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Volumn 379, Issue 6, 1998, Pages 711-719

Isolation and characterization of an alanyl aminopeptidase from rat liver cytosol as a puromycin-sensitive enkephalin-degrading aminopeptidase

Author keywords

N terminal amino acid sequence; Purification; Puromycin sensitive alanyl aminopeptidase; Rat liver cytosol

Indexed keywords

1,10 PHENANTHROLINE; ACTINONIN; AMASTATIN; BESTATIN; LIVER ENZYME; MICROSOMAL AMINOPEPTIDASE; PUROMYCIN;

EID: 0031867950     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.6.711     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 0030968503 scopus 로고    scopus 로고
    • cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity
    • Adachi, H., Tsujimoto, M., Fukasawa, M., Sato, Y., Arai, H., Inoue, K., and Nishimura, T. (1997). cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity. Eur. J. Biochem. 245, 283-288.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 283-288
    • Adachi, H.1    Tsujimoto, M.2    Fukasawa, M.3    Sato, Y.4    Arai, H.5    Inoue, K.6    Nishimura, T.7
  • 2
    • 0023156650 scopus 로고
    • An immunohistochemical study of endopeptidase-24.11 and aminopeptidase N in lymphoid tissues
    • Bowes, M.A., and Kenny, A.J. (1987). An immunohistochemical study of endopeptidase-24.11 and aminopeptidase N in lymphoid tissues. Immunology 60, 247-253.
    • (1987) Immunology , vol.60 , pp. 247-253
    • Bowes, M.A.1    Kenny, A.J.2
  • 3
    • 0023712893 scopus 로고
    • Isolation and characterization of an amphilic form of human intestinal aminopeptidase N
    • Caporale, C., and Troncone, R. (1988). Isolation and characterization of an amphilic form of human intestinal aminopeptidase N. J. Pediatr. Gastroentrol. Nutri. 7, 675-679.
    • (1988) J. Pediatr. Gastroentrol. Nutri. , vol.7 , pp. 675-679
    • Caporale, C.1    Troncone, R.2
  • 4
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase:sequence analysis, expression, and functional characterization
    • Constam, D.R., Tobler, A.R., Rensing-Ehl, 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.R.1    Tobler, A.R.2    Rensing-Ehl, A.3    Kemler, I.4    Hersh, L.B.5    Fontana, A.6
  • 5
    • 0026729302 scopus 로고
    • Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV
    • Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L.K., Sjöström, H., Norén, O., and Laude, H. (1992). Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV. Nature 357, 417-420.
    • (1992) Nature , vol.357 , pp. 417-420
    • Delmas, B.1    Gelfi, J.2    L'Haridon, R.3    Vogel, L.K.4    Sjöström, H.5    Norén, O.6    Laude, H.7
  • 6
    • 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
  • 7
    • 0024382672 scopus 로고
    • Specificity of action of human brain alanyl aminopeptidase on Leu-enkephalin and dynorphin-related peptides
    • Gibson, A.M., McDermott, J.R., Lauffart, B., and Mantle, D. (1989). Specificity of action of human brain alanyl aminopeptidase on Leu-enkephalin and dynorphin-related peptides. Neuropeptides 13, 259-262.
    • (1989) Neuropeptides , vol.13 , pp. 259-262
    • Gibson, A.M.1    McDermott, J.R.2    Lauffart, B.3    Mantle, D.4
  • 8
    • 0026764311 scopus 로고
    • Proteolysis, proteasome and antigen presentation
    • Goldberg, A.L., and Rock, K.L. (1992). Proteolysis, proteasome and antigen presentation. Nature 357, 375-379.
    • (1992) Nature , vol.357 , pp. 375-379
    • Goldberg, A.L.1    Rock, K.L.2
  • 9
    • 0019432699 scopus 로고
    • An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin
    • Hersh, L.B., and McKelvy, J.F. (1981). An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin. J. Neurochem. 36, 171-178.
    • (1981) J. Neurochem. , vol.36 , pp. 171-178
    • Hersh, L.B.1    McKelvy, J.F.2
  • 10
    • 0026655048 scopus 로고
    • Purification and properties of an aminopeptidase from rat-liver cytosol
    • Hiroi, Y., Endo, Y., and Natori, Y. (1992). Purification and properties of an aminopeptidase from rat-liver cytosol. Arch. Biochem. Biophys. 294, 440-445.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 440-445
    • Hiroi, Y.1    Endo, Y.2    Natori, Y.3
  • 11
    • 0030011385 scopus 로고    scopus 로고
    • Dipeptidyl peptidase II from porcine seminal plasma:purification, characterization, and its homology to granzymes, cytotoxic cell proteinases (CCP 1-4)
    • Huang, K., Takagaki, M., Kani, K., and Ohkubo, I. (1996). Dipeptidyl peptidase II from porcine seminal plasma:purification, characterization, and its homology to granzymes, cytotoxic cell proteinases (CCP 1-4). Biochim. Biophys. Acta 1290, 149-156.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 149-156
    • Huang, K.1    Takagaki, M.2    Kani, K.3    Ohkubo, I.4
  • 12
    • 0030679556 scopus 로고    scopus 로고
    • Alanyl aminopeptidase from human seminal plasma: Purification, characterization and immunohistochemical localization in the male genital tract. (1997)
    • Tokyo
    • Huang, K., Takahara, S., Kinouchi, T., Takeyama, M., Ishida, T., Ueyama, H., Nishi, K., and Ohkubo, I. (1997). Alanyl aminopeptidase from human seminal plasma: purification, characterization and immunohistochemical localization in the male genital tract. (1997). J. Biochem. (Tokyo), 122, 779-787.
    • (1997) J. Biochem. , vol.122 , pp. 779-787
    • Huang, K.1    Takahara, S.2    Kinouchi, T.3    Takeyama, M.4    Ishida, T.5    Ueyama, H.6    Nishi, K.7    Ohkubo, I.8
  • 13
    • 0027318680 scopus 로고
    • Two cytosolic puromycin-sensitive aminopeptidase isoenzymes in chicken brain: Molecular homology to brain-specific 14-3-3 protein
    • Hui, K.S., Saito, M., Lajtha, A., Yamamoto, K., and Osawa, T. (1993). Two cytosolic puromycin-sensitive aminopeptidase isoenzymes 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    Lajtha, A.3    Yamamoto, K.4    Osawa, T.5
  • 14
    • 0028983163 scopus 로고
    • Decrease in cytosolic aspartyl-aminopeptidase but not in alanyl-aminopeptidase activity in the frontal cortex of the aged rat
    • Iribar, C., Esteban, M.J., Martines, J.M., and Peinado, J.M. (1995). Decrease in cytosolic aspartyl-aminopeptidase but not in alanyl-aminopeptidase activity in the frontal cortex of the aged rat. Brain Res. 687, 211-213.
    • (1995) Brain Res. , vol.687 , pp. 211-213
    • Iribar, C.1    Esteban, M.J.2    Martines, J.M.3    Peinado, J.M.4
  • 15
    • 0020195866 scopus 로고
    • Purification and characterization of an aminopeptidase from porcine liver
    • Tokyo
    • Kawata, S., Imamura, T., Ninomiya, K., and Makizumi, S. (1982). Purification and characterization of an aminopeptidase from porcine liver. J. Biochem. (Tokyo) 92, 1093-1101.
    • (1982) J. Biochem. , vol.92 , pp. 1093-1101
    • Kawata, S.1    Imamura, T.2    Ninomiya, K.3    Makizumi, S.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0024518875 scopus 로고
    • Human myeloid plasma membrane glycoprotein CD 13 (gp 150) is identical to aminopeptidase N
    • Look, A.T., Ashmun, R.A., Shapiro, L.H., and Peiper, S.C. (1989). Human myeloid plasma membrane glycoprotein CD 13 (gp 150) is identical to aminopeptidase N. J. Clin. Invest. 83, 1299-1307.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1299-1307
    • Look, A.T.1    Ashmun, R.A.2    Shapiro, L.H.3    Peiper, S.C.4
  • 18
    • 0024358644 scopus 로고
    • Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: A member of a super family of zinc-metallohydrolases
    • Malfroy, B., Kado-Fong, H., Gros, C., Giros, B., Schwartz, J.C., and Hellmiss, R. (1989). Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases. Biochem. Biophys. Res. Commun. 161, 236-241.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 236-241
    • Malfroy, B.1    Kado-Fong, H.2    Gros, C.3    Giros, B.4    Schwartz, J.C.5    Hellmiss, R.6
  • 19
    • 0020623720 scopus 로고
    • Purification and characterization of the major aminopeptidase from human skeletal muscle
    • Mantle, D., Hardy, M.F., Lauffart, B., McDermott, J. R., Smith, A.L., and Pennington, J.T. (1983). Purification and characterization of the major aminopeptidase from human skeletal muscle. Biochem. J. 211, 567-573.
    • (1983) Biochem. J. , vol.211 , pp. 567-573
    • Mantle, D.1    Hardy, M.F.2    Lauffart, B.3    McDermott, J.R.4    Smith, A.L.5    Pennington, J.T.6
  • 20
    • 0024502582 scopus 로고
    • Comparison of major cortical aminopeptidase activity in normal brain and brain from patients with Alzheimer's disease
    • Mantle, D., Lauffart, B., Perry, E.K., and Perry, R.H. (1989). Comparison of major cortical aminopeptidase activity in normal brain and brain from patients with Alzheimer's disease. J. Neurol. Sci. 89, 227-234.
    • (1989) J. Neurol. Sci. , vol.89 , pp. 227-234
    • Mantle, D.1    Lauffart, B.2    Perry, E.K.3    Perry, R.H.4
  • 22
    • 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, 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, J.5
  • 23
    • 0001165102 scopus 로고
    • Exopeptidases
    • J.K. McDonald and A.J. Barrett, eds. (London, UK: Academic Press)
    • McDonald, J.K., and Barrett, A.J. (1986). Exopeptidases. In: Mammalian Proteases: A Glossary and Bibliography, Vol. 2, J.K. McDonald and A.J. Barrett, eds. (London, UK: Academic Press), pp.111-144.
    • (1986) Mammalian Proteases: A Glossary and Bibliography , vol.2 , pp. 111-144
    • McDonald, J.K.1    Barrett, A.J.2
  • 24
    • 0023743331 scopus 로고
    • Studies on the tissue distribution of the puromycin-sensitive enkaphalin-degrading aminopeptidases
    • McLellan, S., Dyer, S.H., Rodringuer, G., and Hersh, L.B. (1988). Studies on the tissue distribution of the puromycin-sensitive enkaphalin-degrading aminopeptidases. J. Neurochem. 51, 1552-1559.
    • (1988) J. Neurochem. , vol.51 , pp. 1552-1559
    • McLellan, S.1    Dyer, S.H.2    Rodringuer, G.3    Hersh, L.B.4
  • 28
    • 0028039993 scopus 로고
    • Identification of a 130-kilodalton human biliary concanavalin a binding protein as aminopeptidase N
    • Offner, G.D., Gong, D., and Afdhal, N.H. (1994). Identification of a 130-kilodalton human biliary concanavalin A binding protein as aminopeptidase N. Gastroenterology 106, 755-762.
    • (1994) Gastroenterology , vol.106 , pp. 755-762
    • Offner, G.D.1    Gong, D.2    Afdhal, N.H.3
  • 29
    • 0024230736 scopus 로고
    • Purification and characterization of human plasma Zn-α2-glycoprotein
    • Ohkubo, I., Niwa, M., and Sasaki, M. (1988). Purification and characterization of human plasma Zn-α2-glycoprotein. Prep. Biochem. 18, 413-430.
    • (1988) Prep. Biochem. , vol.18 , pp. 413-430
    • Ohkubo, I.1    Niwa, M.2    Sasaki, M.3
  • 31
    • 0024323498 scopus 로고
    • Cloning of the pig aminopeptidase N gene. Identification of possible regulatory elements and the exon distribution in relation to the membrane-spaning region
    • Olsen, J., Sjostrom, H., and Noren, O. (1989). Cloning of the pig aminopeptidase N gene. Identification of possible regulatory elements and the exon distribution in relation to the membrane-spaning region. FEBS Lett. 251, 275-281.
    • (1989) FEBS Lett. , vol.251 , pp. 275-281
    • Olsen, J.1    Sjostrom, H.2    Noren, O.3
  • 32
    • 0027434567 scopus 로고
    • The oligomeric structure of renal aminopeptidase N from bovine brush-border membrane vesicles
    • Plakidou Dymock, S., and McGivan, J.D. (1993). The oligomeric structure of renal aminopeptidase N from bovine brush-border membrane vesicles. Bichim. Biophys. Acta 1145, 105-112.
    • (1993) Bichim. Biophys. Acta , vol.1145 , pp. 105-112
    • Plakidou Dymock, S.1    McGivan, J.D.2
  • 33
    • 0025169326 scopus 로고
    • Identification and characterization of the major stilbene-disulphonate- And concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N
    • See, H., and Reithmeier, R.A. (1990). Identification and characterization of the major stilbene-disulphonate-and concanavalin A-binding protein of the porcine renal brush-border membrane as aminopeptidase N. Biochem. J. 271, 147-155.
    • (1990) Biochem. J. , vol.271 , pp. 147-155
    • See, H.1    Reithmeier, R.A.2
  • 34
    • 0022370746 scopus 로고
    • Bestatin, a microbial aminopeptidase inhibitor, inhibits DNA synthesis induced by insulin or epidermal growth factor in primary cultured rat hepatocyte
    • Tokyo
    • Takahashi, S., Kato, H., Seki, T., Noguchi, T., Naito, H., Aoyagi, T., and Umezawa, H. (1985). Bestatin, a microbial aminopeptidase inhibitor, inhibits DNA synthesis induced by insulin or epidermal growth factor in primary cultured rat hepatocyte. J. Antibiot. (Tokyo) 38, 1767-1773.
    • (1985) J. Antibiot. , vol.38 , pp. 1767-1773
    • Takahashi, S.1    Kato, H.2    Seki, T.3    Noguchi, T.4    Naito, H.5    Aoyagi, T.6    Umezawa, H.7
  • 35
    • 0024428352 scopus 로고
    • The effects of bestatin, a microbial aminopeptidase inhibitor, on epidermal growth factor-induced DNA synthesis and cell division in primary cultured hepatocytes of rats
    • Takahashi, S., Ohishi, Y., Kato, H., Noguchi, T., Naito, H., and Aoyagi, T. (1989). The effects of bestatin, a microbial aminopeptidase inhibitor, on epidermal growth factor-induced DNA synthesis and cell division in primary cultured hepatocytes of rats. Exp. Cell Res. 183, 399-412.
    • (1989) Exp. Cell Res. , vol.183 , pp. 399-412
    • Takahashi, S.1    Ohishi, Y.2    Kato, H.3    Noguchi, T.4    Naito, H.5    Aoyagi, T.6
  • 36
    • 0027208935 scopus 로고
    • Aminopeptidases: Towards a mechanism of action
    • Taylor, A. (1993). Aminopeptidases: towards a mechanism of action. Trends Biochem. Sci. 18, 167-172.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-172
    • Taylor, A.1
  • 38
    • 0021224832 scopus 로고
    • Purification and characterization of aminopeptidase N from human plasma
    • Tokioka, T.M., Hiwasa, K., and Kokubu, T. (1984). Purification and characterization of aminopeptidase N from human plasma. Enzyme 32, 65-75.
    • (1984) Enzyme , vol.32 , pp. 65-75
    • Tokioka, T.M.1    Hiwasa, K.2    Kokubu, T.3
  • 39
    • 0024511780 scopus 로고
    • Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N
    • Watt, V.M., and Yip, C.C. (1989). Amino acid sequence deduced from a rat kidney cDNA suggests it encodes the Zn-peptidase aminopeptidase N. J. Biol. Chem. 264, 5480-5487.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5480-5487
    • Watt, V.M.1    Yip, C.C.2
  • 40
    • 0027589142 scopus 로고
    • Complete sequence of rabbit kidney aminopeptidase N and mRNA localization in rabbit kidney by in situ hybridization
    • Yang, X.F., Milhiet, P.E., Gaudoux, F., Crine, P., and Boileau, G. (1993). Complete sequence of rabbit kidney aminopeptidase N and mRNA localization in rabbit kidney by in situ hybridization. Biochem. Cell Biol. 71, 278-287.
    • (1993) Biochem. Cell Biol. , vol.71 , pp. 278-287
    • Yang, X.F.1    Milhiet, P.E.2    Gaudoux, F.3    Crine, P.4    Boileau, G.5


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