메뉴 건너뛰기




Volumn 169, Issue 1, 2010, Pages 1-11

The kunitz domain protein BLI-5 plays a functionally conserved role in cuticle formation in a diverse range of nematodes

Author keywords

Brugia malayi; Caenorhabditis elegans; Collagen; Cuticle; Haemonchus contortus

Indexed keywords

BLISTER 5 PROTEIN; COLLAGEN; HELMINTH PROTEIN; MUTANT PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

EID: 71549132727     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2009.08.005     Document Type: Article
Times cited : (16)

References (42)
  • 1
    • 0141754038 scopus 로고    scopus 로고
    • Enzymes involved in the biogenesis of the nematode cuticle
    • Page A.P., and Winter A.D. Enzymes involved in the biogenesis of the nematode cuticle. Adv Parasitol 53 (2003) 85-148
    • (2003) Adv Parasitol , vol.53 , pp. 85-148
    • Page, A.P.1    Winter, A.D.2
  • 2
    • 38449121369 scopus 로고    scopus 로고
    • Page AP, Johnstone IL. The cuticle. In WormBook. (The C. elegans research community, eds.) WormBook 2007, 10.1895/wormbook.1.138.1.
    • Page AP, Johnstone IL. The cuticle. In WormBook. (The C. elegans research community, eds.) WormBook 2007, 10.1895/wormbook.1.138.1.
  • 3
    • 67650510676 scopus 로고    scopus 로고
    • Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans
    • Thein M.C., Winter A.D., Stepek G., et al. Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans. J Biol Chem 284 (2009) 17549-17563
    • (2009) J Biol Chem , vol.284 , pp. 17549-17563
    • Thein, M.C.1    Winter, A.D.2    Stepek, G.3
  • 4
    • 34547670979 scopus 로고    scopus 로고
    • Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans
    • Winter A.D., McCormack G., and Page A.P. Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans. Dev Biol 308 (2007) 449-461
    • (2007) Dev Biol , vol.308 , pp. 449-461
    • Winter, A.D.1    McCormack, G.2    Page, A.P.3
  • 5
    • 33646188278 scopus 로고    scopus 로고
    • The C terminus of collagen SQT-3 has complex and essential functions in nematode collagen assembly
    • Novelli J., Page A.P., and Hodgkin J. The C terminus of collagen SQT-3 has complex and essential functions in nematode collagen assembly. Genetics 172 (2006) 2253-2267
    • (2006) Genetics , vol.172 , pp. 2253-2267
    • Novelli, J.1    Page, A.P.2    Hodgkin, J.3
  • 6
    • 0024756911 scopus 로고
    • Cuticle collagen genes of Haemonchus contortus and Caenorhabditis elegans are highly conserved
    • Shamansky L.M., Pratt D., Boisvenue R.J., and Cox G.N. Cuticle collagen genes of Haemonchus contortus and Caenorhabditis elegans are highly conserved. Mol Biochem Parasitol 37 (1989) 73-86
    • (1989) Mol Biochem Parasitol , vol.37 , pp. 73-86
    • Shamansky, L.M.1    Pratt, D.2    Boisvenue, R.J.3    Cox, G.N.4
  • 7
    • 0025002920 scopus 로고
    • Structure and expression of Ascaris suum collagen genes: a comparison with Caenorhabditis elegans
    • Kingston I.B., and Pettitt J. Structure and expression of Ascaris suum collagen genes: a comparison with Caenorhabditis elegans. Acta Trop 47 (1990) 283-287
    • (1990) Acta Trop , vol.47 , pp. 283-287
    • Kingston, I.B.1    Pettitt, J.2
  • 8
    • 0025965946 scopus 로고
    • Nematode collagen genes
    • Kingston I.B. Nematode collagen genes. Parasitol Today 7 (1991) 11-15
    • (1991) Parasitol Today , vol.7 , pp. 11-15
    • Kingston, I.B.1
  • 9
    • 0028906117 scopus 로고
    • Molecular cloning of the cuticular collagen gene Bmcol-2 from Brugia malayi
    • Scott A.L., Yenbutr P., Eisinger S.W., and Raghavan N. Molecular cloning of the cuticular collagen gene Bmcol-2 from Brugia malayi. Mol Biochem Parasitol 70 (1995) 221-225
    • (1995) Mol Biochem Parasitol , vol.70 , pp. 221-225
    • Scott, A.L.1    Yenbutr, P.2    Eisinger, S.W.3    Raghavan, N.4
  • 10
    • 0030249919 scopus 로고    scopus 로고
    • Cuticular collagen genes from the parasitic nematode Ostertagia circumcincta
    • Johnstone I.L., Shafi Y., Majeed A., and Barry J.D. Cuticular collagen genes from the parasitic nematode Ostertagia circumcincta. Mol Biochem Parasitol 80 (1996) 103-112
    • (1996) Mol Biochem Parasitol , vol.80 , pp. 103-112
    • Johnstone, I.L.1    Shafi, Y.2    Majeed, A.3    Barry, J.D.4
  • 11
    • 26444458292 scopus 로고    scopus 로고
    • Functional genomic analysis of C. elegans molting
    • Frand A.R., Russel S., and Ruvkun G. Functional genomic analysis of C. elegans molting. PLoS Biol 3 (2005) 1719-1733
    • (2005) PLoS Biol , vol.3 , pp. 1719-1733
    • Frand, A.R.1    Russel, S.2    Ruvkun, G.3
  • 12
    • 33745298447 scopus 로고    scopus 로고
    • Caenorhabditis elegans dpy-5 is a cuticle procollagen processed by a proprotein convertase
    • Thacker C., Sheps J.A., and Rose A.M. Caenorhabditis elegans dpy-5 is a cuticle procollagen processed by a proprotein convertase. Cell Mol Life Sci 63 (2006) 1193-1204
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1193-1204
    • Thacker, C.1    Sheps, J.A.2    Rose, A.M.3
  • 13
    • 10844246408 scopus 로고    scopus 로고
    • Gene interactions in Caenorhabditis elegans define DPY-31 as a candidate procollagen C-proteinase and SQT-3/ROL-4 as its predicted major target
    • Novelli J., Ahmed S., and Hodgkin J. Gene interactions in Caenorhabditis elegans define DPY-31 as a candidate procollagen C-proteinase and SQT-3/ROL-4 as its predicted major target. Genetics 168 (2004) 1259-1273
    • (2004) Genetics , vol.168 , pp. 1259-1273
    • Novelli, J.1    Ahmed, S.2    Hodgkin, J.3
  • 14
    • 33646796713 scopus 로고    scopus 로고
    • Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterisation of a novel serine protease inhibitor
    • Page A.P., McCormack G., and Birnie A.J. Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterisation of a novel serine protease inhibitor. Int J Parasitol 36 (2006) 681-689
    • (2006) Int J Parasitol , vol.36 , pp. 681-689
    • Page, A.P.1    McCormack, G.2    Birnie, A.J.3
  • 15
    • 34648836102 scopus 로고    scopus 로고
    • Draft genome of the filarial nematode parasite Brugia malayi
    • Ghedin E., Wang S., Spiro D., et al. Draft genome of the filarial nematode parasite Brugia malayi. Science 317 (2007) 1756-1760
    • (2007) Science , vol.317 , pp. 1756-1760
    • Ghedin, E.1    Wang, S.2    Spiro, D.3
  • 16
    • 0029898363 scopus 로고    scopus 로고
    • Temporal reiteration of a precise gene expression pattern during nematode development
    • Johnstone I.L., and Barry J.D. Temporal reiteration of a precise gene expression pattern during nematode development. EMBO J 15 (1996) 3633-3639
    • (1996) EMBO J , vol.15 , pp. 3633-3639
    • Johnstone, I.L.1    Barry, J.D.2
  • 17
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier F.W. Protein production by auto-induction in high-density shaking cultures. Protein Expr Purif 41 (2005) 207-234
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 18
    • 0034703067 scopus 로고    scopus 로고
    • A broad spectrum kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum
    • Milstone A.M., Harrison L.M., Bungiro R.D., Kuzmi P., and Cappello M. A broad spectrum kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum. J Biol Chem 275 (2000) 29391-29399
    • (2000) J Biol Chem , vol.275 , pp. 29391-29399
    • Milstone, A.M.1    Harrison, L.M.2    Bungiro, R.D.3    Kuzmi, P.4    Cappello, M.5
  • 19
    • 0032485270 scopus 로고    scopus 로고
    • A molecular evolutionary framework for the phylum Nematoda
    • Blaxter M.L., De Ley P., Garey J.R., et al. A molecular evolutionary framework for the phylum Nematoda. Nature 392 (1998) 71-75
    • (1998) Nature , vol.392 , pp. 71-75
    • Blaxter, M.L.1    De Ley, P.2    Garey, J.R.3
  • 20
    • 0035862835 scopus 로고    scopus 로고
    • Expression of Haemonchus contortus pepsinogen in Caenorhabditis elegans
    • Redmond D.L., Clucas C., Johnstone I.L., and Knox D.P. Expression of Haemonchus contortus pepsinogen in Caenorhabditis elegans. Mol Biochem Parasitol 112 (2001) 125-131
    • (2001) Mol Biochem Parasitol , vol.112 , pp. 125-131
    • Redmond, D.L.1    Clucas, C.2    Johnstone, I.L.3    Knox, D.P.4
  • 21
    • 33645881686 scopus 로고    scopus 로고
    • Caenorhabditis elegans ivermectin receptors regulate locomotor behaviour and are functional orthologues of Haemonchus contortus receptors
    • Cook A., Aptel N., Portillo V., et al. Caenorhabditis elegans ivermectin receptors regulate locomotor behaviour and are functional orthologues of Haemonchus contortus receptors. Mol Biochem Parasitol 147 (2006) 118-125
    • (2006) Mol Biochem Parasitol , vol.147 , pp. 118-125
    • Cook, A.1    Aptel, N.2    Portillo, V.3
  • 22
    • 0027196767 scopus 로고
    • The serine protease inhibitor family from Ascaris suum: chemical determination of the five disulphide bridges
    • Bernard V.D., and Peanasky R.J. The serine protease inhibitor family from Ascaris suum: chemical determination of the five disulphide bridges. Arch Biochem Biophys 303 (1993) 367-376
    • (1993) Arch Biochem Biophys , vol.303 , pp. 367-376
    • Bernard, V.D.1    Peanasky, R.J.2
  • 23
    • 0000455702 scopus 로고    scopus 로고
    • Anticoagulant repertoire of the hookworm Ancylostoma caninum
    • Stanssens P., Bergum P.W., Gansemans Y., et al. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proc Natl Acad Sci USA 93 (1996) 2149-2154
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2149-2154
    • Stanssens, P.1    Bergum, P.W.2    Gansemans, Y.3
  • 24
    • 3342988385 scopus 로고    scopus 로고
    • Ancylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa
    • Mieszczanek J., Harrison L.M., and Cappello M. Ancylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa. Mol Biochem Parasitol 137 (2004) 151-159
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 151-159
    • Mieszczanek, J.1    Harrison, L.M.2    Cappello, M.3
  • 25
    • 0033979344 scopus 로고    scopus 로고
    • Trichuris suis: a secretory serine protease inhibitor
    • Rhoads M.L., Fetterer R.H., and Hill D.E. Trichuris suis: a secretory serine protease inhibitor. Exp Parasitol 94 (2000) 1-7
    • (2000) Exp Parasitol , vol.94 , pp. 1-7
    • Rhoads, M.L.1    Fetterer, R.H.2    Hill, D.E.3
  • 26
    • 28844497908 scopus 로고    scopus 로고
    • Characterisation of a novel filarial serine protease inhibitor, Ov-SPI-1, from Onchocerca volvulus, with potential multifunctional roles during development of the parasite
    • Ford L., Guiliano D.B., Oksov Y., et al. Characterisation of a novel filarial serine protease inhibitor, Ov-SPI-1, from Onchocerca volvulus, with potential multifunctional roles during development of the parasite. J Biol Chem 280 (2005) 40845-40856
    • (2005) J Biol Chem , vol.280 , pp. 40845-40856
    • Ford, L.1    Guiliano, D.B.2    Oksov, Y.3
  • 28
    • 45549109409 scopus 로고    scopus 로고
    • rBmTI-6, a kunitz-BPTI domain protease inhibitor from the tick Boophilus microplus, its cloning, expression and biochemical characterisation
    • Sasaki S.D., and Tanaka A.S. rBmTI-6, a kunitz-BPTI domain protease inhibitor from the tick Boophilus microplus, its cloning, expression and biochemical characterisation. Vet Parasitol 155 (2008) 133-141
    • (2008) Vet Parasitol , vol.155 , pp. 133-141
    • Sasaki, S.D.1    Tanaka, A.S.2
  • 29
    • 0034518571 scopus 로고    scopus 로고
    • Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases
    • Kramerova I.A., Kawaguchi N., Fessler L.I., et al. Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases. Development 127 (2000) 5475-5485
    • (2000) Development , vol.127 , pp. 5475-5485
    • Kramerova, I.A.1    Kawaguchi, N.2    Fessler, L.I.3
  • 30
    • 3242714188 scopus 로고    scopus 로고
    • A kunitz type protease inhibitor related protein is synthesised in Drosophila prepupal salivary glands and released into the moulting fluid during pupation
    • Kress H., Jarrin A., Thüroff E., et al. A kunitz type protease inhibitor related protein is synthesised in Drosophila prepupal salivary glands and released into the moulting fluid during pupation. Insect Biochem Mol Biol 34 (2004) 855-869
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 855-869
    • Kress, H.1    Jarrin, A.2    Thüroff, E.3
  • 31
    • 0028046189 scopus 로고
    • Aprotinin, a kunitz-type protease inhibitor, stimulates skeletal muscle differentiation
    • Wells J.M., and Strickland S. Aprotinin, a kunitz-type protease inhibitor, stimulates skeletal muscle differentiation. Development 120 (1994) 3639-3647
    • (1994) Development , vol.120 , pp. 3639-3647
    • Wells, J.M.1    Strickland, S.2
  • 32
    • 0034799036 scopus 로고    scopus 로고
    • Cloning and characterisation of thrombospondin, a novel multidomain glycoprotein found in association with a host protective gut extract from Haemonchus contortus
    • Skuce P.J., Newlands G.F.J., Stewart E.M., et al. Cloning and characterisation of thrombospondin, a novel multidomain glycoprotein found in association with a host protective gut extract from Haemonchus contortus. Mol Biochem Parasitol 117 (2001) 241-244
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 241-244
    • Skuce, P.J.1    Newlands, G.F.J.2    Stewart, E.M.3
  • 33
    • 0037398198 scopus 로고    scopus 로고
    • Molecular cloning of a novel multidomain kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum
    • Hawdon J.M., Datu B., and Crowell M. Molecular cloning of a novel multidomain kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum. J Parasitol 89 (2003) 402-407
    • (2003) J Parasitol , vol.89 , pp. 402-407
    • Hawdon, J.M.1    Datu, B.2    Crowell, M.3
  • 34
    • 1842431649 scopus 로고    scopus 로고
    • Molecular characterisation of Ancylostoma ceylanicum kunitz-type serine protease inhibitor: evidence for a role in hookworm-associated growth delay
    • Chu D., Bungiro R.D., Ibanez M., et al. Molecular characterisation of Ancylostoma ceylanicum kunitz-type serine protease inhibitor: evidence for a role in hookworm-associated growth delay. Infect Immun 72 (2004) 2214-2221
    • (2004) Infect Immun , vol.72 , pp. 2214-2221
    • Chu, D.1    Bungiro, R.D.2    Ibanez, M.3
  • 35
    • 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., Peters K., Srayko M., and Rose A.M. The bli-4 locus of Caenorhabditis elegans encodes structurally distinct kex2/subtilisin-like endoproteases essential for early development and adult morphology. Genes Dev 9 (1995) 956-971
    • (1995) Genes Dev , vol.9 , pp. 956-971
    • Thacker, C.1    Peters, K.2    Srayko, M.3    Rose, A.M.4
  • 36
    • 0034636699 scopus 로고    scopus 로고
    • Mutational analysis of bli-4/kpc-4 reveals critical residues required for proprotein convertase function in C. elegans
    • Thacker C., Srayko M., and Rose A.M. Mutational analysis of bli-4/kpc-4 reveals critical residues required for proprotein convertase function in C. elegans. Gene 252 (2000) 15-25
    • (2000) Gene , vol.252 , pp. 15-25
    • Thacker, C.1    Srayko, M.2    Rose, A.M.3
  • 37
    • 0141592515 scopus 로고    scopus 로고
    • Cloning and characterisation of blisterase, a subtilisin-like convertase from the filarial parasite, Onchocerca volvulus
    • Poole C.B., Jin J., and McReynolds L.A. Cloning and characterisation of blisterase, a subtilisin-like convertase from the filarial parasite, Onchocerca volvulus. J Biol Chem 278 (2003) 36183-36190
    • (2003) J Biol Chem , vol.278 , pp. 36183-36190
    • Poole, C.B.1    Jin, J.2    McReynolds, L.A.3
  • 38
    • 0022778251 scopus 로고
    • Caenorhabditis elegans morphogenesis-the role of the cytoskeleton in elongation of the embryo
    • Priess J.R., and Hirsh D.I. Caenorhabditis elegans morphogenesis-the role of the cytoskeleton in elongation of the embryo. Dev Biol 117 (1986) 156-173
    • (1986) Dev Biol , vol.117 , pp. 156-173
    • Priess, J.R.1    Hirsh, D.I.2
  • 39
    • 0037382329 scopus 로고    scopus 로고
    • Alternative splicing of papilin and the diversity of Drosophila extracellular matrix during embryonic morphogenesis
    • Kramerova I.A., Kramerov A.A., and Fessler J.H. Alternative splicing of papilin and the diversity of Drosophila extracellular matrix during embryonic morphogenesis. Dev Dyn 226 (2003) 634-642
    • (2003) Dev Dyn , vol.226 , pp. 634-642
    • Kramerova, I.A.1    Kramerov, A.A.2    Fessler, J.H.3
  • 40
    • 16544369169 scopus 로고    scopus 로고
    • Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development
    • Fessler J.H., Kramerova I., Kramerov A., Chen Y., and Fessler L.I. Papilin, a novel component of basement membranes, in relation to ADAMTS metalloproteases and ECM development. Int J Biochem Cell Biol 36 (2004) 1079-1084
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1079-1084
    • Fessler, J.H.1    Kramerova, I.2    Kramerov, A.3    Chen, Y.4    Fessler, L.I.5
  • 41
    • 0032923247 scopus 로고    scopus 로고
    • Functional genomics in Caenorhabditis elegans: an approach involving comparisons of sequences from related nematodes
    • Thacker C., Marra M.A., Jones A., Baillie D.L., and Rose A.M. Functional genomics in Caenorhabditis elegans: an approach involving comparisons of sequences from related nematodes. Genome Res 9 (1999) 348-359
    • (1999) Genome Res , vol.9 , pp. 348-359
    • Thacker, C.1    Marra, M.A.2    Jones, A.3    Baillie, D.L.4    Rose, A.M.5
  • 42
    • 0037330694 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a serine proteinase gene of Trichinella spiralis
    • Nagano I., Wu Z., Nakada T., Boonmars T., and Takahashi Y. Molecular cloning and characterisation of a serine proteinase gene of Trichinella spiralis. J Parasitol 89 (2003) 92-98
    • (2003) J Parasitol , vol.89 , pp. 92-98
    • Nagano, I.1    Wu, Z.2    Nakada, T.3    Boonmars, T.4    Takahashi, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.