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Volumn 189, Issue 1, 1997, Pages

Correlation of the exon/intron organization to the secondary structures of the protease domain of mouse meprin α subunit

Author keywords

Astacin family; Meprin gene; Metalloendopeptidase

Indexed keywords

MEPRIN; PROTEIN SUBUNIT; PROTEINASE;

EID: 0342602071     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(96)00834-7     Document Type: Article
Times cited : (12)

References (42)
  • 3
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • Bode, W., Gomis-Rüth, F.X., Stöcker, W. (1993) Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett. 331, 134-140.
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stöcker, W.3
  • 4
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • Bond, J.S. and Beynon, R.J. (1995) The astacin family of metalloendopeptidases. Protein Sci. 4, 1247-1261.
    • (1995) Protein Sci. , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 5
    • 0021188625 scopus 로고
    • Mep-1 gene controlling a kidney metalloendopeptidase is linked to the major histocompatibility complex in mice
    • Bond, J.S., Beynon, R.J., Reckelhoff, J.F. and David, C.S. (1984) Mep-1 gene controlling a kidney metalloendopeptidase is linked to the major histocompatibility complex in mice. Proc. Natl. Acad. Sci. USA 81, 5542-5545.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5542-5545
    • Bond, J.S.1    Beynon, R.J.2    Reckelhoff, J.F.3    David, C.S.4
  • 6
    • 0028906545 scopus 로고
    • The structural genes, MEP1A and MEP1B, for the α and β subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively
    • Bond, J.S., Rojas, K., Overhauser, J., Zoghbi, H.Y. and Jiang, W. (1995) The structural genes, MEP1A and MEP1B, for the α and β subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively. Genomics 25, 300-303.
    • (1995) Genomics , vol.25 , pp. 300-303
    • Bond, J.S.1    Rojas, K.2    Overhauser, J.3    Zoghbi, H.Y.4    Jiang, W.5
  • 7
    • 0028223030 scopus 로고
    • Two domains of the tolloid protein contribute to its unusual genetic interaction with decapentaplegic
    • Childs, S.R. and O'Connor, M.B. (1994) Two domains of the tolloid protein contribute to its unusual genetic interaction with decapentaplegic. Dev. Biol. 162, 209-220.
    • (1994) Dev. Biol. , vol.162 , pp. 209-220
    • Childs, S.R.1    O'Connor, M.B.2
  • 8
    • 0026801333 scopus 로고
    • Molecular cloning of the α subunit of rat endopeptidase-24.18 (endopeptidase-2) and co-localization with endopeptidase-24.11 in rat kidney by in situ hybridization
    • Corbell, D., Gaudoux, F., Wainwright, S., Ingram, J., Kenny, A.J., Boileau, G. and Crine, P. (1992) Molecular cloning of the α subunit of rat endopeptidase-24.18 (endopeptidase-2) and co-localization with endopeptidase-24.11 in rat kidney by in situ hybridization. FEBS Lett. 309, 203-208.
    • (1992) FEBS Lett. , vol.309 , pp. 203-208
    • Corbell, D.1    Gaudoux, F.2    Wainwright, S.3    Ingram, J.4    Kenny, A.J.5    Boileau, G.6    Crine, P.7
  • 9
    • 0030032714 scopus 로고    scopus 로고
    • A novel meprin β′ mRNA in mouse embryonal and human colon carcinoma cells
    • 1996
    • Dietrich, J.M., Jiang, W. and Bond, J.S. (1996) (1996) A novel meprin β′ mRNA in mouse embryonal and human colon carcinoma cells. J. Biol. Chem. 271, 2271-2278.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2271-2278
    • Dietrich, J.M.1    Jiang, W.2    Bond, J.S.3
  • 10
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle, R.F. (1995) The multiplicity of domains in proteins. Annu. Rev. Biochem. 64, 287-314.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 12
    • 0027360581 scopus 로고
    • Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS-1 cells
    • Dumermuth, E., Eldering, J.A., Grünberg, H., Jiang, W. and Sterchi, E.E. (1993) Cloning of the PABA peptide hydrolase alpha subunit (PPHα) from human small intestine and its expression in COS-1 cells. FEBS Lett. 335, 367-375.
    • (1993) FEBS Lett. , vol.335 , pp. 367-375
    • Dumermuth, E.1    Eldering, J.A.2    Grünberg, H.3    Jiang, W.4    Sterchi, E.E.5
  • 13
    • 0028295172 scopus 로고
    • Mutational analysis of the Drosophila tolloid gene, a human BMP-1 homolog
    • Finelli, A.L., Bossie, C.A., Xie, T. and Padgett, R.W. (1994) Mutational analysis of the Drosophila tolloid gene, a human BMP-1 homolog. Development 120, 861-870.
    • (1994) Development , vol.120 , pp. 861-870
    • Finelli, A.L.1    Bossie, C.A.2    Xie, T.3    Padgett, R.W.4
  • 17
    • 0027771868 scopus 로고
    • On the ancient nature of introns
    • Gilbert, W. and Glynias, M. (1993) On the ancient nature of introns. Gene 135, 137-144.
    • (1993) Gene , vol.135 , pp. 137-144
    • Gilbert, W.1    Glynias, M.2
  • 19
    • 0026451216 scopus 로고
    • Families of metalloendopeptidases and their relationships
    • Jiang, W. and Bond, J.S. (1992) Families of metalloendopeptidases and their relationships. FEBS Lett. 312, 110-114.
    • (1992) FEBS Lett. , vol.312 , pp. 110-114
    • Jiang, W.1    Bond, J.S.2
  • 20
    • 84990703594 scopus 로고    scopus 로고
    • Astacin family of metalloendopeptidases
    • Hooper, N.M. (Ed.), Taylor and Francis, London
    • Jiang, W. and Bond, J.S. (1996) Astacin family of metalloendopeptidases. In: Hooper, N.M. (Ed.), Zinc Metalloproteases in Health and Disease. Taylor and Francis, London.
    • (1996) Zinc Metalloproteases in Health and Disease
    • Jiang, W.1    Bond, J.S.2
  • 21
    • 0026788142 scopus 로고
    • The α subunit of meprin A: Molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the α and β subunits
    • Jiang, W., Gorbea, C.M., Flannery, A.V., Beynon, R.J., Grant, G.A. and Bond, J.S. (1992) The α subunit of meprin A: molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the α and β subunits. J. Biol. Chem. 267, 9185-9193.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9185-9193
    • Jiang, W.1    Gorbea, C.M.2    Flannery, A.V.3    Beynon, R.J.4    Grant, G.A.5    Bond, J.S.6
  • 22
    • 0027176126 scopus 로고
    • Tissue-specific expression and chromosomal localization of the α subunit of mouse meprin A
    • Jiang, W., Sadler, P.M., Jenkins, N.A., Gilbert, D.J., Copeland, N.G. and Bond, J.S. (1993) Tissue-specific expression and chromosomal localization of the α subunit of mouse meprin A. J. Biol. Chem. 268, 10380-10385.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10380-10385
    • Jiang, W.1    Sadler, P.M.2    Jenkins, N.A.3    Gilbert, D.J.4    Copeland, N.G.5    Bond, J.S.6
  • 24
    • 0026716396 scopus 로고
    • Cloning a rat meprin cDNA reveals the enzyme is a heterodimer
    • Johnson, G.D. and Hersh, L.B. (1992) Cloning a rat meprin cDNA reveals the enzyme is a heterodimer. J. Biol. Chem. 267, 13505-13512.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13505-13512
    • Johnson, G.D.1    Hersh, L.B.2
  • 26
    • 0023646322 scopus 로고
    • Intron-dependent evolution: Preferred types of exons and introns
    • Patthy, L. (1987) Intron-dependent evolution: preferred types of exons and introns. FEBS Lett. 214, 1-7.
    • (1987) FEBS Lett. , vol.214 , pp. 1-7
    • Patthy, L.1
  • 28
    • 0025986820 scopus 로고
    • The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1
    • Shimell, M.J., Ferguson, E.L., Childs, S.R. and O'Connor, M.B. (1991) The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1. Cell 67, 461-481.
    • (1991) Cell , vol.67 , pp. 461-481
    • Shimell, M.J.1    Ferguson, E.L.2    Childs, S.R.3    O'Connor, M.B.4
  • 29
    • 0028034161 scopus 로고
    • Distribution of, and a putative role for, the cell surface neutral metalloendopeptidases during mammalian craniofacial development
    • Spencer-Dene, B., Thorogood, P., Nair, S., Kenny, J., Harris, M. and Henderson, B. (1994) Distribution of, and a putative role for, the cell surface neutral metalloendopeptidases during mammalian craniofacial development. Development 120, 3213-3226.
    • (1994) Development , vol.120 , pp. 3213-3226
    • Spencer-Dene, B.1    Thorogood, P.2    Nair, S.3    Kenny, J.4    Harris, M.5    Henderson, B.6
  • 30
    • 0028043139 scopus 로고
    • Testing the exon theory of genes: The evidence from protein structure
    • Stoltzfus, A., Spencer, D.F., Zuker, M., Logsdon, J.M. and Doolittle, W.F. (1994) Testing the exon theory of genes: the evidence from protein structure. Science 265, 202-207.
    • (1994) Science , vol.265 , pp. 202-207
    • Stoltzfus, A.1    Spencer, D.F.2    Zuker, M.3    Logsdon, J.M.4    Doolittle, W.F.5
  • 31
    • 0027287308 scopus 로고
    • Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases
    • Stöcker, W., Gomis-Rüth, F.-X., Bode, W. and Zwilling, R. (1993) Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases. Eur. J. Biochem. 214, 215-231.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 215-231
    • Stöcker, W.1    Gomis-Rüth, F.-X.2    Bode, W.3    Zwilling, R.4
  • 32
    • 0028969678 scopus 로고
    • The metzincins- Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stöcker, W., Grams, F., Baumann, R., Reinemer, P., Gomis-Rüth, F.-X., McKay, D.B. and Bode, W. (1995) The metzincins- Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stöcker, W.1    Grams, F.2    Baumann, R.3    Reinemer, P.4    Gomis-Rüth, F.-X.5    McKay, D.B.6    Bode, W.7
  • 33
    • 0029096831 scopus 로고
    • Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene
    • Takahara, K., Lee, S., Wood, S. and Breenspan, D.S. (1995) Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene. Genomics 29, 9-15.
    • (1995) Genomics , vol.29 , pp. 9-15
    • Takahara, K.1    Lee, S.2    Wood, S.3    Breenspan, D.S.4
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 0029051493 scopus 로고
    • Molecular cloning and sequence analysis of flavastacin: An O-glycosylated prokaryotic zinc metalloendopeptidase
    • Tarentino, A.L., Quinones, G., Grimwood, B.G., Hauer, C.R., Plummer Jr., T.H. (1995) Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase. Arch. Biochem. Biophys. 319, 281-285.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 281-285
    • Tarentino, A.L.1    Quinones, G.2    Grimwood, B.G.3    Hauer, C.R.4    Plummer T.H., Jr.5
  • 37
    • 0028288181 scopus 로고
    • Intron positions in actin genes seem unrelated to the secondary structure of the protein
    • Weber, K. and Kabsch, W. (1994) Intron positions in actin genes seem unrelated to the secondary structure of the protein. EMBO J. 13, 1280-1286.
    • (1994) EMBO J. , vol.13 , pp. 1280-1286
    • Weber, K.1    Kabsch, W.2
  • 40
    • 0028675675 scopus 로고
    • Purification of meprin from human kidney and its role in parathyroid hormone degradation
    • Yamaguchi, T., Fukase, M., Sugimoto, T., Kido, H. and Chihara, K. (1994) Purification of meprin from human kidney and its role in parathyroid hormone degradation. Biol. Chem. Hoppe-Seyler 375, 821-824.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 821-824
    • Yamaguchi, T.1    Fukase, M.2    Sugimoto, T.3    Kido, H.4    Chihara, K.5
  • 41
    • 0026697681 scopus 로고
    • Ioslation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development
    • Yasumasu, S., Yamada, K., Akasaka, K., Mitsunaga, K., Iuchi, I., Shimada, H. and Yamagami, K. (1992) Ioslation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development. Dev. Biol. 153, 250-258.
    • (1992) Dev. Biol. , vol.153 , pp. 250-258
    • Yasumasu, S.1    Yamada, K.2    Akasaka, K.3    Mitsunaga, K.4    Iuchi, I.5    Shimada, H.6    Yamagami, K.7
  • 42
    • 0028025092 scopus 로고
    • cDNA and the genes of HCE and LCE, two constituents of the medaka hatching enzyme
    • Yasumasu, S., Iuchi, I. and Yamagami, K. (1994) cDNA and the genes of HCE and LCE, two constituents of the medaka hatching enzyme. Dev. Growth Differ. 36, 241-250.
    • (1994) Dev. Growth Differ. , vol.36 , pp. 241-250
    • Yasumasu, S.1    Iuchi, I.2    Yamagami, K.3


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