메뉴 건너뛰기




Volumn 68, Issue 3, 1997, Pages 889-897

Cloning of the human puromycin-sensitive aminopeptidase and evidence for expression in neurons

Author keywords

Amino peptidase; Apoptosis; Enkephalinase; Neurons; Puromycin

Indexed keywords

AMINOPEPTIDASE; PUROMYCIN;

EID: 0031028814     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.68030889.x     Document Type: Article
Times cited : (60)

References (36)
  • 1
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C. and De Jong J. P. (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18, 6069-6074.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, J.P.2
  • 2
    • 0023873980 scopus 로고
    • Angiotensin metabolism by cerebral microvascular aminopeptidase A
    • Bausback H. H., Churchill L., and Ward P. E. (1988) Angiotensin metabolism by cerebral microvascular aminopeptidase A. Biochem. Pharmacol. 37, 155-160.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 155-160
    • Bausback, H.H.1    Churchill, L.2    Ward, P.E.3
  • 3
    • 0024501822 scopus 로고
    • Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae
    • Chang Y. H. and Smith J. A. (1989) Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae. J. Biol. Chem. 264, 6979-6983.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6979-6983
    • Chang, Y.H.1    Smith, J.A.2
  • 4
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization
    • Constam D. B., Tobler A. R., Rensing E. A., Kemler I., Hersh L. B., and Fontana A. (1995) Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization. J. Biol. Chem. 270, 26931-26939.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26931-26939
    • Constam, D.B.1    Tobler, A.R.2    Rensing, E.A.3    Kemler, I.4    Hersh, L.B.5    Fontana, A.6
  • 5
    • 0027743341 scopus 로고
    • Puromycin-elicited c-myc mRNA superinduction precedes apoptosis in HL-60 leukaemic cells
    • Davidoff A. N. and Mendelow B. V. (1993) Puromycin-elicited c-myc mRNA superinduction precedes apoptosis in HL-60 leukaemic cells. Anticancer Res. 13, 2257-2260.
    • (1993) Anticancer Res. , vol.13 , pp. 2257-2260
    • Davidoff, A.N.1    Mendelow, B.V.2
  • 6
    • 0020662674 scopus 로고
    • Participation of both 'enkephalinase' and aminopeptidase activities in the metabolism of endogenous enkephalins
    • De La Baume S., Yi C. C., Schwartz J. C., Chaillet P., Marcais C. H., and Costentin J. (1983) Participation of both 'enkephalinase' and aminopeptidase activities in the metabolism of endogenous enkephalins. Neuroscience 8, 143-151.
    • (1983) Neuroscience , vol.8 , pp. 143-151
    • De La Baume, S.1    Yi, C.C.2    Schwartz, J.C.3    Chaillet, P.4    Marcais, C.H.5    Costentin, J.6
  • 7
    • 0025057536 scopus 로고
    • Comparison of the soluble and membrane-bound forms of the puromycin-sensitive enkephalin-degrading aminopeptidases from rat
    • Dyer S. H., Slaughter C. A., Orth K., Moomaw C. R., and Hersh L. B. (1990) Comparison of the soluble and membrane-bound forms of the puromycin-sensitive enkephalin-degrading aminopeptidases from rat. J. Neurochem. 54, 547-554.
    • (1990) J. Neurochem. , vol.54 , pp. 547-554
    • Dyer, S.H.1    Slaughter, C.A.2    Orth, K.3    Moomaw, C.R.4    Hersh, L.B.5
  • 8
    • 0021795178 scopus 로고
    • A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
    • Gallione C. J. and Rose J. K. (1985) A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. J. Virol. 54, 374-382.
    • (1985) J. Virol. , vol.54 , pp. 374-382
    • Gallione, C.J.1    Rose, J.K.2
  • 9
    • 0022257123 scopus 로고
    • Identification of aminopeptidase M as an enkephalin-inactivating enzyme in rat cerebral membranes
    • Gros C., Giros B., and Schwartz J. C. (1985) Identification of aminopeptidase M as an enkephalin-inactivating enzyme in rat cerebral membranes. Biochemistry 24, 2179-2185.
    • (1985) Biochemistry , vol.24 , pp. 2179-2185
    • Gros, C.1    Giros, B.2    Schwartz, J.C.3
  • 10
    • 0026670801 scopus 로고
    • Rapid, reliable ligation-independent cloning of PCR products using modified plasmid vectors
    • Haun R. S., Serventi I. M., and Moss J. (1992) Rapid, reliable ligation-independent cloning of PCR products using modified plasmid vectors. Biotechniques 13, 515-518.
    • (1992) Biotechniques , vol.13 , pp. 515-518
    • Haun, R.S.1    Serventi, I.M.2    Moss, J.3
  • 11
    • 0025784806 scopus 로고
    • Temporal and spatial patterns of transin/stromelysin RNA expression following toxic injury in rat liver
    • Herbst H., Heinrichs O., Schuppan D., Milani S., and Stein H. (1991) Temporal and spatial patterns of transin/stromelysin RNA expression following toxic injury in rat liver. Virchows Arch. [B] 60, 295-300.
    • (1991) Virchows Arch. [B] , vol.60 , pp. 295-300
    • Herbst, H.1    Heinrichs, O.2    Schuppan, D.3    Milani, S.4    Stein, H.5
  • 13
    • 0021849522 scopus 로고
    • Characterization of membrane-bound aminopeptidases from rat brain: Identification of the enkephalin-degrading aminopeptidase
    • Hersh L. B. (1985) Characterization of membrane-bound aminopeptidases from rat brain: identification of the enkephalin-degrading aminopeptidase. J. Neurochem. 44, 1427-1435.
    • (1985) J. Neurochem. , vol.44 , pp. 1427-1435
    • Hersh, L.B.1
  • 14
    • 0023181886 scopus 로고
    • Immunohistochemical localization of aminopeptidase M in rat brain and periphery: Relationship of enzyme localization and enkephalin metabolism
    • Hersh L. B., Aboukhair N., and Watson S. (1987) Immunohistochemical localization of aminopeptidase M in rat brain and periphery: relationship of enzyme localization and enkephalin metabolism. Peptides 8, 523-532.
    • (1987) Peptides , vol.8 , pp. 523-532
    • Hersh, L.B.1    Aboukhair, N.2    Watson, S.3
  • 15
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N. M. (1994) Families of zinc metalloproteases. FEBS Lett. 354, 1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 16
    • 0020558176 scopus 로고
    • Purification and characterization of an enkephalin aminopeptidase from rat brain membranes
    • Hui K. S., Wang Y. J., and Lajtha A. (1983) Purification and characterization of an enkephalin aminopeptidase from rat brain membranes. Biochemistry 22, 1062-1067.
    • (1983) Biochemistry , vol.22 , pp. 1062-1067
    • Hui, K.S.1    Wang, Y.J.2    Lajtha, A.3
  • 17
    • 0023803422 scopus 로고
    • Major rat brain membrane-associated and cytosolic enkephalin-degrading aminopeptidases: Comparison studies
    • Hui K. S., Hui M. P., and Lajtha A. (1988) Major rat brain membrane-associated and cytosolic enkephalin-degrading aminopeptidases: comparison studies. J. Neurosci. Res. 20, 231-240.
    • (1988) J. Neurosci. Res. , vol.20 , pp. 231-240
    • Hui, K.S.1    Hui, M.P.2    Lajtha, A.3
  • 18
    • 0025543732 scopus 로고
    • Cellular localization of puromycin-sensitive aminopeptidase isozymes
    • Hui K. S., Hui M., Lajtha A., Saito M., and Saito M. (1990) Cellular localization of puromycin-sensitive aminopeptidase isozymes. Neurochem. Res. 15, 1147-1151.
    • (1990) Neurochem. Res. , vol.15 , pp. 1147-1151
    • Hui, K.S.1    Hui, M.2    Lajtha, A.3    Saito, M.4    Saito, M.5
  • 19
    • 0027318680 scopus 로고
    • Two cytosolic puromycin-sensitive aminopeptidase isozymes in chicken brain: Molecular homology to brain-specific 14-3-3 protein
    • Hui K. S., Saito M., Hui M., Saito M., Lajtha A., Yamamoto K., and Osawa T. (1993) Two cytosolic puromycin-sensitive aminopeptidase isozymes in chicken brain: molecular homology to brain-specific 14-3-3 protein. Neurochem. Int. 22, 445-453.
    • (1993) Neurochem. Int. , vol.22 , pp. 445-453
    • Hui, K.S.1    Saito, M.2    Hui, M.3    Saito, M.4    Lajtha, A.5    Yamamoto, K.6    Osawa, T.7
  • 20
    • 0027410350 scopus 로고
    • A new soluble brain-specific protein: Identification and partial purification
    • Hui M. P., Lajtha A., and Hui K. S. (1993) A new soluble brain-specific protein: identification and partial purification. Brain Res. 606, 36-43.
    • (1993) Brain Res. , vol.606 , pp. 36-43
    • Hui, M.P.1    Lajtha, A.2    Hui, K.S.3
  • 21
    • 0015973588 scopus 로고
    • The purification and specificity of a neutral endopeptidase from rabbit kidney brush border
    • Kerr M. A. and Kenny A. J. (1974) The purification and specificity of a neutral endopeptidase from rabbit kidney brush border. Biochem. J. 137, 477-488.
    • (1974) Biochem. J. , vol.137 , pp. 477-488
    • Kerr, M.A.1    Kenny, A.J.2
  • 22
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak M. (1991) Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266, 19867-19870.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 23
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis T. E. (1986) Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J. 5, 931-941.
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 24
    • 0018073489 scopus 로고
    • High-affinity enkephalin-degrading peptidase in brain is increased after morphine
    • Malfroy B., Swerts J. P., Guyon A., Roques B. P., and Schwartz J. C. (1978) High-affinity enkephalin-degrading peptidase in brain is increased after morphine. Nature 276, 523-526.
    • (1978) Nature , vol.276 , pp. 523-526
    • Malfroy, B.1    Swerts, J.P.2    Guyon, A.3    Roques, B.P.4    Schwartz, J.C.5
  • 25
    • 0022006475 scopus 로고
    • The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N
    • Matsas R., Stephenson S. L., Hryszko J., Kenny A. J., and Turner A. J. (1985) The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N. Biochem. J. 231, 445-449.
    • (1985) Biochem. J. , vol.231 , pp. 445-449
    • Matsas, R.1    Stephenson, S.L.2    Hryszko, J.3    Kenny, A.J.4    Turner, A.J.5
  • 26
    • 0022364574 scopus 로고
    • Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain
    • McDermott J. R., Mantle D., Lauffart B., and Kidd A. M. (1985) Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain. J. Neurochem. 45, 752-759.
    • (1985) J. Neurochem. , vol.45 , pp. 752-759
    • McDermott, J.R.1    Mantle, D.2    Lauffart, B.3    Kidd, A.M.4
  • 27
    • 0022930828 scopus 로고
    • Inactivation and metabolism of neuropeptides
    • McKelvy J. F. and Blumberg S. (1986) Inactivation and metabolism of neuropeptides. Annu. Rev. Neurosci. 9, 415-434.
    • (1986) Annu. Rev. Neurosci. , vol.9 , pp. 415-434
    • McKelvy, J.F.1    Blumberg, S.2
  • 28
    • 0023743331 scopus 로고
    • Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases
    • McLellan S., Dyer S. H., Rodriguez G., and Hersh L. B. (1988) Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases. J. Neurochem. 51, 1552-1559.
    • (1988) J. Neurochem. , vol.51 , pp. 1552-1559
    • McLellan, S.1    Dyer, S.H.2    Rodriguez, G.3    Hersh, L.B.4
  • 30
    • 0018772357 scopus 로고
    • Isolation and characterization of an enkephalin-degrading aminopeptidase from rat brain
    • Schnebli H. P., Phillipps M. A., and Barclay R. K. (1979) Isolation and characterization of an enkephalin-degrading aminopeptidase from rat brain. Biochim. Biophys. Acta 569, 89-98.
    • (1979) Biochim. Biophys. Acta , vol.569 , pp. 89-98
    • Schnebli, H.P.1    Phillipps, M.A.2    Barclay, R.K.3
  • 31
    • 0021883344 scopus 로고
    • Use of freeze-dried paraffin-embedded sections for immunohistologic staining with monoclonal antibodies
    • Stein H., Gatter K., Asbahr H., and Mason D. Y. (1985) Use of freeze-dried paraffin-embedded sections for immunohistologic staining with monoclonal antibodies. Lab. Invest. 52, 676-683.
    • (1985) Lab. Invest. , vol.52 , pp. 676-683
    • Stein, H.1    Gatter, K.2    Asbahr, H.3    Mason, D.Y.4
  • 32
    • 0027208935 scopus 로고
    • Aminopeptidases: Towards a mechanism of action
    • Taylor A. (1993a) Aminopeptidases: towards a mechanism of action. Trends Biochem. Sci. 18, 167-171.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-171
    • Taylor, A.1
  • 33
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • Taylor A. (1993b) Aminopeptidases: structure and function. FASEB J. 7, 290-298.
    • (1993) FASEB J. , vol.7 , pp. 290-298
    • Taylor, A.1
  • 34
    • 1842283624 scopus 로고
    • Chapter 3, (Fink G. and Harmar A. J., eds), John Wiley & Sons, New York
    • Turner A. J., Hooper N. M., and Kenny A. J. (1989) Chapter 3, in Neuropeptides: A Methodology (Fink G. and Harmar A. J., eds), pp. 120-127. John Wiley & Sons, New York.
    • (1989) Neuropeptides: A Methodology , pp. 120-127
    • Turner, A.J.1    Hooper, N.M.2    Kenny, A.J.3
  • 35
    • 0022245187 scopus 로고
    • Degradation of alpha and beta neo-endorphin by rat brain membrane peptidases
    • Ulrich C. and Hersh L. B. (1985) Degradation of alpha and beta neo-endorphin by rat brain membrane peptidases. Peptides 6, 475-482.
    • (1985) Peptides , vol.6 , pp. 475-482
    • Ulrich, C.1    Hersh, L.B.2
  • 36
    • 0019948751 scopus 로고
    • Nociception, enkephalin content and dipeptidyl carboxypeptidase activity in brain of mice treated with exopeptidase inhibitors
    • Zhang A. Z., Yang H. Y., and Costa E. (1982) Nociception, enkephalin content and dipeptidyl carboxypeptidase activity in brain of mice treated with exopeptidase inhibitors. Neuropharmacology 21, 625-630.
    • (1982) Neuropharmacology , vol.21 , pp. 625-630
    • Zhang, A.Z.1    Yang, H.Y.2    Costa, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.