메뉴 건너뛰기




Volumn 91, Issue 2, 2008, Pages 129-141

Phylogenetic analysis of vertebrate kininogen genes

Author keywords

Alternative splicing; Bradykinin; Evolutionary dynamics; Gene duplication; Gene structure; Kininogen

Indexed keywords

BRADYKININ; BRADYKININ RECEPTOR; KININOGEN; SIGNAL PEPTIDE;

EID: 38349076324     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2007.10.007     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 0014223386 scopus 로고
    • Structural features of plasma kinins and kininogens
    • Pierce J.V. Structural features of plasma kinins and kininogens. Fed. Proc. 27 (1968) 52-57
    • (1968) Fed. Proc. , vol.27 , pp. 52-57
    • Pierce, J.V.1
  • 2
    • 0014743975 scopus 로고
    • Studies on the structure of bovine kininogen: cleavages of disulfide bonds and of methionyl bonds in kininogen-II
    • Kato H., Nagasawa S., and Suzuki T. Studies on the structure of bovine kininogen: cleavages of disulfide bonds and of methionyl bonds in kininogen-II. J. Biochem. 67 (1970) 313-323
    • (1970) J. Biochem. , vol.67 , pp. 313-323
    • Kato, H.1    Nagasawa, S.2    Suzuki, T.3
  • 3
    • 0022356775 scopus 로고
    • Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin: structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor
    • Furuto-Kato S., Matsumoto A., Kitamura N., and Nakanishi S. Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin: structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor. J. Biol. Chem. 260 (1985) 12054-12059
    • (1985) J. Biol. Chem. , vol.260 , pp. 12054-12059
    • Furuto-Kato, S.1    Matsumoto, A.2    Kitamura, N.3    Nakanishi, S.4
  • 4
    • 0030976652 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs for mouse low-molecular-weight and high-molecular-weight prekininogens
    • Takano M., et al. Molecular cloning of cDNAs for mouse low-molecular-weight and high-molecular-weight prekininogens. Biochim. Biophys. Acta 1352 (1997) 222-230
    • (1997) Biochim. Biophys. Acta , vol.1352 , pp. 222-230
    • Takano, M.1
  • 5
    • 0033994627 scopus 로고    scopus 로고
    • Whale high-molecular-weight and low-molecular-weight kininogens
    • Semba U., Shibuya Y., Okabe H., Hayashi I., and Yamamoto T. Whale high-molecular-weight and low-molecular-weight kininogens. Thromb. Res. 97 (2000) 481-490
    • (2000) Thromb. Res. , vol.97 , pp. 481-490
    • Semba, U.1    Shibuya, Y.2    Okabe, H.3    Hayashi, I.4    Yamamoto, T.5
  • 6
    • 0034810752 scopus 로고    scopus 로고
    • A novel bradykinin-related peptide from skin secretions of toad Bombina maxima and its precursor containing six identical copies of the final product
    • Lai R., Liu H., Lee W.H., and Zhang Y. A novel bradykinin-related peptide from skin secretions of toad Bombina maxima and its precursor containing six identical copies of the final product. Biochem. Biophys. Res. Commun. 286 (2001) 259-263
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 259-263
    • Lai, R.1    Liu, H.2    Lee, W.H.3    Zhang, Y.4
  • 7
    • 0036711249 scopus 로고    scopus 로고
    • Bradykinins and their precursor cDNAs from the skin of the fire-bellied toad (Bombina orientalis)
    • Chen T.B., et al. Bradykinins and their precursor cDNAs from the skin of the fire-bellied toad (Bombina orientalis). Peptides 23 (2002) 1547-1555
    • (2002) Peptides , vol.23 , pp. 1547-1555
    • Chen, T.B.1
  • 8
    • 0036380755 scopus 로고    scopus 로고
    • Novel bradykinins and their precursor cDNAs from European yellow-bellied toad (Bombina variegata) skin
    • Chen T.B., et al. Novel bradykinins and their precursor cDNAs from European yellow-bellied toad (Bombina variegata) skin. Eur. J. Biochem. 269 (2002) 4693-4700
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4693-4700
    • Chen, T.B.1
  • 9
    • 0037303368 scopus 로고    scopus 로고
    • Bombinakinin M gene associated peptide, a novel bioactive peptide from skin secretions of the toad Bombina maxima
    • Lai R., Liu H., Lee W.H., and Zhang Y. Bombinakinin M gene associated peptide, a novel bioactive peptide from skin secretions of the toad Bombina maxima. Peptides 24 (2003) 199-204
    • (2003) Peptides , vol.24 , pp. 199-204
    • Lai, R.1    Liu, H.2    Lee, W.H.3    Zhang, Y.4
  • 10
    • 0041929613 scopus 로고    scopus 로고
    • Cloning of maximakinin precursor cDNAs from Chinese toad, Bombina maxima, venom
    • Chen T.B., et al. Cloning of maximakinin precursor cDNAs from Chinese toad, Bombina maxima, venom. Peptides 24 (2003) 853-861
    • (2003) Peptides , vol.24 , pp. 853-861
    • Chen, T.B.1
  • 11
    • 0041428178 scopus 로고    scopus 로고
    • Bradykinins and their cDNA from piebald odorous frog, Odorrana schmackeri, skin
    • Li L., et al. Bradykinins and their cDNA from piebald odorous frog, Odorrana schmackeri, skin. Peptides 24 (2003) 863-872
    • (2003) Peptides , vol.24 , pp. 863-872
    • Li, L.1
  • 12
    • 0242495081 scopus 로고    scopus 로고
    • Cloning of the (Thr6)-phyllokinin precursor from Phyllomedusa sauvagei skin confirms a non-consensus tyrosine O-sulfation motif
    • Chen T.B., and Shaw C. Cloning of the (Thr6)-phyllokinin precursor from Phyllomedusa sauvagei skin confirms a non-consensus tyrosine O-sulfation motif. Peptides 24 (2003) 1123-1130
    • (2003) Peptides , vol.24 , pp. 1123-1130
    • Chen, T.B.1    Shaw, C.2
  • 13
    • 33746933811 scopus 로고    scopus 로고
    • Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis
    • Chen T.B., Zhou M., Gagliardo R., Walker B., and Shaw C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. Peptides 27 (2006) 2129-2136
    • (2006) Peptides , vol.27 , pp. 2129-2136
    • Chen, T.B.1    Zhou, M.2    Gagliardo, R.3    Walker, B.4    Shaw, C.5
  • 14
    • 33750048776 scopus 로고    scopus 로고
    • A novel bradykinin-like peptide from skin secretions of rufous-spotted torrent frog, Amolops loloensis
    • Liang J.G., Han Y., Li J.X., Xu X.Q., Rees H.H., and Lai R. A novel bradykinin-like peptide from skin secretions of rufous-spotted torrent frog, Amolops loloensis. Peptides 27 (2006) 2683-2687
    • (2006) Peptides , vol.27 , pp. 2683-2687
    • Liang, J.G.1    Han, Y.2    Li, J.X.3    Xu, X.Q.4    Rees, H.H.5    Lai, R.6
  • 15
    • 33845572736 scopus 로고    scopus 로고
    • Bradykinin-related peptides from Phyllomedusa hypochondrialis azurea: mass spectrometric structural characterisation and cloning of precursor cDNAs
    • Thompson A.H., Bjourson A.J., Shaw C., and McClean S. Bradykinin-related peptides from Phyllomedusa hypochondrialis azurea: mass spectrometric structural characterisation and cloning of precursor cDNAs. Rapid Commun. Mass Spectrom. 20 (2006) 3780-3788
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 3780-3788
    • Thompson, A.H.1    Bjourson, A.J.2    Shaw, C.3    McClean, S.4
  • 16
    • 33847372913 scopus 로고    scopus 로고
    • 1)-bradykinin, from the skin secretion of Guenther's frog, Hylarana guentheri and their molecular precursors
    • 1)-bradykinin, from the skin secretion of Guenther's frog, Hylarana guentheri and their molecular precursors. Peptides 28 (2007) 781-789
    • (2007) Peptides , vol.28 , pp. 781-789
    • Zhou, J.W.1
  • 17
    • 34249691187 scopus 로고    scopus 로고
    • The complex array of bradykinin-related peptides (BRPs) in the peptidome of pickerel frog (Rana palustris) skin secretion is the product of transcriptional economy
    • McCrudden C.M., et al. The complex array of bradykinin-related peptides (BRPs) in the peptidome of pickerel frog (Rana palustris) skin secretion is the product of transcriptional economy. Peptides 28 (2007) 1275-1281
    • (2007) Peptides , vol.28 , pp. 1275-1281
    • McCrudden, C.M.1
  • 18
    • 0033572814 scopus 로고    scopus 로고
    • Atlantic salmon (Salmo salar L.) skin contains a novel kininogen and another cysteine proteinase inhibitor
    • Ylönen A., et al. Atlantic salmon (Salmo salar L.) skin contains a novel kininogen and another cysteine proteinase inhibitor. Eur. J. Biochem. 266 (1999) 1066-1072
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1066-1072
    • Ylönen, A.1
  • 19
    • 0036268058 scopus 로고    scopus 로고
    • Purification and characterization of novel kininogens from spotted wolffish and Atlantic cod
    • Ylönen A., et al. Purification and characterization of novel kininogens from spotted wolffish and Atlantic cod. Eur. J. Biochem. 269 (2002) 2639-2646
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2639-2646
    • Ylönen, A.1
  • 21
    • 0023839733 scopus 로고
    • Localization of DNA sequences governing alternative mRNA production of rat kininogen genes
    • Kakizuka A., Kitamura N., and Nakanishi S. Localization of DNA sequences governing alternative mRNA production of rat kininogen genes. J. Biol. Chem. 263 (1988) 3884-3892
    • (1988) J. Biol. Chem. , vol.263 , pp. 3884-3892
    • Kakizuka, A.1    Kitamura, N.2    Nakanishi, S.3
  • 22
    • 0022555509 scopus 로고
    • Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases
    • Salvesen G., Parkes C., Abrahamson M., Grubb A., and Barrett A.J. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem. J. 234 (1986) 429-434
    • (1986) Biochem. J. , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 23
    • 0018995127 scopus 로고
    • Pharmacology of bradykinin and related kinins
    • Regoli D., and Barabe J. Pharmacology of bradykinin and related kinins. Pharmacol. Rev. 32 (1980) 1-46
    • (1980) Pharmacol. Rev. , vol.32 , pp. 1-46
    • Regoli, D.1    Barabe, J.2
  • 24
    • 0019212624 scopus 로고
    • Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin-mediated activation of factor XI1 (Hageman factor)
    • Sugo T., Ikari N., Kato H., Iwanaga S., and Fujii S. Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin-mediated activation of factor XI1 (Hageman factor). Biochemistry 19 (1980) 3215-3220
    • (1980) Biochemistry , vol.19 , pp. 3215-3220
    • Sugo, T.1    Ikari, N.2    Kato, H.3    Iwanaga, S.4    Fujii, S.5
  • 25
    • 0023257512 scopus 로고
    • Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI
    • Tait J., and Fujikawa K. Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. J. Biol. Chem. 262 (1987) 11651-11656
    • (1987) J. Biol. Chem. , vol.262 , pp. 11651-11656
    • Tait, J.1    Fujikawa, K.2
  • 26
    • 0029053039 scopus 로고
    • Kallikrein generates angiotensin II but not bradykinin in the plasma of the urodele, Amphiuma tridactylum
    • Conlon J.M., and Yano K. Kallikrein generates angiotensin II but not bradykinin in the plasma of the urodele, Amphiuma tridactylum. Comp. Biochem. Physiol. C 110 (1995) 305-311
    • (1995) Comp. Biochem. Physiol. C , vol.110 , pp. 305-311
    • Conlon, J.M.1    Yano, K.2
  • 27
    • 0032801764 scopus 로고    scopus 로고
    • Bradykinin and its receptors in nonmammalian vertebrates
    • Conlon J.M. Bradykinin and its receptors in nonmammalian vertebrates. Regul. Pept. 79 (1999) 71-81
    • (1999) Regul. Pept. , vol.79 , pp. 71-81
    • Conlon, J.M.1
  • 28
    • 0030689711 scopus 로고    scopus 로고
    • The natural history of amphibian skin secretions, their normal functioning and potential medical applications
    • Clarke B.T. The natural history of amphibian skin secretions, their normal functioning and potential medical applications. Biol. Rev. 72 (1997) 365-379
    • (1997) Biol. Rev. , vol.72 , pp. 365-379
    • Clarke, B.T.1
  • 29
    • 0022350512 scopus 로고
    • Genealogy of mammalian cysteine proteinase inhibitors: common evolutionary origin of stefins, cystatins and kininogens
    • Müller-Esterl W., et al. Genealogy of mammalian cysteine proteinase inhibitors: common evolutionary origin of stefins, cystatins and kininogens. FEBS Lett. 191 (1985) 221-226
    • (1985) FEBS Lett. , vol.191 , pp. 221-226
    • Müller-Esterl, W.1
  • 31
    • 0035477813 scopus 로고    scopus 로고
    • Exon structure conservation despite low sequence similarity: a relic of dramatic events in evolution?
    • Betts M.J., Guigó R., Agarwal P., and Russell R.B. Exon structure conservation despite low sequence similarity: a relic of dramatic events in evolution?. EMBO J. 20 (2001) 5354-5360
    • (2001) EMBO J. , vol.20 , pp. 5354-5360
    • Betts, M.J.1    Guigó, R.2    Agarwal, P.3    Russell, R.B.4
  • 32
    • 33947586113 scopus 로고    scopus 로고
    • Analysis of the exon-intron structures of fish, amphibian, bird and mammalian hatching enzyme genes, with special reference to the intron loss evolution of hatching enzyme genes in Teleostei
    • Kawaguchi M., et al. Analysis of the exon-intron structures of fish, amphibian, bird and mammalian hatching enzyme genes, with special reference to the intron loss evolution of hatching enzyme genes in Teleostei. Gene 392 (2007) 77-78
    • (2007) Gene , vol.392 , pp. 77-78
    • Kawaguchi, M.1
  • 34
    • 21244485401 scopus 로고    scopus 로고
    • 2+ exchanger (NCX) genes from genomic data identifies new gene duplications and a new family member in fish species
    • 2+ exchanger (NCX) genes from genomic data identifies new gene duplications and a new family member in fish species. Physiol. Genomics 21 (2005) 161-173
    • (2005) Physiol. Genomics , vol.21 , pp. 161-173
    • Marshall, C.R.1
  • 35
    • 33947575311 scopus 로고    scopus 로고
    • Origin of the genes for the isoforms of creatine kinase
    • Bertin M., et al. Origin of the genes for the isoforms of creatine kinase. Gene 392 (2007) 273-282
    • (2007) Gene , vol.392 , pp. 273-282
    • Bertin, M.1
  • 36
    • 34249785354 scopus 로고    scopus 로고
    • Evolution of the 12 kDa FK506-binding protein gene
    • Somarelli J.A., and Herrera R.J. Evolution of the 12 kDa FK506-binding protein gene. Biol. Cell 99 (2007) 311-321
    • (2007) Biol. Cell , vol.99 , pp. 311-321
    • Somarelli, J.A.1    Herrera, R.J.2
  • 37
    • 0033230110 scopus 로고    scopus 로고
    • Intron insertion as a phylogenetic character: the engrailed homeobox of Strepsiptera does not indicate affinity with Diptera
    • Rokas A., Kathirithamby J., and Holland P.W. Intron insertion as a phylogenetic character: the engrailed homeobox of Strepsiptera does not indicate affinity with Diptera. Insect Mol. Biol. 8 (1999) 527-530
    • (1999) Insect Mol. Biol. , vol.8 , pp. 527-530
    • Rokas, A.1    Kathirithamby, J.2    Holland, P.W.3
  • 38
    • 0033793019 scopus 로고    scopus 로고
    • Rare genomic changes as a tool for phylogenetics
    • Rokas A., and Holland P.W. Rare genomic changes as a tool for phylogenetics. Trends Ecol. Evol. 15 (2000) 454-459
    • (2000) Trends Ecol. Evol. , vol.15 , pp. 454-459
    • Rokas, A.1    Holland, P.W.2
  • 39
    • 0036132976 scopus 로고    scopus 로고
    • Dynamic insertion-deletion of introns in deuterostome EF-1 alpha genes
    • Wada H., et al. Dynamic insertion-deletion of introns in deuterostome EF-1 alpha genes. J. Mol. Evol. 54 (2002) 118-128
    • (2002) J. Mol. Evol. , vol.54 , pp. 118-128
    • Wada, H.1
  • 42
    • 0036889686 scopus 로고    scopus 로고
    • Orthology, paralogy and proposed classification for paralog subtypes
    • Sonnhammer E.L.L., and Koonin E.V. Orthology, paralogy and proposed classification for paralog subtypes. Trends Genet. 18 (2002) 619-620
    • (2002) Trends Genet. , vol.18 , pp. 619-620
    • Sonnhammer, E.L.L.1    Koonin, E.V.2
  • 43
    • 2542419881 scopus 로고    scopus 로고
    • Structure and expression of two kininogen genes in mice
    • Cardoso C.C., et al. Structure and expression of two kininogen genes in mice. Biol. Chem. 385 (2004) 295-301
    • (2004) Biol. Chem. , vol.385 , pp. 295-301
    • Cardoso, C.C.1
  • 44
    • 0031569840 scopus 로고    scopus 로고
    • Tetraodon fluviatilis, a new puffer fish model for genome studies
    • Crnogorac-Jurcevic T., Brown J.R., Lehrach H., and Schalkwyk L.C. Tetraodon fluviatilis, a new puffer fish model for genome studies. Genomics 41 (1997) 177-184
    • (1997) Genomics , vol.41 , pp. 177-184
    • Crnogorac-Jurcevic, T.1    Brown, J.R.2    Lehrach, H.3    Schalkwyk, L.C.4
  • 46
    • 0346155809 scopus 로고    scopus 로고
    • Pseudogenes: are they "junk" or functional DNA?
    • Balakirev E.S., and Ayala F.J. Pseudogenes: are they "junk" or functional DNA?. Annu. Rev. Genet. 37 (2003) 123-151
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 123-151
    • Balakirev, E.S.1    Ayala, F.J.2
  • 47
    • 0037795455 scopus 로고    scopus 로고
    • Large-scale comparison of intron positions in mammalian genes shows intron loss but no gain
    • Roy S.W., Fedorov A., and Gilbert W. Large-scale comparison of intron positions in mammalian genes shows intron loss but no gain. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7158-7162
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7158-7162
    • Roy, S.W.1    Fedorov, A.2    Gilbert, W.3
  • 48
    • 34547617526 scopus 로고    scopus 로고
    • The structure and function of cold shock proteins (Csps) in Archaea
    • Giaquinto L., et al. The structure and function of cold shock proteins (Csps) in Archaea. J. Bacteriol. 189 (2007) 5738-5748
    • (2007) J. Bacteriol. , vol.189 , pp. 5738-5748
    • Giaquinto, L.1
  • 49
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX 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 ClustalX Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24 (1997) 4876-4882
    • (1997) Nucleic 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
  • 50
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5 (2004) 150-163
    • (2004) Brief. Bioinform. , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 51
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey T.L., and Elkan C. Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol. 2 (1994) 28-36
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.