메뉴 건너뛰기




Volumn 93, Issue 4, 2009, Pages 367-375

A comparative analysis of serpin genes in the silkworm genome

Author keywords

Bombyx mori; Hemolymph protein; Insect immunity; Melanization; Serine protease inhibitor; Sp tzle processing

Indexed keywords

MESSENGER RNA; SERINE PROTEINASE INHIBITOR;

EID: 61849184076     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2008.12.010     Document Type: Article
Times cited : (97)

References (50)
  • 1
    • 0036470428 scopus 로고    scopus 로고
    • Evolution of enzyme cascades from embryonic development to blood coagulation
    • Krem M.M., and Di Cera E. Evolution of enzyme cascades from embryonic development to blood coagulation. Trends Biochem. Sci. 27 (2002) 67-74
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 67-74
    • Krem, M.M.1    Di Cera, E.2
  • 2
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • Jiang H., and Kanost M.R. The clip-domain family of serine proteinases in arthropods. Insect Biochem. Mol. Biol. 30 (2000) 95-105
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 3
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function
    • Irving J.A., Pike R.N., Lesk A.M., and Whisstock J.C. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res. 10 (2000) 1845-1864
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 4
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins P.G. Serpin structure, mechanism, and function. Chem. Rev. 102 (2002) 4751-4804
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 5
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington J.A., Read R.J., and Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407 (2000) 923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 6
    • 0021405056 scopus 로고
    • Isolation of two novel proteinase inhibitors from hemolymph of silkworm larva, Bombyx mori
    • Sasaki T., and Kobayashi K. Isolation of two novel proteinase inhibitors from hemolymph of silkworm larva, Bombyx mori. J. Biochem. 95 (1984) 1009-1117
    • (1984) J. Biochem. , vol.95 , pp. 1009-1117
    • Sasaki, T.1    Kobayashi, K.2
  • 7
    • 0026046935 scopus 로고
    • Patchwork-structure serpins from silkworm (Bombyx mori) larval hemolymph
    • Sasaki T. Patchwork-structure serpins from silkworm (Bombyx mori) larval hemolymph. Eur. J. Biochem. 202 (1991) 255-261
    • (1991) Eur. J. Biochem. , vol.202 , pp. 255-261
    • Sasaki, T.1
  • 8
    • 0024969423 scopus 로고
    • Primary structure of a member of the serpin superfamily of proteinase inhibitors from an insect, Manduca sexta
    • Kanost M.R., Prasad S.V., and Wells M.A. Primary structure of a member of the serpin superfamily of proteinase inhibitors from an insect, Manduca sexta. J. Biol. Chem. 264 (1989) 965-972
    • (1989) J. Biol. Chem. , vol.264 , pp. 965-972
    • Kanost, M.R.1    Prasad, S.V.2    Wells, M.A.3
  • 9
    • 0031012783 scopus 로고    scopus 로고
    • Characterization and functional analysis of 12 naturally occurring reactive site variants of serpin-1 from Manduca sexta
    • Jiang H., and Kanost M.R. Characterization and functional analysis of 12 naturally occurring reactive site variants of serpin-1 from Manduca sexta. J. Biol. Chem. 272 (1997) 1082-1087
    • (1997) J. Biol. Chem. , vol.272 , pp. 1082-1087
    • Jiang, H.1    Kanost, M.R.2
  • 10
    • 0035954672 scopus 로고    scopus 로고
    • A bacteria-induced, intracellular serpin in granular hemocytes of Manduca sexta
    • Gan H., Wang Y., Jiang H., Mita K., and Kanost M.R. A bacteria-induced, intracellular serpin in granular hemocytes of Manduca sexta. Insect Biochem. Mol. Biol. 31 (2001) 887-898
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 887-898
    • Gan, H.1    Wang, Y.2    Jiang, H.3    Mita, K.4    Kanost, M.R.5
  • 11
    • 0344875577 scopus 로고    scopus 로고
    • Manduca sexta serpin-3 regulates prophenoloxidase activation in response to infection by inhibiting prophenoloxidase-activating proteinases
    • Zhu Y., Wang Y., Gorman M.J., Jiang H., and Kanost M.R. Manduca sexta serpin-3 regulates prophenoloxidase activation in response to infection by inhibiting prophenoloxidase-activating proteinases. J. Biol. Chem. 278 (2003) 46556-46564
    • (2003) J. Biol. Chem. , vol.278 , pp. 46556-46564
    • Zhu, Y.1    Wang, Y.2    Gorman, M.J.3    Jiang, H.4    Kanost, M.R.5
  • 12
    • 17644379634 scopus 로고    scopus 로고
    • Identification of plasma proteases inhibited by Manduca sexta serpin-4 and serpin-5 and their association with components of the prophenol oxidase activation pathway
    • Tong Y., Jiang H., and Kanost M.R. Identification of plasma proteases inhibited by Manduca sexta serpin-4 and serpin-5 and their association with components of the prophenol oxidase activation pathway. J. Biol. Chem. 280 (2005) 14932-14942
    • (2005) J. Biol. Chem. , vol.280 , pp. 14932-14942
    • Tong, Y.1    Jiang, H.2    Kanost, M.R.3
  • 13
    • 1842539324 scopus 로고    scopus 로고
    • Purification and characterization of Manduca sexta serpin-6: a serine proteinase inhibitor that selectively inhibits prophenoloxidase-activating proteinase-3
    • Wang Y., and Jiang H. Purification and characterization of Manduca sexta serpin-6: a serine proteinase inhibitor that selectively inhibits prophenoloxidase-activating proteinase-3. Insect Biochem. Mol. Biol. 34 (2004) 387-395
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 387-395
    • Wang, Y.1    Jiang, H.2
  • 14
    • 0035933366 scopus 로고    scopus 로고
    • Purification and characterization of two serine protease inhibitors from the hemolymph of Mythimna unipuncta
    • Cherqui A., Cruz N., and Simoes N. Purification and characterization of two serine protease inhibitors from the hemolymph of Mythimna unipuncta. Insect Biochem. Mol. Biol. 31 (2001) 761-769
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 761-769
    • Cherqui, A.1    Cruz, N.2    Simoes, N.3
  • 15
    • 0032516888 scopus 로고    scopus 로고
    • Isolation and characterization of the gene encoding a novel factor Xa-directed anticoagulant from the yellow fever mosquito, Aedes aegypti
    • Stark K.R., and James A.A. Isolation and characterization of the gene encoding a novel factor Xa-directed anticoagulant from the yellow fever mosquito, Aedes aegypti. J. Biol. Chem. 273 (1998) 20802-20809
    • (1998) J. Biol. Chem. , vol.273 , pp. 20802-20809
    • Stark, K.R.1    James, A.A.2
  • 16
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost M.R. Serine proteinase inhibitors in arthropod immunity. Dev. Comp. Immunol. 23 (1999) 291-301
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 17
    • 44149112551 scopus 로고    scopus 로고
    • The biochemical basis of antimicrobial responses in Manduca sexta
    • Jiang H. The biochemical basis of antimicrobial responses in Manduca sexta. Insect Sci. 15 (2008) 53-66
    • (2008) Insect Sci. , vol.15 , pp. 53-66
    • Jiang, H.1
  • 18
    • 0141924388 scopus 로고    scopus 로고
    • Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs
    • Jiang H., Wang Y., Yu X.Q., Zhu Y., and Kanost M.R. Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs. Insect Biochem. Mol. Biol. 33 (2003) 1049-1060
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 1049-1060
    • Jiang, H.1    Wang, Y.2    Yu, X.Q.3    Zhu, Y.4    Kanost, M.R.5
  • 19
    • 17144374377 scopus 로고    scopus 로고
    • Manduca sexta serpin-6 regulates immune serine proteinases PAP-3 and HP8. cDNA cloning, protein expression, inhibition kinetics, and function elucidation
    • Zou Z., and Jiang H. Manduca sexta serpin-6 regulates immune serine proteinases PAP-3 and HP8. cDNA cloning, protein expression, inhibition kinetics, and function elucidation. J. Biol. Chem. 280 (2005) 14341-14348
    • (2005) J. Biol. Chem. , vol.280 , pp. 14341-14348
    • Zou, Z.1    Jiang, H.2
  • 20
    • 0033578917 scopus 로고    scopus 로고
    • Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila
    • Levashina E.A., et al. Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila. Science 285 (1999) 1917-1919
    • (1999) Science , vol.285 , pp. 1917-1919
    • Levashina, E.A.1
  • 21
    • 18644376155 scopus 로고    scopus 로고
    • An immune-responsive serpin regulates the melanization cascade in Drosophila
    • De Gregorio E., et al. An immune-responsive serpin regulates the melanization cascade in Drosophila. Dev. Cell 3 (2002) 581-592
    • (2002) Dev. Cell , vol.3 , pp. 581-592
    • De Gregorio, E.1
  • 22
    • 0037423382 scopus 로고    scopus 로고
    • Cloning and characterization of four Anopheles gambiae serpin isoforms, differentially induced in the midgut by Plasmodium berghei invasion
    • Danielli A., Kafatos F.C., and Loukeris T.G. Cloning and characterization of four Anopheles gambiae serpin isoforms, differentially induced in the midgut by Plasmodium berghei invasion. J. Biol. Chem. 278 (2003) 4184-4193
    • (2003) J. Biol. Chem. , vol.278 , pp. 4184-4193
    • Danielli, A.1    Kafatos, F.C.2    Loukeris, T.G.3
  • 23
    • 28044458306 scopus 로고    scopus 로고
    • An immune-responsive serpin, SRPN6, mediates mosquito defense against malaria parasites
    • Abraham E.G., et al. An immune-responsive serpin, SRPN6, mediates mosquito defense against malaria parasites. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 16327-16332
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16327-16332
    • Abraham, E.G.1
  • 24
    • 33750959610 scopus 로고    scopus 로고
    • Increased melanizing activity in Anopheles gambiae does not affect development of Plasmodium falciparum
    • Michel K., et al. Increased melanizing activity in Anopheles gambiae does not affect development of Plasmodium falciparum. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 16858-16863
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16858-16863
    • Michel, K.1
  • 27
    • 13844318276 scopus 로고    scopus 로고
    • Overexpression and altered nucleocytoplasmic distribution of Anopheles ovalbumin-like SRPN10 serpins in Plasmodium-infected midgut cells
    • Danielli A., Barillas-Mury C., Kumar S., Kafatos F.C., and Loukeris T.G. Overexpression and altered nucleocytoplasmic distribution of Anopheles ovalbumin-like SRPN10 serpins in Plasmodium-infected midgut cells. Cell. Microbiol. 7 (2005) 181-190
    • (2005) Cell. Microbiol. , vol.7 , pp. 181-190
    • Danielli, A.1    Barillas-Mury, C.2    Kumar, S.3    Kafatos, F.C.4    Loukeris, T.G.5
  • 28
    • 28044443956 scopus 로고    scopus 로고
    • Anopheles gambiae SRPN2 facilitates midgut invasion by the malaria parasite Plasmodium berghei
    • Michel K., Budd A., Pinto S., Gibson T.J., and Kafatos F.C. Anopheles gambiae SRPN2 facilitates midgut invasion by the malaria parasite Plasmodium berghei. EMBO Rep. 6 (2005) 891-897
    • (2005) EMBO Rep. , vol.6 , pp. 891-897
    • Michel, K.1    Budd, A.2    Pinto, S.3    Gibson, T.J.4    Kafatos, F.C.5
  • 29
    • 28244470961 scopus 로고    scopus 로고
    • Tip of another iceberg: Drosophila serpins
    • Reichhart J.M. Tip of another iceberg: Drosophila serpins. Trends Cell. Biol. 15 (2005) 659-665
    • (2005) Trends Cell. Biol. , vol.15 , pp. 659-665
    • Reichhart, J.M.1
  • 30
    • 0037020201 scopus 로고    scopus 로고
    • Immunity-related genes and gene families in Anopheles gambiae
    • Christophides G.K., et al. Immunity-related genes and gene families in Anopheles gambiae. Science 298 (2002) 159-165
    • (2002) Science , vol.298 , pp. 159-165
    • Christophides, G.K.1
  • 31
    • 34250860637 scopus 로고    scopus 로고
    • Evolutionary dynamics of immune-related genes and pathways in disease-vector mosquitoes
    • Waterhouse R.M., et al. Evolutionary dynamics of immune-related genes and pathways in disease-vector mosquitoes. Science 316 (2007) 1738-1743
    • (2007) Science , vol.316 , pp. 1738-1743
    • Waterhouse, R.M.1
  • 32
    • 33750477010 scopus 로고    scopus 로고
    • Comparative analysis of serine protease-related genes in the honey bee genome: possible involvement in embryonic development and innate immunity
    • Zou Z., Lopez D.L., Kanost M.R., Evans J.D., and Jiang H. Comparative analysis of serine protease-related genes in the honey bee genome: possible involvement in embryonic development and innate immunity. Insect Mol. Biol. 15 (2006) 603-614
    • (2006) Insect Mol. Biol. , vol.15 , pp. 603-614
    • Zou, Z.1    Lopez, D.L.2    Kanost, M.R.3    Evans, J.D.4    Jiang, H.5
  • 33
    • 36749066016 scopus 로고    scopus 로고
    • Comparative genomic analysis of the Tribolium immune system
    • Zou Z., et al. Comparative genomic analysis of the Tribolium immune system. Genome Biol. 8 (2007) R177
    • (2007) Genome Biol. , vol.8
    • Zou, Z.1
  • 34
    • 10344265019 scopus 로고    scopus 로고
    • A draft sequence for the genome of the domesticated silkworm (Bombyx mori)
    • Xia Q., et al. A draft sequence for the genome of the domesticated silkworm (Bombyx mori). Science 306 (2004) 1937-1940
    • (2004) Science , vol.306 , pp. 1937-1940
    • Xia, Q.1
  • 35
    • 5144229657 scopus 로고    scopus 로고
    • The genome sequence of silkworm, Bombyx mori
    • Mita K., et al. The genome sequence of silkworm, Bombyx mori. DNA Res. 11 (2004) 27-35
    • (2004) DNA Res. , vol.11 , pp. 27-35
    • Mita, K.1
  • 36
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: a DNA sequence assembly program
    • Huang X., and Madan A. CAP3: a DNA sequence assembly program. Genome Res. 9 (1999) 868-877
    • (1999) Genome Res. , vol.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 37
    • 0027182969 scopus 로고
    • Effects of mutations in the hinge region of serpins
    • Hopkins P.C., Carrell R.W., and Stone S.R. Effects of mutations in the hinge region of serpins. Biochemistry 32 (1993) 7650-7657
    • (1993) Biochemistry , vol.32 , pp. 7650-7657
    • Hopkins, P.C.1    Carrell, R.W.2    Stone, S.R.3
  • 38
    • 38549101559 scopus 로고    scopus 로고
    • The role of serpins in the surveillance of the secretory pathway
    • Ragg H. The role of serpins in the surveillance of the secretory pathway. Cell Mol. Life Sci. 64 (2007) 2763-2770
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 2763-2770
    • Ragg, H.1
  • 39
    • 34247093851 scopus 로고    scopus 로고
    • Studies on middle and posterior silk glands of silkworm (Bombyx mori) using two-dimensional electrophoresis and mass spectrometry
    • Hou Y., et al. Studies on middle and posterior silk glands of silkworm (Bombyx mori) using two-dimensional electrophoresis and mass spectrometry. Insect Biochem. Mol. Biol. 37 (2007) 486-496
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 486-496
    • Hou, Y.1
  • 41
    • 0346493030 scopus 로고    scopus 로고
    • Computational analysis of evolution and conservation in a protein superfamily
    • Irving J.A., Askew D.J., and Whisstock J.C. Computational analysis of evolution and conservation in a protein superfamily. Nature Methods 32 (2004) 73-92
    • (2004) Nature Methods , vol.32 , pp. 73-92
    • Irving, J.A.1    Askew, D.J.2    Whisstock, J.C.3
  • 42
    • 33747862007 scopus 로고    scopus 로고
    • An overview of the serpin superfamily
    • Law R.H., et al. An overview of the serpin superfamily. Genome Biol. 7 (2006) 216
    • (2006) Genome Biol. , vol.7 , pp. 216
    • Law, R.H.1
  • 43
    • 4644325614 scopus 로고    scopus 로고
    • Serpins in unicellular eukarya, archaea, and bacteria: sequence analysis and evolution
    • Roberts T.H., Hejgaard J., Saunders N.F., Cavicchioli R., and Curmi P.M. Serpins in unicellular eukarya, archaea, and bacteria: sequence analysis and evolution. J. Mol. Evol. 59 (2004) 437-447
    • (2004) J. Mol. Evol. , vol.59 , pp. 437-447
    • Roberts, T.H.1    Hejgaard, J.2    Saunders, N.F.3    Cavicchioli, R.4    Curmi, P.M.5
  • 45
    • 0037178277 scopus 로고    scopus 로고
    • Widespread occurrence of serpin genes with multiple reactive centre-containing exon cassettes in insects and nematodes
    • Krüger O., Ladewig J., Köster K., and Ragg H. Widespread occurrence of serpin genes with multiple reactive centre-containing exon cassettes in insects and nematodes. Gene 293 (2002) 97-105
    • (2002) Gene , vol.293 , pp. 97-105
    • Krüger, O.1    Ladewig, J.2    Köster, K.3    Ragg, H.4
  • 46
    • 44949147879 scopus 로고    scopus 로고
    • Differential expansion and evolution of the exon family encoding the serpin-1 reactive centre loop has resulted in divergent serpin repertoires among the Lepidoptera
    • Hegedus D.D., Erlandson M., Baldwin D., Hou X., and Chamankhah M. Differential expansion and evolution of the exon family encoding the serpin-1 reactive centre loop has resulted in divergent serpin repertoires among the Lepidoptera. Gene 418 (2008) 15-21
    • (2008) Gene , vol.418 , pp. 15-21
    • Hegedus, D.D.1    Erlandson, M.2    Baldwin, D.3    Hou, X.4    Chamankhah, M.5
  • 47
    • 0029953513 scopus 로고    scopus 로고
    • Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop
    • Jiang H., et al. Organization of serpin gene-1 from Manduca sexta. Evolution of a family of alternate exons encoding the reactive site loop. J. Biol. Chem. 271 (1996) 28017-28023
    • (1996) J. Biol. Chem. , vol.271 , pp. 28017-28023
    • Jiang, H.1
  • 48
    • 28544440426 scopus 로고    scopus 로고
    • Analysis of vertebrate genomes suggests a new model for clade B serpin evolution
    • Kaiserman D., and Bird P.I. Analysis of vertebrate genomes suggests a new model for clade B serpin evolution. BMC Genomics 6 (2005) 167
    • (2005) BMC Genomics , vol.6 , pp. 167
    • Kaiserman, D.1    Bird, P.I.2
  • 50
    • 0141509877 scopus 로고    scopus 로고
    • Conserved Ser residues, the shutter region, and speciation in serpin evolution
    • Krem M.M., and Di Cera E. Conserved Ser residues, the shutter region, and speciation in serpin evolution. J. Biol. Chem. 278 (2003) 37810-37814
    • (2003) J. Biol. Chem. , vol.278 , pp. 37810-37814
    • Krem, M.M.1    Di Cera, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.