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Volumn 64, Issue 2, 1999, Pages 211-221

XCE, a new member of the endothelin-converting enzyme and neutral endopeptidase family, is preferentially expressed in the CNS

Author keywords

Endothelin converting enzyme; Medulla; Neutral endopeptidase; Spinal cord; Zinc metallopeptidase

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE METALLOENDOPEPTIDASE; MEMBRANE METALLOENDOPEPTIDASE XCE; UNCLASSIFIED DRUG;

EID: 0033524706     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(98)00321-0     Document Type: Article
Times cited : (83)

References (34)
  • 1
    • 0031031038 scopus 로고    scopus 로고
    • Expression of endothelin-converting enzyme in both neuroblastoma and glial cell lines and its localization in rat hippocampus
    • K. Barnes, B.J. Walkden, T.C. Wilkinson, A.J. Turner, Expression of endothelin-converting enzyme in both neuroblastoma and glial cell lines and its localization in rat hippocampus, J. Neurochem. 68 (1997) 570-577.
    • (1997) J. Neurochem. , vol.68 , pp. 570-577
    • Barnes, K.1    Walkden, B.J.2    Wilkinson, T.C.3    Turner, A.J.4
  • 2
    • 0025961397 scopus 로고
    • Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4.24.11)
    • A. Beaumont, H. Le Moual, G. Boileau, P. Crine, B.P. Roques, Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4.24.11), J. Biol. Chem. 266 (1991) 214-220.
    • (1991) J. Biol. Chem. , vol.266 , pp. 214-220
    • Beaumont, A.1    Le Moual, H.2    Boileau, G.3    Crine, P.4    Roques, B.P.5
  • 3
    • 0029099749 scopus 로고
    • Metabolism of galanin and galanin (1-16) in isolated cerebrospinal fluid and spinal cord membranes from rat
    • K. Bedecs, U. Langel, T. Bartfai, Metabolism of galanin and galanin (1-16) in isolated cerebrospinal fluid and spinal cord membranes from rat, Neuropeptides 29 (1995) 137-143.
    • (1995) Neuropeptides , vol.29 , pp. 137-143
    • Bedecs, K.1    Langel, U.2    Bartfai, T.3
  • 4
    • 0026609207 scopus 로고
    • Murine common acute lymphoblastic leukemia antigen (CD10 neutral endopeptidase 24.11). Molecular characterization, chromosomal localization, and modeling of the active site
    • C.Y. Chen, G. Salles, M.F. Seldin, A.E. Kister, E.L. Reinherz, M.A. Shipp, Murine common acute lymphoblastic leukemia antigen (CD10 neutral endopeptidase 24.11). Molecular characterization, chromosomal localization, and modeling of the active site, J. Immunol. 148 (1992) 2817-2825.
    • (1992) J. Immunol. , vol.148 , pp. 2817-2825
    • Chen, C.Y.1    Salles, G.2    Seldin, M.F.3    Kister, A.E.4    Reinherz, E.L.5    Shipp, M.A.6
  • 6
    • 0024284245 scopus 로고
    • Exploration of the catalytic site of endopeptidase 24.11 by site-directed mutagenesis. Histidine residues 583 and 587 are essential for catalysis
    • A. Devault, V. Sales, C. Nault, A. Beaumont, B.P. Roques, P. Crine, G. Boileau, Exploration of the catalytic site of endopeptidase 24.11 by site-directed mutagenesis. Histidine residues 583 and 587 are essential for catalysis, FEBS Lett. 231 (1988) 54-58.
    • (1988) FEBS Lett. , vol.231 , pp. 54-58
    • Devault, A.1    Sales, V.2    Nault, C.3    Beaumont, A.4    Roques, B.P.5    Crine, P.6    Boileau, G.7
  • 7
    • 0027456271 scopus 로고
    • Kinetic evidence that His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state
    • N. Dion, H. Le Moual, P. Crine, G. Boileau, Kinetic evidence that His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state, FEBS Lett. 318 (1993) 301-304.
    • (1993) FEBS Lett. , vol.318 , pp. 301-304
    • Dion, N.1    Le Moual, H.2    Crine, P.3    Boileau, G.4
  • 8
    • 0030586965 scopus 로고    scopus 로고
    • cDNA cloning of the murine Pex gene implicated in X-linked hypophosphatemia and evidence for expression in bone
    • L. Du, M. Desbarats, J. Viel, F.H. Glorieux, C. Cawthorn, B. Ecarot, cDNA cloning of the murine Pex gene implicated in X-linked hypophosphatemia and evidence for expression in bone, Genomics 36 (1996) 22-28.
    • (1996) Genomics , vol.36 , pp. 22-28
    • Du, L.1    Desbarats, M.2    Viel, J.3    Glorieux, F.H.4    Cawthorn, C.5    Ecarot, B.6
  • 9
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum
    • N. Emoto, M. Yanagisawa, Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum, J. Biol. Chem. 270 (1995) 15262-15268.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 10
    • 70350503363 scopus 로고    scopus 로고
    • The basal ganglia
    • L.W. Swanson, A. Björklund, T. Hökfelt (Eds.), Integrated Systems of the CNS, Part III: Cerebellum, Basal Ganglia, Olfactory System. Elsevier, Amsterdam
    • Gerfen, C.R., Wilson, C.J., The basal ganglia, in: L.W. Swanson, A. Björklund, T. Hökfelt (Eds.), Integrated Systems of the CNS, Part III: Cerebellum, Basal Ganglia, Olfactory System. Handbook of Chemical Neuroanatomy, Vol. 12, Elsevier, Amsterdam, 1996, pp. 371-468.
    • (1996) Handbook of Chemical Neuroanatomy , vol.12 , pp. 371-468
    • Gerfen, C.R.1    Wilson, C.J.2
  • 11
    • 0030700341 scopus 로고    scopus 로고
    • Novel activity of endothelin-converting enzyme: Hydrolysis of bradykinin
    • M.V. Hoang, A.J. Turner, Novel activity of endothelin-converting enzyme: hydrolysis of bradykinin, Biochem. J. 327 (1997) 23-26.
    • (1997) Biochem. J. , vol.327 , pp. 23-26
    • Hoang, M.V.1    Turner, A.J.2
  • 12
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • N.M. Hooper, Families of zinc metalloproteases, FEBS Lett. 354 (1994) 1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 13
    • 0028809746 scopus 로고
    • Striatal interneurones: Chemical, physiological and morphological characterization
    • Y. Kawaguchi, C.J. Wilson, S.J. Augood, P.C. Emson, Striatal interneurones: chemical, physiological and morphological characterization, Trends Neurosci. 18 (1995) 527-535.
    • (1995) Trends Neurosci. , vol.18 , pp. 527-535
    • Kawaguchi, Y.1    Wilson, C.J.2    Augood, S.J.3    Emson, P.C.4
  • 14
    • 0014949207 scopus 로고
    • U.K. Laemmli, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0030820550 scopus 로고    scopus 로고
    • Molecular basis of Kell blood group phenotypes
    • S. Lee, Molecular basis of Kell blood group phenotypes, Vox Sang. 73 (1997) 1-11.
    • (1997) Vox Sang. , vol.73 , pp. 1-11
    • Lee, S.1
  • 16
    • 0025779323 scopus 로고
    • Molecular cloning and primary structure of Kell blood group protein
    • S. Lee, E.D. Zambas, W.L. Marsh, C.M. Redman, Molecular cloning and primary structure of Kell blood group protein, Proc. Natl. Acad. Sci. USA 88 (1991) 6353-6357.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6353-6357
    • Lee, S.1    Zambas, E.D.2    Marsh, W.L.3    Redman, C.M.4
  • 18
    • 0028883725 scopus 로고
    • Comparison of the structure and expression of the human and rat neprilysin (endopeptidase 24.11)-encoding genes
    • C. Li, G. Chen, N.P. Gerard, C. Gerard, C.R. Bozic, L.B. Hersh, Comparison of the structure and expression of the human and rat neprilysin (endopeptidase 24.11)-encoding genes, Gene 164 (1995) 363-366.
    • (1995) Gene , vol.164 , pp. 363-366
    • Li, C.1    Chen, G.2    Gerard, N.P.3    Gerard, C.4    Bozic, C.R.5    Hersh, L.B.6
  • 19
    • 0023868637 scopus 로고
    • Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)
    • B. Malfroy, W.J. Kuang, P.H. Seeburg, A.J. Mason, P.R. Schofield, Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase), FEBS Lett. 229 (1988) 206-210.
    • (1988) FEBS Lett. , vol.229 , pp. 206-210
    • Malfroy, B.1    Kuang, W.J.2    Seeburg, P.H.3    Mason, A.J.4    Schofield, P.R.5
  • 20
    • 0030793366 scopus 로고    scopus 로고
    • Evidence of alternative promoters directing isoform-specific expression of human endothelin-converting enzyme-1 mRNA in cultured endothelial cells
    • H.D. Orzechowski, C.M. Richter, H. Funke-Kaiser, B. Kroger, M. Schmidt, S. Menzel, H. Bohnemeier, M. Paul, Evidence of alternative promoters directing isoform-specific expression of human endothelin-converting enzyme-1 mRNA in cultured endothelial cells, J. Mol. Med. 75 (1997) 512-521.
    • (1997) J. Mol. Med. , vol.75 , pp. 512-521
    • Orzechowski, H.D.1    Richter, C.M.2    Funke-Kaiser, H.3    Kroger, B.4    Schmidt, M.5    Menzel, S.6    Bohnemeier, H.7    Paul, M.8
  • 21
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: Similarities to the angiotensin converting enzyme secretase
    • S. Parvathy, I. Hussain, E.H. Karran, A.J. Turner, N.M. Hooper, Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase, Biochemistry 37 (1998) 1680-1685.
    • (1998) Biochemistry , vol.37 , pp. 1680-1685
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 24
    • 0027475050 scopus 로고
    • Neutral endopeptidase 24.11: Structure, inhibition, and experimental and clinical pharmacology
    • B.P. Roques, F. Noble, V. Dauge, M.C. Fournie-Zaluski, A. Beaumont, Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology, Pharmacol. Rev. 45 (1993) 87-146.
    • (1993) Pharmacol. Rev. , vol.45 , pp. 87-146
    • Roques, B.P.1    Noble, F.2    Dauge, V.3    Fournie-Zaluski, M.C.4    Beaumont, A.5
  • 27
    • 0029149716 scopus 로고
    • Identification and characterization of two isoforms of an endothelin-converting enzyme-1
    • K. Shimada, M. Takahashi, M. Ikeda, K. Tanzawa, Identification and characterization of two isoforms of an endothelin-converting enzyme-1, FEBS Lett. 371 (1995) 140-144.
    • (1995) FEBS Lett. , vol.371 , pp. 140-144
    • Shimada, K.1    Takahashi, M.2    Ikeda, M.3    Tanzawa, K.4
  • 28
    • 0028261084 scopus 로고
    • Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells
    • K. Shimada, M. Takahashi, K. Tanzawa, Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells, J. Biol. Chem. 269 (1994) 18275-18278.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18275-18278
    • Shimada, K.1    Takahashi, M.2    Tanzawa, K.3
  • 29
    • 0029997473 scopus 로고    scopus 로고
    • Rat endothelin-converting enzyme-1 forms a dimer through Cys412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11
    • K. Shimada, M. Takahashi, A.J. Turner, K. Tanzawa, Rat endothelin-converting enzyme-1 forms a dimer through Cys412 with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11, Biochem. J. 315 (1996) 863-867.
    • (1996) Biochem. J. , vol.315 , pp. 863-867
    • Shimada, K.1    Takahashi, M.2    Turner, A.J.3    Tanzawa, K.4
  • 30
    • 0029160578 scopus 로고
    • A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets
    • The HYP Consortium, A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets, Nat. Genet. 11 (1995) 130-136.
    • (1995) Nat. Genet. , vol.11 , pp. 130-136
  • 32
    • 0030899822 scopus 로고    scopus 로고
    • Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
    • A.J. Turner, K. Tanzawa, Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX, FASEB J. 11 (1997) 355-364.
    • (1997) FASEB J. , vol.11 , pp. 355-364
    • Turner, A.J.1    Tanzawa, K.2
  • 33
    • 0029585975 scopus 로고
    • Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)
    • O. Valdenaire, E. Rohrbacher, M.G. Mattel, Organization of the gene encoding the human endothelin-converting enzyme (ECE-1), J. Biol. Chem. 270 (1995) 29794-29798.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29794-29798
    • Valdenaire, O.1    Rohrbacher, E.2    Mattel, M.G.3
  • 34
    • 0027992642 scopus 로고
    • ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1
    • D. Xu, N. Emoto, A. Giaid, C. Slaughter, S. Kaw, D. deWit, M. Yanagisawa, ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1, Cell 78 (1994) 473-485.
    • (1994) Cell , vol.78 , pp. 473-485
    • Xu, D.1    Emoto, N.2    Giaid, A.3    Slaughter, C.4    Kaw, S.5    Dewit, D.6    Yanagisawa, M.7


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