • Page, A.P.1    MacNiven, K.2    Hengartner, M.O.3
  • 27
    • 0026006124 scopus 로고
    • Mutations in the bli-4 (I) locus of Caenorhabditis elegans disrupt both adult cuticle and early larval development
    • Peters, K., J. McDowall, and A. M. Rose. 1991. Mutations in the bli-4 (I) locus of Caenorhabditis elegans disrupt both adult cuticle and early larval development. Genetics 129:95-102.
    • (1991) Genetics , vol.129 , pp. 95-102
    • Peters, K.1    McDowall, J.2    Rose, A.M.3
  • 28
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi, T., T. Helaakoski, K. Tasanen, R. Myllyla, M.-L. Huhtal, J. K. Koivu, and K. I. Kivirikko. 1987. Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6:643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtal, M.-L.5    Koivu, J.K.6    Kivirikko, K.I.7
  • 29
    • 0022778251 scopus 로고
    • Caenorhabditis elegans morphogenesis - The role of the cytoskeleton in elongation of the embryo
    • Priess, J., and D. Hirsh. 1986. Caenorhabditis elegans morphogenesis - the role of the cytoskeleton in elongation of the embryo. Dev. Biol. 117:156-173.
    • (1986) Dev. Biol. , vol.117 , pp. 156-173
    • Priess, J.1    Hirsh, D.2
  • 30
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potential for therapy
    • Prockop, D. J., and K. I. Kivirikko. 1995. Collagens: molecular biology, diseases, and potential for therapy. Annu. Rev. Biochem. 64:403-434.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 31
    • 0020858899 scopus 로고
    • The embryonic-cell lineage of the nematode Caenorhabditis elegans
    • Sulston, J., E. Schierenberg, J. White, and J. Thomason. 1983. The embryonic-cell lineage of the nematode Caenorhabditis elegans. Dev. Biol. 100:64-119.
    • (1983) Dev. Biol. , vol.100 , pp. 64-119
    • Sulston, J.1    Schierenberg, E.2    White, J.3    Thomason, J.4
  • 32
    • 0028957414 scopus 로고
    • The bli-4 locus of Caenorhabditis elegans encodes structurally distinct kex2/subtilisin-like endoproteases essential for early development and adult morphology
    • Thacker, C., K. Peters, M. Srayko, and A. M. Rose. 1995. The bli-4 locus of Caenorhabditis elegans encodes structurally distinct kex2/subtilisin-like endoproteases essential for early development and adult morphology. Genes Dev. 9:956-971.
    • (1995) Genes Dev. , vol.9 , pp. 956-971
    • Thacker, C.1    Peters, K.2    Srayko, M.3    Rose, A.M.4
  • 33
    • 0028101915 scopus 로고
    • Caenorhabditis elegans sqt-3 mutants have mutations in the COL-1 collagen gene
    • Vanderkeyl, H., H. Kim, R. Espey, C. V. Oke, and M. K. Edwards. 1994. Caenorhabditis elegans sqt-3 mutants have mutations in the COL-1 collagen gene. Dev. Dynamics 201:86-94.
    • (1994) Dev. Dynamics , vol.201 , pp. 86-94
    • Vanderkeyl, H.1    Kim, H.2    Espey, R.3    Oke, C.V.4    Edwards, M.K.5
  • 34
    • 0029838075 scopus 로고    scopus 로고
    • Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterisation of prolyl 4-hydroxylases containing one of these polypeptides as their β-subunit
    • Veijola, J., P. Annunen, P. Koivunen, A. P. Page, T. Pihlajaniemi, and K. I. Kivirikko. 1996. Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterisation of prolyl 4-hydroxylases containing one of these polypeptides as their β-subunit. Biochem. J. 317:721-729.
    • (1996) Biochem. J. , vol.317 , pp. 721-729
    • Veijola, J.1    Annunen, P.2    Koivunen, P.3    Page, A.P.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 35
    • 0028027778 scopus 로고
    • Cloning, baculovirus expression, and characterization of the α-subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans - This α-subunit forms an active αβ dimer with the human protein disulfide-isomerase β-subunit
    • Veijola, J., P. Koivunen, P. Annunen, T. Pihlajaniemi, and K. I. Kivirikko. 1994. Cloning, baculovirus expression, and characterization of the α-subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans - this α-subunit forms an active αβ dimer with the human protein disulfide-isomerase β-subunit. J. Biol. Chem. 269:26746-26753.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26746-26753
    • Veijola, J.1    Koivunen, P.2    Annunen, P.3    Pihlajaniemi, T.4    Kivirikko, K.I.5
  • 36
    • 0026672695 scopus 로고
    • Site-directed mutagenesis of human protein disulfide isomerase - Effect on the assembly, activity and endoplasmic-reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells
    • Vuori, K., T. Pihlajaniemi, R. Myllyla, and K. I. Kivirikko. 1992. Site-directed mutagenesis of human protein disulfide isomerase - effect on the assembly, activity and endoplasmic-reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells. EMBO J. 11:4213-4217.
    • (1992) EMBO J. , vol.11 , pp. 4213-4217
    • Vuori, K.1    Pihlajaniemi, T.2    Myllyla, R.3    Kivirikko, K.I.4
  • 37
    • 0033591252 scopus 로고    scopus 로고
    • Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase
    • Walmsley, A., M. Batten, U. Lad, and N. Bulleid. 1999. Intracellular retention of procollagen within the endoplasmic reticulum is mediated by prolyl 4-hydroxylase. J. Biol. Chem. 274:14884-14892.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14884-14892
    • Walmsley, A.1    Batten, M.2    Lad, U.3    Bulleid, N.4
  • 38
    • 0028230454 scopus 로고
    • In vitro mutagenesis of Caenorhabditis elegans cuticle collagens identifies a potential subtilisin-like protease cleavage site and demonstrates that carboxyl domain disulfide bonding is required for normal function but not assembly
    • Yang, J., and J. M. Kramer. 1994. In vitro mutagenesis of Caenorhabditis elegans cuticle collagens identifies a potential subtilisin-like protease cleavage site and demonstrates that carboxyl domain disulfide bonding is required for normal function but not assembly. Mol. Cell. Biol. 14:2722-2730.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2722-2730
    • Yang, J.1    Kramer, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.