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Volumn 288, Issue 3, 2013, Pages 1750-1761

Prolyl 4-hydroxlase activity is essential for development and cuticle formation in the human infective parasitic nematode brugia malayi

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYPROLINES; BIOCHEMICAL ACTIVITY; BIOINFORMATIC ANALYSIS; BIOSYNTHETIC ENZYMES; CAENORHABDITIS ELEGANS; CO-EXPRESSION; COLLAGEN POLYPEPTIDES; COMPLEX FORMATIONS; CONTROL MECHANISM; COVALENT LINK; DERIVED MATERIALS; ELEGANS; ENZYMATIC ACTIVITIES; EXTRACELLULAR MATRICES; HETEROLOGOUS EXPRESSION; HUMAN ENZYMES; INSECT CELLS; NON-REDUCIBLE; OLIGOMERIC COMPLEXES; PARASITE; PARASITE CONTROL; PROLINE RESIDUES; PROTEIN DISULFIDE ISOMERASES; SEQUENCE DATABASE; TRIPLE HELIXES; UNIQUE FEATURES;

EID: 84872713545     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.397604     Document Type: Article
Times cited : (17)

References (37)
  • 4
    • 0034111331 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans
    • DOI 10.1128/MCB.20.11.4084-4093.2000
    • Winter, A. D., and Page, A. P. (2000) Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans. Mol. Cell Biol. 20, 4084-4093 (Pubitemid 30314506)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.11 , pp. 4084-4093
    • Winter, A.D.1    Page, A.P.2
  • 5
    • 0037047409 scopus 로고    scopus 로고
    • The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylase with unique combinations of subunits
    • Myllyharju, J., Kukkola, L., Winter, A. D., and Page, A. P. (2002) The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylase with unique combinations of subunits. J. Biol. Chem. 277, 29187-29196
    • (2002) J. Biol. Chem. , vol.277 , pp. 29187-29196
    • Myllyharju, J.1    Kukkola, L.2    Winter, A.D.3    Page, A.P.4
  • 6
    • 34547670979 scopus 로고    scopus 로고
    • Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans
    • DOI 10.1016/j.ydbio.2007.05.041, PII S0012160607011116
    • Winter, A. D., McCormack, G., and Page, A. P. (2007) Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans. Dev. Biol. 308, 449-461 (Pubitemid 47223109)
    • (2007) Developmental Biology , vol.308 , Issue.2 , pp. 449-461
    • Winter, A.D.1    McCormack, G.2    Page, A.P.3
  • 7
    • 0141754038 scopus 로고    scopus 로고
    • Enzymes involved in the biogenesis of the nematode cuticle
    • DOI 10.1016/S0065-308X(03)53003-2
    • Page, A. P., and Winter, A. D. (2003) Enzymes involved in the biogenesis of the nematode cuticle. Adv. Parasitol. 53, 85-148 (Pubitemid 37221990)
    • (2003) Advances in Parasitology , vol.53 , pp. 85-148
    • Page, A.P.1    Winter, A.D.2
  • 8
    • 50649120554 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
    • Myllyharju, J. (2008) Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets. Ann. Med. 40, 402-417
    • (2008) Ann. Med. , vol.40 , pp. 402-417
    • Myllyharju, J.1
  • 9
    • 34248999415 scopus 로고    scopus 로고
    • Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits
    • DOI 10.1016/j.matbio.2007.01.008, PII S0945053X07000157
    • Winter, A. D., Keskiaho, K., Kukkola, L., McCormack, G., Felix, M. A., Myllyharju, J., and Page, A. P. (2007) Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits. Matrix Biol. 26, 382-395 (Pubitemid 46803256)
    • (2007) Matrix Biology , vol.26 , Issue.5 , pp. 382-395
    • Winter, A.D.1    Keskiaho, K.2    Kukkola, L.3    McCormack, G.4    Felix, M.-A.5    Myllyharju, J.6    Page, A.P.7
  • 10
    • 0034894096 scopus 로고    scopus 로고
    • Characterization and expression of enzymatically active recombinant filarial prolyl 4-hydroxylase
    • DOI 10.1016/S0166-6851(01)00317-6, PII S0166685101003176
    • Merriweather, A., Guenzler, V., Brenner, M., and Unnasch, T. R. (2001) Characterization and expression of enzymatically active recombinant filarial prolyl 4-hydroxylase. Mol. Biochem. Parasitol. 116, 185-197 (Pubitemid 32777827)
    • (2001) Molecular and Biochemical Parasitology , vol.116 , Issue.2 , pp. 185-197
    • Merriweather, A.1    Guenzler, V.2    Brenner, M.3    Unnasch, T.R.4
  • 11
    • 0141856407 scopus 로고    scopus 로고
    • Ascorbic acid is a requirement for the morphogenesis of the human filarial parasite Brugia malayi
    • DOI 10.1645/GE-3137RN
    • Rajan, T. V., Paciorkowski, N., Kalajzic, I., and McGuiness, C. (2003) Ascorbic acid is a requirement for the morphogenesis of the human filarial parasite Brugia malayi. J. Parasitol. 89, 868-870 (Pubitemid 37151601)
    • (2003) Journal of Parasitology , vol.89 , Issue.4 , pp. 868-870
    • Rajan, T.V.1    Paclorkowski, N.2    Kalajzic, I.3    McGuiness, C.4
  • 12
    • 0026111378 scopus 로고
    • Onchocerca volvulus, O. gutturosa, Brugia malayi, and Dirofilaria immitis:Acomparative study of the immunochemical properties of cuticular proteins from filarial parasites
    • Petralanda, I., and Piessens, W. F. (1991) Onchocerca volvulus, O. gutturosa, Brugia malayi, and Dirofilaria immitis:Acomparative study of the immunochemical properties of cuticular proteins from filarial parasites. Exp. Parasitol. 72, 164-173
    • (1991) Exp. Parasitol. , vol.72 , pp. 164-173
    • Petralanda, I.1    Piessens, W.F.2
  • 13
    • 0019596981 scopus 로고
    • Cuticle of Caenorhabditis elegans: Its isolation and partial characterization
    • Cox, G. N., Kusch, M., and Edgar, R. S. (1981) Cuticle of Caenorhabditis elegans: its isolation and partial characterization. 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
  • 14
    • 0037462716 scopus 로고    scopus 로고
    • A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase
    • DOI 10.1074/jbc.M210381200
    • Winter, A. D., Myllyharju, J., and Page, A. P. (2003) A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulphide isomerase. J. Biol. Chem. 278, 2554-2562 (Pubitemid 36801333)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2554-2562
    • Winter, A.D.1    Myllyharju, J.2    Page, A.P.3
  • 15
    • 84855733708 scopus 로고    scopus 로고
    • Efficient in vitro RNA interference and immunofluorescence-based phenotype analysis in a human parasitic nematode, Brugia malayi
    • Landmann, F., Foster, J. M., Slatko, B. E., and Sullivan, W. (2012) Efficient in vitro RNA interference and immunofluorescence-based phenotype analysis in a human parasitic nematode, Brugia malayi. Parasit. Vectors 5, 16
    • (2012) Parasit. Vectors , vol.5 , pp. 16
    • Landmann, F.1    Foster, J.M.2    Slatko, B.E.3    Sullivan, W.4
  • 16
    • 38449085292 scopus 로고    scopus 로고
    • Maintenance of C. elegans
    • doi: 10.1895/ wormbook.1.101.1
    • Stiernagle, T. (2006) Maintenance of C. elegans. WormBook, doi/10.1895/ wormbook.1.101.1
    • (2006) WormBook
    • Stiernagle, T.1
  • 17
    • 0035941485 scopus 로고    scopus 로고
    • Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans
    • DOI 10.1016/S0378-1119(00)00579-5, PII S0378111900005795
    • Timmons, L., Court, D. L., and Fire, A. (2001) Ingestion of bacterially expressed dRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Gene 263, 103-112 (Pubitemid 32167059)
    • (2001) Gene , vol.263 , Issue.1-2 , pp. 103-112
    • Timmons, L.1    Court, D.L.2    Fire, A.3
  • 18
    • 0035229245 scopus 로고    scopus 로고
    • Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans
    • Kamath, R. S., Martinez-Campos, M., Zipperlen, P., Fraser, A. G., and Ahringer, J. (2001) Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans. Genome Biol. 2, RESEARCH0002
    • (2001) Genome Biol. , vol.2
    • Kamath, R.S.1    Martinez-Campos, M.2    Zipperlen, P.3    Fraser, A.G.4    Ahringer, J.5
  • 19
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes
    • Kivirikko, K. I., and Myllylä, R. (1982) Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods Enzymol. 82, 245-304
    • (1982) Methods Enzymol. , vol.82 , pp. 245-304
    • Kivirikko, K.I.1    Myllylä, R.2
  • 20
    • 67650722550 scopus 로고    scopus 로고
    • Transformation and microinjection
    • doi: 10.1895/wormbook.1.108.1
    • Evans, T. C. (2006) Transformation and microinjection. WormBook, doi/10.1895/wormbook.1.108.1
    • (2006) WormBook
    • Evans, T.C.1
  • 21
    • 0030903160 scopus 로고    scopus 로고
    • Distinct requirements for somatic and germline expression of a generally expressed Caenorhabditis elegans gene
    • Kelly, W. G., Xu, S., Montgomery, M. K., and Fire, A. (1997) Distinct requirements for somatic and germline expression of a generally expressed Caernorhabditis elegans gene. Genetics 146, 227-238 (Pubitemid 27194401)
    • (1997) Genetics , vol.146 , Issue.1 , pp. 227-238
    • Kelly, W.G.1    Xu, S.2    Montgomery, M.K.3    Fire, A.4
  • 22
    • 0000241017 scopus 로고
    • A 22-nucleotide spliced leader sequence in the human parasitic nematode Brugia malayi is identical to the trans-spliced leader exon in Caenorhabditis elegans
    • Takacs, A. M., Denker, J. A., Perrine, K. G., Maroney, P. A., and Nilsen, T. W. (1988) A 22-nucleotide spliced leader sequence in the human parasitic nematode Brugia malayi is identical to the trans-spliced leader exon in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 85, 7932-7936
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7932-7936
    • Takacs, A.M.1    Denker, J.A.2    Perrine, K.G.3    Maroney, P.A.4    Nilsen, T.W.5
  • 23
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Bendtsen, J. D., Nielsen, H., von Heijne, G., and Brunak, S. (2004) Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340, 783-795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 24
    • 0028190340 scopus 로고
    • Prolyl 4-hydroxylase: Defective assembly of a-subunit mutants indicates that assembled a-subunits are intramolecularly disulfide bonded
    • John, D. C., and Bulleid, N. J. (1994) Prolyl 4-hydroxylase: defective assembly of a-subunit mutants indicates that assembled a-subunits are intramolecularly disulfide bonded. Biochemistry 33, 14018-14025
    • (1994) Biochemistry , vol.33 , pp. 14018-14025
    • John, D.C.1    Bulleid, N.J.2
  • 25
    • 0028957849 scopus 로고
    • Site-directed mutagenesis of the a-subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity
    • Lamberg, A., Pihlajaniemi, T., and Kivirikko, K. I. (1995) Site-directed mutagenesis of the a-subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity. J. Biol. Chem. 270, 9926-9931
    • (1995) J. Biol. Chem. , vol.270 , pp. 9926-9931
    • Lamberg, A.1    Pihlajaniemi, T.2    Kivirikko, K.I.3
  • 26
    • 0030962028 scopus 로고    scopus 로고
    • Characterization of the iron- and 2-oxoglutavate binding sites of human prolyl 4-hydroxylase
    • DOI 10.1093/emboj/16.6.1173
    • Myllyharju, J., and Kivirikko, K. I. (1997) Characterization of the iron-and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase. EMBO J. 16, 1173-1180 (Pubitemid 27136084)
    • (1997) EMBO Journal , vol.16 , Issue.6 , pp. 1173-1180
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 28
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • DOI 10.1038/sj.embor.7400311
    • Ellgaard, L., and Ruddock, L. W. (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6, 28-32 (Pubitemid 41710070)
    • (2005) EMBO Reports , vol.6 , Issue.1 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 30
    • 0033521682 scopus 로고    scopus 로고
    • The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
    • DOI 10.1093/emboj/18.1.65
    • Koivunen, P., Pirneskoski, A., Karvonen, P., Ljung, J., Helaakoski, T., Notbohm, H., and Kivirikko, K. I. (1999) The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide. EMBO J. 18, 65-74 (Pubitemid 29005024)
    • (1999) EMBO Journal , vol.18 , Issue.1 , pp. 65-74
    • Koivunen, P.1    Pirneskoski, A.2    Karvonen, P.3    Ljung, J.4    Helaakoski, T.5    Notbohm, H.6    Kivirikko, K.I.7
  • 33
    • 80052521105 scopus 로고    scopus 로고
    • Deep small RNA sequencing from the nematode Ascaris reveals conservation, functional diversification, and novel developmental profiles
    • Wang, J., Czech, B., Crunk, A., Wallace, A., Mitreva, M., Hannon, G. J., and Davis, R. E. (2011) Deep small RNA sequencing from the nematode Ascaris reveals conservation, functional diversification, and novel developmental profiles. Genome Res. 21, 1462-1477
    • (2011) Genome Res. , vol.21 , pp. 1462-1477
    • Wang, J.1    Czech, B.2    Crunk, A.3    Wallace, A.4    Mitreva, M.5    Hannon, G.J.6    Davis, R.E.7
  • 36
    • 0037124029 scopus 로고    scopus 로고
    • Egg shell collagen formation in Caenorhabditis elegans involves a novel prolyl 4-hydroxylase expressed in spermatheca and embryos and possessing many unique properties
    • DOI 10.1074/jbc.M200895200
    • Riihimaa, P., Nissi, R., Page, A. P., Winter, A. D., Keskiaho, K., Kivirikko, K. I., and Myllyharju, J. (2002) Egg shell collagen formation in Caenorhabditis elegans involves a novel prolyl 4-hydroxylase expressed in spermatheca and embryos and possessing many unique properties. J. Biol. Chem. 277, 18238-18243 (Pubitemid 34967640)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 18238-18243
    • Riihimaa, P.1    Nissi, R.2    Page, A.P.3    Winter, A.D.4    Keskiaho, K.5    Kivirikko, K.I.6    Myllyharju, J.7
  • 37
    • 84859401080 scopus 로고    scopus 로고
    • Nucleic acid transfection and transgenesis in parasitic nematodes
    • Lok, J. B. (2012) Nucleic acid transfection and transgenesis in parasitic nematodes. Parasitology 139, 574-588
    • (2012) Parasitology , vol.139 , pp. 574-588
    • Lok, J.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.