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Volumn 245, Issue 2, 1997, Pages 283-288

cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity

Author keywords

Aminoendopeptidase; Aminopeptidase; cDNA cloning; Expression; Thiol protease

Indexed keywords

AMINOPEPTIDASE; CYSTEINE PROTEINASE; HYDROLASE; PROTEINASE;

EID: 0030968503     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00283.x     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0020511655 scopus 로고
    • Accumulation of acid soluble peptides in rat liver in vivo and after injection of bestatin
    • Noguchi, T., Sonaka, I. & Naito, H. (1983) Accumulation of acid soluble peptides in rat liver in vivo and after injection of bestatin, Agric. Biol. Chem. 47, 647-650.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 647-650
    • Noguchi, T.1    Sonaka, I.2    Naito, H.3
  • 2
    • 0023268858 scopus 로고
    • Mode of action of bestatin and leupeptin to induce the accumulation of acid soluble peptides in rat liver in vivo and properties of the accumulated peptides. The important role of bestatin- and leupeptin-sensitive proteases in the protein degradation pathway in vivo
    • Takahashi, S., Kato, H., Takahashi, A., Noguchi, T. & Naito, H. (1987) Mode of action of bestatin and leupeptin to induce the accumulation of acid soluble peptides in rat liver in vivo and properties of the accumulated peptides. The important role of bestatin- and leupeptin-sensitive proteases in the protein degradation pathway in vivo, Int. J. Biochem. 19, 401-405.
    • (1987) Int. J. Biochem. , vol.19 , pp. 401-405
    • Takahashi, S.1    Kato, H.2    Takahashi, A.3    Noguchi, T.4    Naito, H.5
  • 3
    • 0024371802 scopus 로고
    • Role of bestatin-sensitive exopeptidase in the intracellular degradation of hepatic proteins
    • Botbol, V. & Scornik, O. A. (1989) Role of bestatin-sensitive exopeptidase in the intracellular degradation of hepatic proteins, J. Biol. Chem 264, 13 504-13 509.
    • (1989) J. Biol. Chem , vol.264 , pp. 13504-13509
    • Botbol, V.1    Scornik, O.A.2
  • 4
    • 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. & 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
  • 5
    • 0023743331 scopus 로고
    • Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases
    • McLellen, S., Dyer, S. H., Rodriguez, G. & 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
    • McLellen, S.1    Dyer, S.H.2    Rodriguez, G.3    Hersh, L.B.4
  • 6
    • 0025269825 scopus 로고
    • Aminopeptidase in human CSF which degrades delta-sleeping inducing peptide (DSIP)
    • Nyberg, F., Thornwall, M. & Hetta, J. (1990) Aminopeptidase in human CSF which degrades delta-sleeping inducing peptide (DSIP), Biochem. Biophys. Res. Commun. 167, 1256-1262.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 1256-1262
    • Nyberg, F.1    Thornwall, M.2    Hetta, J.3
  • 7
    • 0024544669 scopus 로고
    • Presence of a particulate thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase activity in rat liver
    • Scharfmann, R., Morgat, J. L. & Aratan-Spire, S. (1989) Presence of a particulate thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase activity in rat liver, Neuroendocrinology 49, 442-448.
    • (1989) Neuroendocrinology , vol.49 , pp. 442-448
    • Scharfmann, R.1    Morgat, J.L.2    Aratan-Spire, S.3
  • 8
    • 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.-I., Oishi, Y., Kato, H., Noguchi, T. Naito, H. & 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.-I.1    Oishi, Y.2    Kato, H.3    Noguchi, T.4    Naito, H.5    Aoyagi, T.6
  • 9
    • 0026783641 scopus 로고
    • Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae
    • Chang, Y.-H., Teichert, U. & Smith, J. A. (1992) Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae, J. Biol. Chem. 267, 8007-8011.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8007-8011
    • Chang, Y.-H.1    Teichert, U.2    Smith, J.A.3
  • 10
    • 0013946995 scopus 로고
    • Leucine aminopeptidase in extracts of swine muscle
    • Joseph, R. L. & Sanders, W. J. (1966) Leucine aminopeptidase in extracts of swine muscle, Biochem. J. 100, 827-832.
    • (1966) Biochem. J. , vol.100 , pp. 827-832
    • Joseph, R.L.1    Sanders, W.J.2
  • 11
    • 0020623720 scopus 로고
    • Purification and partial characterization of arginine aminopeptidase from human skeletal muscle
    • Mantle, D., Lauffart, B. & Pennington, R. J. T. (1984) Purification and partial characterization of arginine aminopeptidase from human skeletal muscle, Biochem. Soc. Trans. 211, 567-573.
    • (1984) Biochem. Soc. Trans. , vol.211 , pp. 567-573
    • Mantle, D.1    Lauffart, B.2    Pennington, R.J.T.3
  • 12
    • 0021950945 scopus 로고
    • Purification and characterization of two Cl - Activated aminopeptidases hydrolyzing basic termini from human skeletal muscle
    • Mantle, D., Lauffart, B., McDermott, J. R., Kidd, A. M. & Pennington, R. J. T. (1985) Purification and characterization of two Cl - activated aminopeptidases hydrolyzing basic termini from human skeletal muscle, Eur. J. Biochem. 147, 307-312.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 307-312
    • Mantle, D.1    Lauffart, B.2    McDermott, J.R.3    Kidd, A.M.4    Pennington, R.J.T.5
  • 13
    • 0023447871 scopus 로고
    • Human skeletal muscle contains two major aminopeptidases: An anion-activated aminopeptidase B and an aminopeptidase M-like enzyme
    • Ishiura, S., Yamamoto, T., Yamamoto, M., Nojima, M., Aoyagi, T. & Sugita, H. (1987) Human skeletal muscle contains two major aminopeptidases: an anion-activated aminopeptidase B and an aminopeptidase M-like enzyme, J. Biochem. (Tokyo) 102, 1023-1031.
    • (1987) J. Biochem. (Tokyo) , vol.102 , pp. 1023-1031
    • Ishiura, S.1    Yamamoto, T.2    Yamamoto, M.3    Nojima, M.4    Aoyagi, T.5    Sugita, H.6
  • 14
    • 0017046457 scopus 로고
    • Purification and properties of an aminopeptidase from rabbit skeletal muscle
    • Otsuka, Y., Okitani, A., Katakai, R. & Fujimaki, M. (1976) Purification and properties of an aminopeptidase from rabbit skeletal muscle, Agric. Biol. Chem. 40, 2335-2342.
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 2335-2342
    • Otsuka, Y.1    Okitani, A.2    Katakai, R.3    Fujimaki, M.4
  • 15
    • 0642381214 scopus 로고
    • Further characterization of aminopeptidase of rabbit skeletal muscle
    • Otsuka, Y., Okitani, A., Kondo, Y., Kato, H. & Fujimaki, M. (1980) Further characterization of aminopeptidase of rabbit skeletal muscle, Agric. Biol. Chem. 44, 1617-1622.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 1617-1622
    • Otsuka, Y.1    Okitani, A.2    Kondo, Y.3    Kato, H.4    Fujimaki, M.5
  • 17
    • 0026184666 scopus 로고
    • Purification and properties of aminopeptidase C from chicken skeletal muscle
    • Nishimura, T., Kato, Y. Okitani, A. & Kato, H. (1991) Purification and properties of aminopeptidase C from chicken skeletal muscle, Agric. Biol. Chem. 55, 1771-1778.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1771-1778
    • Nishimura, T.1    Kato, Y.2    Okitani, A.3    Kato, H.4
  • 18
    • 0026524254 scopus 로고
    • Purification and properties of aminopeptidase C from chicken skeletal muscle
    • Nishimura, T., Kato, Y., Rhyu, M. R., Okitani, A. & Kato, H. (1992) Purification and properties of aminopeptidase C from chicken skeletal muscle, Comp. Biochem. Physiol. 102B, 129-135.
    • (1992) Comp. Biochem. Physiol. , vol.102 B , pp. 129-135
    • Nishimura, T.1    Kato, Y.2    Rhyu, M.R.3    Okitani, A.4    Kato, H.5
  • 19
    • 0042299174 scopus 로고
    • Purification and properties of BANA hydrolase H of rabbit skeletal muscle, a new enzyme hydrolyzing α-N-benzoylarginine-β-naphthylamide
    • Okitani, A., Nishimura, T., Otsuka, U., Matsukura, Y. & Kato, H. (1980) Purification and properties of BANA hydrolase H of rabbit skeletal muscle, a new enzyme hydrolyzing α-N-benzoylarginine-β-naphthylamide, Agric. Biol. Chem. 44, 1705-1708.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 1705-1708
    • Okitani, A.1    Nishimura, T.2    Otsuka, U.3    Matsukura, Y.4    Kato, H.5
  • 20
    • 0019555638 scopus 로고
    • Characterization of hydrolase H, a new muscle protease possessing aminoendopeptidase activity
    • Okitani, A., Nishimura, T. & Kato, H. (1981) Characterization of hydrolase H, a new muscle protease possessing aminoendopeptidase activity, Eur. J. Biochem. 115, 269-274.
    • (1981) Eur. J. Biochem. , vol.115 , pp. 269-274
    • Okitani, A.1    Nishimura, T.2    Kato, H.3
  • 21
    • 0021044841 scopus 로고
    • Mode of action towards oligopeptides and proteins of hydrolase H, a high-molecular-weight mass aminoendopeptidase from rabbit skeletal muscle
    • Nishimura, T., Okitani, A., Katakai, R. & Kato, H. (1983) Mode of action towards oligopeptides and proteins of hydrolase H, a high-molecular-weight mass aminoendopeptidase from rabbit skeletal muscle. Eur. J. Biochem. 137, 23-27.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 23-27
    • Nishimura, T.1    Okitani, A.2    Katakai, R.3    Kato, H.4
  • 22
    • 84908815093 scopus 로고
    • Purification and properties of aminopeptidase H from porcine skeletal muscle
    • Nishimura, T., Rhyu, M. R. & Kato, H. (1991) Purification and properties of aminopeptidase H from porcine skeletal muscle, Agric. Biol. Chem. 55, 1779-1786.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1779-1786
    • Nishimura, T.1    Rhyu, M.R.2    Kato, H.3
  • 23
    • 0026701567 scopus 로고
    • Purification and properties of aminopeptidase H from chicken skeletal muscle
    • Rhyu, M. R., Nishimura, T., Kato, Y. Okitani, A. & Kato, H. (1992) Purification and properties of aminopeptidase H from chicken skeletal muscle, Eur. J. Biochem. 208, 53-59.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 53-59
    • Rhyu, M.R.1    Nishimura, T.2    Kato, Y.3    Okitani, A.4    Kato, H.5
  • 24
    • 0012786896 scopus 로고
    • Purification and properties of aminopeptidase H from bovine skeletal muscle
    • Nishimura, T., Rhyu, M. R., Kato, H. & Arai, S. (1994) Purification and properties of aminopeptidase H from bovine skeletal muscle, J. Agric. Food Chem. 46, 2709-2712.
    • (1994) J. Agric. Food Chem. , vol.46 , pp. 2709-2712
    • Nishimura, T.1    Rhyu, M.R.2    Kato, H.3    Arai, S.4
  • 25
    • 0023677326 scopus 로고
    • Rationalization of aminopeptidase activities in human skeletal muscle soluble extract
    • Lauffart, B. & Mantle, D. (1988) Rationalization of aminopeptidase activities in human skeletal muscle soluble extract, Biochim. Biophys. Acta 956, 300-306.
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 300-306
    • Lauffart, B.1    Mantle, D.2
  • 26
    • 8244221271 scopus 로고
    • The peptidases of skeletal, heart, and uterine muscle
    • Smith, E. L. (1948) The peptidases of skeletal, heart, and uterine muscle, J. Biol. Chem. 173, 553-569.
    • (1948) J. Biol. Chem. , vol.173 , pp. 553-569
    • Smith, E.L.1
  • 27
    • 8244234077 scopus 로고
    • The glycylglycine dipeptidases of skeletal muscle and human uterus
    • Smith, E. L. (1948) The glycylglycine dipeptidases of skeletal muscle and human uterus, J. Biol. Chem. 173, 571-584.
    • (1948) J. Biol. Chem. , vol.173 , pp. 571-584
    • Smith, E.L.1
  • 28
    • 84957881622 scopus 로고
    • Studies on dipeptidases, II. Some properties of the glycyl-L-leucine dipeptidases of animal tissues
    • Smith, E. L. (1948) Studies on dipeptidases, II. Some properties of the glycyl-L-leucine dipeptidases of animal tissues, J. Biol. Chem. 176, 9-19.
    • (1948) J. Biol. Chem. , vol.176 , pp. 9-19
    • Smith, E.L.1
  • 29
  • 30
    • 0023941841 scopus 로고
    • Generation of cDNA probes directed by amino acid sequence: Cloning of urate oxidase
    • Lee, C. C., Wu, X., Gibbs, R. A., Cook, R. G., Muzhy, D. M. & Caskey, C. T. (1988) Generation of cDNA probes directed by amino acid sequence: cloning of urate oxidase, Science 239, 1288-1291.
    • (1988) Science , vol.239 , pp. 1288-1291
    • Lee, C.C.1    Wu, X.2    Gibbs, R.A.3    Cook, R.G.4    Muzhy, D.M.5    Caskey, C.T.6
  • 31
  • 32
    • 0025949477 scopus 로고
    • Screening recombinant DNA libraries: A rapid and efficient method for isolating cDNA clones utilizing the PCR
    • Isola, N. R., Harn, H. J. & Cooper, D. L. (1991) Screening recombinant DNA libraries: a rapid and efficient method for isolating cDNA clones utilizing the PCR, BioTechniques 11, 580-582.
    • (1991) BioTechniques , vol.11 , pp. 580-582
    • Isola, N.R.1    Harn, H.J.2    Cooper, D.L.3
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Anderson, J. (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose, J. Biochem. Biophys. Methods 10, 203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Anderson, J.1
  • 37
    • 0024379958 scopus 로고
    • Bleomycin hydrolase: Molecular cloning, sequencing, and biochemical studies reveal membership in the cysteine protease family
    • Sebti, S. M., Mignano, J. E., Jani, J. P., Srimatkandada, S. & Lazo, J. S. (1989) Bleomycin hydrolase: Molecular cloning, sequencing, and biochemical studies reveal membership in the cysteine protease family, Biochemistry 28, 6544-6548.
    • (1989) Biochemistry , vol.28 , pp. 6544-6548
    • Sebti, S.M.1    Mignano, J.E.2    Jani, J.P.3    Srimatkandada, S.4    Lazo, J.S.5
  • 38
    • 0027499191 scopus 로고
    • BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase
    • Enenkel, C. & Wolf, D. H. (1993) BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase, J. Biol. Chem. 268, 7036-7043.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7036-7043
    • Enenkel, C.1    Wolf, D.H.2
  • 39
    • 0027394008 scopus 로고
    • A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family of member of thiol proteinases
    • Magdolen, U., Muller, G., Magdolen, V. & Bandlow, W. (1993) A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family of member of thiol proteinases, Biochim. Biophys. Acta 1171, 299-303.
    • (1993) Biochim. Biophys. Acta , vol.1171 , pp. 299-303
    • Magdolen, U.1    Muller, G.2    Magdolen, V.3    Bandlow, W.4
  • 41
    • 0023653171 scopus 로고
    • Purification, characterization, and amino acid composition of rabbit pulmonary bleomycin hydrolase
    • Sebti, S. M., DeLeon, J. C. & Lazo, J. S. (1987) Purification, characterization, and amino acid composition of rabbit pulmonary bleomycin hydrolase, Biochemistry 26, 4213-4219.
    • (1987) Biochemistry , vol.26 , pp. 4213-4219
    • Sebti, S.M.1    DeLeon, J.C.2    Lazo, J.S.3


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