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Volumn 31, Issue 11, 2007, Pages 1168-1182

Molecular cloning, structural analysis and expression of complement component Bf/C2 genes in the nurse shark, Ginglymostoma cirratum

Author keywords

Complement C2; Evolution; Factor B; Gene cloning; Ginglymostoma cirratum; Phylogenetics; Shark complement

Indexed keywords

ALTERNATIVE COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C2; COMPLEMENTARY DNA; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; SERINE PROTEINASE; SIGNAL PEPTIDE;

EID: 35348858079     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2007.03.001     Document Type: Article
Times cited : (20)

References (51)
  • 1
    • 0019364862 scopus 로고
    • The proteolytic activation system of complement
    • Reid K.B.M., and Porter R.R. The proteolytic activation system of complement. Ann Rev Biochem 50 (1981) 433
    • (1981) Ann Rev Biochem , vol.50 , pp. 433
    • Reid, K.B.M.1    Porter, R.R.2
  • 2
    • 0035023198 scopus 로고    scopus 로고
    • Structural biology of the alternative pathway convertase
    • Volanakis J.E. Structural biology of the alternative pathway convertase. Immunol Rev 180 (2001) 123-135
    • (2001) Immunol Rev , vol.180 , pp. 123-135
    • Volanakis, J.E.1
  • 3
    • 0023204278 scopus 로고
    • The catalytic role of the active site aspartic acid in serine proteases
    • Craik C.S., Roczniak S., Largman C., and Rutter W.J. The catalytic role of the active site aspartic acid in serine proteases. Science 237 (1987) 909-913
    • (1987) Science , vol.237 , pp. 909-913
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 4
    • 0028914722 scopus 로고    scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona J.J., and Craik C.S. Structural basis of substrate specificity in the serine proteases. Protein Sci 4 (1997) 337-360
    • (1997) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 5
    • 0024487453 scopus 로고
    • C3 convertase of complement: molecular genetics, structure and function of the catalytic domains, C2 and B
    • Cruse J.M., and Lewis Jr. R.E. (Eds), Karger Press, Basel
    • Volanakis J.E. C3 convertase of complement: molecular genetics, structure and function of the catalytic domains, C2 and B. In: Cruse J.M., and Lewis Jr. R.E. (Eds). The year in immunology 1988: cellular, molecular and clinical aspects (1989), Karger Press, Basel 218
    • (1989) The year in immunology 1988: cellular, molecular and clinical aspects , pp. 218
    • Volanakis, J.E.1
  • 6
    • 0027139795 scopus 로고
    • Human complement factor B: cDNA cloning, nucleotide sequencing, phenotype conversion by site-directed mutagenesis and expression
    • Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S., and Volanakis J.E. Human complement factor B: cDNA cloning, nucleotide sequencing, phenotype conversion by site-directed mutagenesis and expression. Mol Immunol 30 (1993) 1587-1592
    • (1993) Mol Immunol , vol.30 , pp. 1587-1592
    • Horiuchi, T.1    Kim, S.2    Matsumoto, M.3    Watanabe, I.4    Fujita, S.5    Volanakis, J.E.6
  • 7
    • 0030948650 scopus 로고    scopus 로고
    • Surface loops adjacent to the cation-binding site of the complement factor B-von Willebrand factor type A module determine C3b binding specificity
    • Tuckwell D.S., Xu Y., Newham P., Humphries M.J., and Volanakis J.E. Surface loops adjacent to the cation-binding site of the complement factor B-von Willebrand factor type A module determine C3b binding specificity. Biochemistry 36 (1997) 6605-6613
    • (1997) Biochemistry , vol.36 , pp. 6605-6613
    • Tuckwell, D.S.1    Xu, Y.2    Newham, P.3    Humphries, M.J.4    Volanakis, J.E.5
  • 8
    • 0029086243 scopus 로고
    • Analysis of the short consensus repeats of human complement factor B by directed mutagenesis
    • Hourcade D.E., Wagner L.M., and Oglesby T.J. Analysis of the short consensus repeats of human complement factor B by directed mutagenesis. J Biol Chem 270 (1995) 19716-19722
    • (1995) J Biol Chem , vol.270 , pp. 19716-19722
    • Hourcade, D.E.1    Wagner, L.M.2    Oglesby, T.J.3
  • 9
    • 0031570468 scopus 로고    scopus 로고
    • Contribution of the complement control protein modules of C2 in C4b binding assessed by analysis of C2/Bf chimeras
    • Xu Y., and Volanakis J.E. Contribution of the complement control protein modules of C2 in C4b binding assessed by analysis of C2/Bf chimeras. J Immunol 158 (1997) 5958-5965
    • (1997) J Immunol , vol.158 , pp. 5958-5965
    • Xu, Y.1    Volanakis, J.E.2
  • 10
    • 0344022441 scopus 로고
    • Structure and organization of complement genes
    • Whaley K., Loos M., and Weiler J.M. (Eds), Kluwer Academic Publishers, Lancaster, UK
    • Reid K.B.M., and Campbell R.D. Structure and organization of complement genes. In: Whaley K., Loos M., and Weiler J.M. (Eds). Complement in health and disease (1993), Kluwer Academic Publishers, Lancaster, UK 89-125
    • (1993) Complement in health and disease , pp. 89-125
    • Reid, K.B.M.1    Campbell, R.D.2
  • 11
    • 0019721708 scopus 로고
    • The complement system of the nurse shark: hemolytic and comparative characteristics
    • Jensen J.A., Festa E., Cayer M., and Smith D.S. The complement system of the nurse shark: hemolytic and comparative characteristics. Science 214 (1981) 566-569
    • (1981) Science , vol.214 , pp. 566-569
    • Jensen, J.A.1    Festa, E.2    Cayer, M.3    Smith, D.S.4
  • 12
    • 0032415095 scopus 로고    scopus 로고
    • Shark complement: an assessment
    • Smith S.L. Shark complement: an assessment. Immunol Rev 166 (1998) 67-78
    • (1998) Immunol Rev , vol.166 , pp. 67-78
    • Smith, S.L.1
  • 13
    • 0022467696 scopus 로고
    • Primary structure of human complement component C2: homology to two unrelated protein families
    • Bently D.R. Primary structure of human complement component C2: homology to two unrelated protein families. Biochem J 239 (1986) 339-345
    • (1986) Biochem J , vol.239 , pp. 339-345
    • Bently, D.R.1
  • 14
    • 0021348357 scopus 로고
    • Complete primary structure for the zymogen of human complement factor B
    • Mole J.E., Anderson J.K., Davison E.A., and Woods D.E. Complete primary structure for the zymogen of human complement factor B. J Biol Chem 259 (1984) 3407-3412
    • (1984) J Biol Chem , vol.259 , pp. 3407-3412
    • Mole, J.E.1    Anderson, J.K.2    Davison, E.A.3    Woods, D.E.4
  • 15
    • 0025131406 scopus 로고
    • Murine complement C2 and factor B genomic and cDNA cloning reveals different mechanisms for multiple transcripts of C2 and B
    • Ishikawa N., Nonaka M., Wetsel R.A., and Colten H.R. Murine complement C2 and factor B genomic and cDNA cloning reveals different mechanisms for multiple transcripts of C2 and B. J Biol Chem 265 (1990) 19040-19046
    • (1990) J Biol Chem , vol.265 , pp. 19040-19046
    • Ishikawa, N.1    Nonaka, M.2    Wetsel, R.A.3    Colten, H.R.4
  • 16
    • 0028034701 scopus 로고
    • Isolation of the Xenopus complement factor B complementary DNA and linkage of the gene to the frog MHC
    • Kato Y., Salter-Cid L., Flajnik M.F., Kasahara M., Namikawa C., Sasaki M., et al. Isolation of the Xenopus complement factor B complementary DNA and linkage of the gene to the frog MHC. J Immunol 153 (1994) 4546-4554
    • (1994) J Immunol , vol.153 , pp. 4546-4554
    • Kato, Y.1    Salter-Cid, L.2    Flajnik, M.F.3    Kasahara, M.4    Namikawa, C.5    Sasaki, M.6
  • 17
    • 0028220653 scopus 로고
    • Molecular cloning of a lamprey homologue of the mammalian MHC class III gene, complement factor B
    • Nonaka M., Takahashi M., and Sasaki M. Molecular cloning of a lamprey homologue of the mammalian MHC class III gene, complement factor B. J Immunol 152 (1994) 2263-2269
    • (1994) J Immunol , vol.152 , pp. 2263-2269
    • Nonaka, M.1    Takahashi, M.2    Sasaki, M.3
  • 18
    • 0032213265 scopus 로고    scopus 로고
    • Two diverged complement factor B/C2-like cDNA sequences from a teleost, the common carp (Cyprinus carpio)
    • Nakao M., Fushitani Y., Fujiki K., Nonaka M., and Yano T. Two diverged complement factor B/C2-like cDNA sequences from a teleost, the common carp (Cyprinus carpio). J Immunol 161 (1996) 4811-4818
    • (1996) J Immunol , vol.161 , pp. 4811-4818
    • Nakao, M.1    Fushitani, Y.2    Fujiki, K.3    Nonaka, M.4    Yano, T.5
  • 19
    • 0036258779 scopus 로고    scopus 로고
    • Diversity of complement factor B/C2 in the common carp (Cyprinus carpio): three isotopes of B/C2-A expressed in different tissues
    • Nakao M., Matsumoto M., Nakazawa M., Fujiki K., and Yano T. Diversity of complement factor B/C2 in the common carp (Cyprinus carpio): three isotopes of B/C2-A expressed in different tissues. Dev Comp Immunol 26 (2002) 533-541
    • (2002) Dev Comp Immunol , vol.26 , pp. 533-541
    • Nakao, M.1    Matsumoto, M.2    Nakazawa, M.3    Fujiki, K.4    Yano, T.5
  • 20
    • 0029792046 scopus 로고    scopus 로고
    • Molecular cloning and linkage analysis of the Japanese medaka fish complement Bf/C2 gene
    • Kuroda N., Wada H., Naruse K., Simada A., Shima A., Sasaki M., et al. Molecular cloning and linkage analysis of the Japanese medaka fish complement Bf/C2 gene. Immunogenetics 44 (1996) 459-467
    • (1996) Immunogenetics , vol.44 , pp. 459-467
    • Kuroda, N.1    Wada, H.2    Naruse, K.3    Simada, A.4    Shima, A.5    Sasaki, M.6
  • 21
    • 0030130850 scopus 로고    scopus 로고
    • A complement factor B-like cDNA clone from the zebrafish (Brachydanio rerio)
    • Seeger A., Mayer W.E., and Klein J. A complement factor B-like cDNA clone from the zebrafish (Brachydanio rerio). Mol Immunol 33 (1996) 511-520
    • (1996) Mol Immunol , vol.33 , pp. 511-520
    • Seeger, A.1    Mayer, W.E.2    Klein, J.3
  • 22
  • 23
    • 0022891544 scopus 로고
    • Macrophage-like effector of spontaneous cytotoxicity from the shark
    • Mckinney E.C., Haynes L., and Droese A.L. Macrophage-like effector of spontaneous cytotoxicity from the shark. Dev Comp Immunol 10 (1986) 497-508
    • (1986) Dev Comp Immunol , vol.10 , pp. 497-508
    • Mckinney, E.C.1    Haynes, L.2    Droese, A.L.3
  • 24
  • 25
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl Acids Res 24 (1997) 4876-4882
    • (1997) Nucl Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 27
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4 (1987) 406-425
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 28
    • 0032534585 scopus 로고    scopus 로고
    • Coelomocytes express SpBf, a homologue of factor B, the second complement in the sea urchin complement system
    • Smith L.C., Shih C.S., and Dachemhausen S.G. Coelomocytes express SpBf, a homologue of factor B, the second complement in the sea urchin complement system. J Immunol 161 (1998) 6784-6793
    • (1998) J Immunol , vol.161 , pp. 6784-6793
    • Smith, L.C.1    Shih, C.S.2    Dachemhausen, S.G.3
  • 29
    • 0035005842 scopus 로고    scopus 로고
    • Occurrence of structural specialization of the serine protease domain of complement factor B at the emergence of jawed vertebrates and adaptive immunity
    • Terado T., Smith S.L., Nakanhishi T., Nomaka M.I., Kimura H., and Nonaka M. Occurrence of structural specialization of the serine protease domain of complement factor B at the emergence of jawed vertebrates and adaptive immunity. Immunogenetics 53 (2001) 250-254
    • (2001) Immunogenetics , vol.53 , pp. 250-254
    • Terado, T.1    Smith, S.L.2    Nakanhishi, T.3    Nomaka, M.I.4    Kimura, H.5    Nonaka, M.6
  • 30
    • 16844378226 scopus 로고    scopus 로고
    • Structure and the evolutionary implication of the triplicated complement factor B genes of a urochordate ascidian, Ciona intestinalis
    • Yoshizaki F.Y., Ikawa S., Satake M., Satou N., and Nonaka M. Structure and the evolutionary implication of the triplicated complement factor B genes of a urochordate ascidian, Ciona intestinalis. Immunogenetics 56 (2005) 930-942
    • (2005) Immunogenetics , vol.56 , pp. 930-942
    • Yoshizaki, F.Y.1    Ikawa, S.2    Satake, M.3    Satou, N.4    Nonaka, M.5
  • 31
    • 0002875849 scopus 로고    scopus 로고
    • Molecular cloning of complement factor B from a solitary ascidian: unique combination of domains implicating ancient exon shufflings (abstract)
    • Ji X., Namikawa-Yamada C., Nakanishi M., Sasaki M., and Nonaka M. Molecular cloning of complement factor B from a solitary ascidian: unique combination of domains implicating ancient exon shufflings (abstract). Immunopharmacology 49 (2000) 43
    • (2000) Immunopharmacology , vol.49 , pp. 43
    • Ji, X.1    Namikawa-Yamada, C.2    Nakanishi, M.3    Sasaki, M.4    Nonaka, M.5
  • 32
    • 0017324044 scopus 로고
    • Serine proteases: structure and mechanism of catalysis
    • Kraut J. Serine proteases: structure and mechanism of catalysis. Ann Rev Biochem 46 (1977) 331-358
    • (1977) Ann Rev Biochem , vol.46 , pp. 331-358
    • Kraut, J.1
  • 34
    • 0023719006 scopus 로고
    • Evidence for a C4b binding site on the C2b domain of C2
    • Oglesby T.J., Accavitti M.A., and Volanakis J.E. Evidence for a C4b binding site on the C2b domain of C2. J Immunol 141 (1988) 926-931
    • (1988) J Immunol , vol.141 , pp. 926-931
    • Oglesby, T.J.1    Accavitti, M.A.2    Volanakis, J.E.3
  • 35
    • 0024561914 scopus 로고
    • Structure-function relationships of the complement components
    • Reid K.B., and Day A.J. Structure-function relationships of the complement components. Immunol Today 10 (1989) 177-180
    • (1989) Immunol Today , vol.10 , pp. 177-180
    • Reid, K.B.1    Day, A.J.2
  • 36
    • 0030759097 scopus 로고    scopus 로고
    • The tortous story of Asp...... His...... Ser: structural analysis of alpha-chymotrypsin
    • Blow D.M. The tortous story of Asp...... His...... Ser: structural analysis of alpha-chymotrypsin. Trends Biochem Sci 22 (1997) 405-408
    • (1997) Trends Biochem Sci , vol.22 , pp. 405-408
    • Blow, D.M.1
  • 37
    • 0014945734 scopus 로고
    • Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme
    • Henderson R. Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J Mol Biol 54 (1970) 341-354
    • (1970) J Mol Biol , vol.54 , pp. 341-354
    • Henderson, R.1
  • 38
    • 0034677208 scopus 로고    scopus 로고
    • New structural motifs on the chymotrypsin fold and their potential roles in complement factor B
    • Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E., et al. New structural motifs on the chymotrypsin fold and their potential roles in complement factor B. EMBO J 19 (2000) 164-173
    • (2000) EMBO J , vol.19 , pp. 164-173
    • Jing, H.1    Xu, Y.2    Carson, M.3    Moore, D.4    Macon, K.J.5    Volanakis, J.E.6
  • 39
    • 0017056107 scopus 로고
    • Specificity of trypsin and alpha-chymotrypsin towards neutral substrates
    • Vajda T., and Szabo T. Specificity of trypsin and alpha-chymotrypsin towards neutral substrates. Acta Biochim Biophys Acad Sci Hung 11 (1976) 287-294
    • (1976) Acta Biochim Biophys Acad Sci Hung , vol.11 , pp. 287-294
    • Vajda, T.1    Szabo, T.2
  • 40
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: the role of surface loops
    • Hedstrom L., Szilagyi L., and Rutter W.J. Converting trypsin to chymotrypsin: the role of surface loops. Science 255 (1992) 1249-1253
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstrom, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 41
    • 0029832603 scopus 로고    scopus 로고
    • Trypsin: a case study in the structural determinants of enzyme specificity
    • Hedstrom L. Trypsin: a case study in the structural determinants of enzyme specificity. Biol Chem 377 (1996) 465-470
    • (1996) Biol Chem , vol.377 , pp. 465-470
    • Hedstrom, L.1
  • 42
    • 23244458844 scopus 로고    scopus 로고
    • Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant
    • Ma W., Tang C., and Lai L. Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant. Biophys J 89 (2005) 1183-1193
    • (2005) Biophys J , vol.89 , pp. 1183-1193
    • Ma, W.1    Tang, C.2    Lai, L.3
  • 43
    • 0034614640 scopus 로고    scopus 로고
    • Mutational analysis of the primary substrate specificity pocket of complement factor B: Asp226 is a major structural determinant for P1-Arg binding
    • Xu Y., Circolo A., Jing H., Wang Y., Narayana S.V.L., and Volanakis J.E. Mutational analysis of the primary substrate specificity pocket of complement factor B: Asp226 is a major structural determinant for P1-Arg binding. J Biol Chem (2000)
    • (2000) J Biol Chem
    • Xu, Y.1    Circolo, A.2    Jing, H.3    Wang, Y.4    Narayana, S.V.L.5    Volanakis, J.E.6
  • 44
    • 0025895079 scopus 로고
    • Site directed mutagenesis of the region around Cys-241 of complement component C2
    • Horiuchi T., Macon K.J., Engler J.A., and Volanakis J.E. Site directed mutagenesis of the region around Cys-241 of complement component C2. J Immunol 147 (1991) 584-589
    • (1991) J Immunol , vol.147 , pp. 584-589
    • Horiuchi, T.1    Macon, K.J.2    Engler, J.A.3    Volanakis, J.E.4
  • 45
    • 0021745965 scopus 로고
    • Isolation and characterization of a 33,000-dalton fragment of complement factor B with catalytic and C3b binding activity
    • Lambris J.D., and Müller-Eberhard H.J. Isolation and characterization of a 33,000-dalton fragment of complement factor B with catalytic and C3b binding activity. J Biol Chem 259 (1984) 12685-12690
    • (1984) J Biol Chem , vol.259 , pp. 12685-12690
    • Lambris, J.D.1    Müller-Eberhard, H.J.2
  • 46
    • 0025103056 scopus 로고
    • Proteolytic activity of the different fragments of factor B on the third complements of complement (C3). Involvement of the N-terminal domain of Bb in magnesium binding
    • Sanchez-Coraal P., Anton L.C., Alcolea J.M., Marques G., Sanchez A., and Vivanco F. Proteolytic activity of the different fragments of factor B on the third complements of complement (C3). Involvement of the N-terminal domain of Bb in magnesium binding. Mol Immunol 27 (1990) 891-900
    • (1990) Mol Immunol , vol.27 , pp. 891-900
    • Sanchez-Coraal, P.1    Anton, L.C.2    Alcolea, J.M.3    Marques, G.4    Sanchez, A.5    Vivanco, F.6
  • 47
    • 0027519943 scopus 로고
    • Protein glycosylation: structural and functional aspects
    • Lis H., and Sharon N. Protein glycosylation: structural and functional aspects. Curr J Biochem 218 (1993) 1-27
    • (1993) Curr J Biochem , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 48
    • 0030006293 scopus 로고    scopus 로고
    • O-linked protein glycosylation structure and function
    • Hounsell E.F., Davies M.J., and Renouf D.V. O-linked protein glycosylation structure and function. Glycoconjugate J 13 (1996) 19-26
    • (1996) Glycoconjugate J , vol.13 , pp. 19-26
    • Hounsell, E.F.1    Davies, M.J.2    Renouf, D.V.3
  • 50
    • 0015341001 scopus 로고
    • Replacement of asparagine by aspartic acid in hen ovalbumin and a difference in immunochemical reactivity
    • Weisman R.L., Fothergill J.E., and Fothergill L.A. Replacement of asparagine by aspartic acid in hen ovalbumin and a difference in immunochemical reactivity. Biochem J 127 (1972) 775-780
    • (1972) Biochem J , vol.127 , pp. 775-780
    • Weisman, R.L.1    Fothergill, J.E.2    Fothergill, L.A.3
  • 51
    • 0024514446 scopus 로고
    • cDNA cloning and expression of human complement component C2
    • Horiuchi T., Macon K.J., Kidd V.J., and Volanakis J.E. cDNA cloning and expression of human complement component C2. J Immunol 142 (1989) 2105-2111
    • (1989) J Immunol , vol.142 , pp. 2105-2111
    • Horiuchi, T.1    Macon, K.J.2    Kidd, V.J.3    Volanakis, J.E.4


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