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Volumn 137, Issue 3, 2004, Pages 373-382

Todarepsin, a new cathepsin D from hepatopancreas of Japanese common squid (Todarodes pacificus)

Author keywords

Antipain, (S) 1 carboxy 2 phenyethyl carbamoyl L arginyl L valyl L arginal; Aspartic proteinase; Cathepsin D; cDNA; Hepatopancreas; Liver; Phylogenetic tree; Squid (Todarodes pacificus); Todarepsin; tpaD gene

Indexed keywords

AMINO ACID; ASPARTIC PROTEINASE; CATHEPSIN D; COMPLEMENTARY DNA; PEPSTATIN; PEPTIDE; TODAREPSIN; UNCLASSIFIED DRUG;

EID: 1842422074     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2004.01.006     Document Type: Article
Times cited : (21)

References (35)
  • 2
    • 0015458030 scopus 로고
    • Biological activity of pepstatins, pepstanone a and partial peptides on pepsin, cathepsin D and renin
    • Aoyagi T., Morishima H., Nishizawa R., Kunimoto S., Takeuchi T.J. Biological activity of pepstatins, pepstanone A and partial peptides on pepsin, cathepsin D and renin. Antibiotics. 25:1972;689-694.
    • (1972) Antibiotics , vol.25 , pp. 689-694
    • Aoyagi, T.1    Morishima, H.2    Nishizawa, R.3    Kunimoto, S.4    Takeuchi, T.J.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the determination of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the determination of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0022471036 scopus 로고
    • Activation of intracellular serine proteinase in Bacillus subtilis cells during sporulation
    • Burnett T.J., Shankweiler G.W., Hageman J.H. Activation of intracellular serine proteinase in Bacillus subtilis cells during sporulation. J. Bacteriol. 165:1986;139-145.
    • (1986) J. Bacteriol. , vol.165 , pp. 139-145
    • Burnett, T.J.1    Shankweiler, G.W.2    Hageman, J.H.3
  • 5
    • 0017613741 scopus 로고
    • Lysosomes and protein degradation
    • Dean R.T. Lysosomes and protein degradation. Acta Biol. Med. Ger. 36:1977;1815-1820.
    • (1977) Acta Biol. Med. Ger. , vol.36 , pp. 1815-1820
    • Dean, R.T.1
  • 6
    • 0023943263 scopus 로고
    • Cathepsin D is membrane-associated in macrophage endosome
    • Diment S., Leech M.S., Stahl P.D. Cathepsin D is membrane-associated in macrophage endosome. J. Biol. Chem. 263:1988;6901-6907.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6901-6907
    • Diment, S.1    Leech, M.S.2    Stahl, P.D.3
  • 7
    • 1842442165 scopus 로고
    • The primary structure of prochymosin (prorennin) EC 3.4.4.3. Some tryptic fragments of a maleylated preparation
    • Foltman B., Andersen B. The primary structure of prochymosin (prorennin) EC 3.4.4.3. Some tryptic fragments of a maleylated preparation. FEBS Lett. 17:1971;87-89.
    • (1971) FEBS Lett. , vol.17 , pp. 87-89
    • Foltman, B.1    Andersen, B.2
  • 8
    • 0023764679 scopus 로고
    • Characterization and properties of two monoclonal antibodies specific for the Mr 52 000 precursor of cathepsin D in human breast cancer cells
    • Freiss G., Vignon F., Rochefort H. Characterization and properties of two monoclonal antibodies specific for the Mr 52 000 precursor of cathepsin D in human breast cancer cells. Cancer Res. 48:1988;3709-3715.
    • (1988) Cancer Res. , vol.48 , pp. 3709-3715
    • Freiss, G.1    Vignon, F.2    Rochefort, H.3
  • 9
    • 84985399999 scopus 로고
    • Purification and characterization of cathepsin D from the digestive gland of the pelagic squid Todarodes sagittatus
    • Gildberg A. Purification and characterization of cathepsin D from the digestive gland of the pelagic squid Todarodes sagittatus. J. Sci. Food Agric. 39:1987;85-94.
    • (1987) J. Sci. Food Agric. , vol.39 , pp. 85-94
    • Gildberg, A.1
  • 10
    • 0024433733 scopus 로고
    • Sequential processing of lysosomal acid phosphatase by a cytoplasmic thiol protease and lysosomal proteinase
    • Gottschalk S., Waheed A., Schmidt B., Ladler P., von Figura K. Sequential processing of lysosomal acid phosphatase by a cytoplasmic thiol protease and lysosomal proteinase. EMBO J. 8:1989;3215-3219.
    • (1989) EMBO J. , vol.8 , pp. 3215-3219
    • Gottschalk, S.1    Waheed, A.2    Schmidt, B.3    Ladler, P.4    Von Figura, K.5
  • 11
    • 0021234561 scopus 로고
    • Cathepsin D-mediated processing of procollagen: Lysosomal enzyme involvement in secretory processing procollagen
    • Helseth D.L. jr, Veis A. Cathepsin D-mediated processing of procollagen: lysosomal enzyme involvement in secretory processing procollagen. Proc. Natl. Acad. Sci. USA. 81:1984;3302-3306.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3302-3306
    • Helseth Jr., D.L.1    Veis, A.2
  • 12
    • 0036006819 scopus 로고    scopus 로고
    • Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids
    • Hiramatsu N., Ichikawa N., Fukuda H., Fujita T., Sullivan C.V., Hara A. Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J. Exp. Zool. 292:2002;11-25.
    • (2002) J. Exp. Zool. , vol.292 , pp. 11-25
    • Hiramatsu, N.1    Ichikawa, N.2    Fukuda, H.3    Fujita, T.4    Sullivan, C.V.5    Hara, A.6
  • 13
    • 0026079091 scopus 로고
    • Expression and maturation of human cathepsin D in baby-hamster kidney cell
    • Horst M., Hasilik A. Expression and maturation of human cathepsin D in baby-hamster kidney cell. Biochem. J. 273:1991;355-361.
    • (1991) Biochem. J. , vol.273 , pp. 355-361
    • Horst, M.1    Hasilik, A.2
  • 14
    • 0018801568 scopus 로고
    • Cathepsin D isozyme from porcine spleens. Large scale purification and polypeptide chain arrangements
    • Huang J.S., Huang S.S., Tang J. Cathepsin D isozyme from porcine spleens. Large scale purification and polypeptide chain arrangements. J. Biol. Chem. 254:1979;11405-11417.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11405-11417
    • Huang, J.S.1    Huang, S.S.2    Tang, J.3
  • 16
    • 0019152429 scopus 로고
    • A cathepsin D-like acid proteinase from human gastric mucosa. Purification and characterization
    • Kageyama T., Takahashi K. A cathepsin D-like acid proteinase from human gastric mucosa. Purification and characterization. J. Biochem. 87:1980;725-735.
    • (1980) J. Biochem. , vol.87 , pp. 725-735
    • Kageyama, T.1    Takahashi, K.2
  • 17
    • 0017255236 scopus 로고
    • Interaction of human cathepsin D with the inhibitor pepstatin
    • Knight C.G., Barrett A.J. Interaction of human cathepsin D with the inhibitor pepstatin. Biochem. J. 155:1976;117-125.
    • (1976) Biochem. J. , vol.155 , pp. 117-125
    • Knight, C.G.1    Barrett, A.J.2
  • 18
    • 0032859883 scopus 로고    scopus 로고
    • Thimet oligopeptidase cleaves the full-length Alzheimer amyloid precursor protein at a β-secretase cleavage site in COS cells
    • Koike H., Seki H., Kouchi Z., Ito M., Kikuchi T., Tomioka S., et al. Thimet oligopeptidase cleaves the full-length Alzheimer amyloid precursor protein at a β-secretase cleavage site in COS cells. J. Biochem. 126:1999;235-242.
    • (1999) J. Biochem. , vol.126 , pp. 235-242
    • Koike, H.1    Seki, H.2    Kouchi, Z.3    Ito, M.4    Kikuchi, T.5    Tomioka, S.6
  • 20
    • 0027931263 scopus 로고
    • Molecular cloning and nucleotide sequence of complementary DNA for penicillolysin gene, plnC, an 18kDa metalloendopeptidase gene from Penicillium citrinum
    • Matsumoto K., Yamaguchi M., Ichishima E. Molecular cloning and nucleotide sequence of complementary DNA for penicillolysin gene, plnC, an 18kDa metalloendopeptidase gene from Penicillium citrinum. Biochem. Biophys. Acta. 1218:1994;469-472.
    • (1994) Biochem. Biophys. Acta , vol.1218 , pp. 469-472
    • Matsumoto, K.1    Yamaguchi, M.2    Ichishima, E.3
  • 21
    • 0017880177 scopus 로고
    • The structure and function of acid protease. VIII. Purification and characterization of cathepsin D from Japanese monkey lung
    • Moriyama A., Takahashi K. The structure and function of acid protease. VIII. Purification and characterization of cathepsin D from Japanese monkey lung. J. Biochem. 83:1978;441-451.
    • (1978) J. Biochem. , vol.83 , pp. 441-451
    • Moriyama, A.1    Takahashi, K.2
  • 22
    • 0035132092 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D from herring muscle (Clupea harengus)
    • Nielsen L.B., Nielsen H.H. Purification and characterization of cathepsin D from herring muscle (Clupea harengus). Comp. Biochem. Physiol. B128:2001;351-363.
    • (2001) Comp. Biochem. Physiol. , vol.128 , pp. 351-363
    • Nielsen, L.B.1    Nielsen, H.H.2
  • 23
    • 0023955872 scopus 로고
    • Identification of latent procathepsin H in microsomal lumen
    • Nishimura Y., Kato K. Identification of latent procathepsin H in microsomal lumen. Arch. Biochem. Biophys. 260:1988;712-718.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 712-718
    • Nishimura, Y.1    Kato, K.2
  • 24
    • 0024354840 scopus 로고
    • Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosome
    • Nishimura Y., Kawabata T., Furuno K., Kato K. Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosome. Arch. Biochem. Biophys. 271:1989;400-406.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 400-406
    • Nishimura, Y.1    Kawabata, T.2    Furuno, K.3    Kato, K.4
  • 25
    • 0023009774 scopus 로고
    • Production of biologically active fragments of parathyroid hormone by isolated Kupffer's cells
    • Pillai S., Zull J.E. Production of biologically active fragments of parathyroid hormone by isolated Kupffer's cells. J. Biol. Chem. 261:1986;14919-14923.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14919-14923
    • Pillai, S.1    Zull, J.E.2
  • 26
    • 0017805720 scopus 로고
    • The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose
    • Roberts N.B., Taylor W.H. The preparation and purification of individual human pepsins by using diethylaminoethyl-cellulose. Biochem. J. 169:1987;607-615.
    • (1987) Biochem. J. , vol.169 , pp. 607-615
    • Roberts, N.B.1    Taylor, W.H.2
  • 27
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells
    • Saftig P., Hetman M., Schmahl W., Weber K., Heine L., Mossmann H., et al. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 14:1995;3599-3608.
    • (1995) EMBO J. , vol.14 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6
  • 28
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 29
    • 0004501772 scopus 로고
    • Neutral proteinases I and II of Aspergillus sojae isolation in homogeneous form
    • Sekine H. Neutral proteinases I and II of Aspergillus sojae isolation in homogeneous form. Agr. Biol. Chem. 36:1972;198-206.
    • (1972) Agr. Biol. Chem. , vol.36 , pp. 198-206
    • Sekine, H.1
  • 30
    • 0027250352 scopus 로고
    • Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments
    • 602-16 609
    • Siman R., Mistretta S., Durkin J.T., Savage M.J., Loh T., Trusko S., et al. Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments. J. Biol. Chem. 268:1993;16 602-16 609.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16
    • Siman, R.1    Mistretta, S.2    Durkin, J.T.3    Savage, M.J.4    Loh, T.5    Trusko, S.6
  • 31
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic protease
    • Tang J., Wang R.N.S. Evolution in the structure and function of aspartic protease. J. Cell Biochem. 33:1987;53-63.
    • (1987) J. Cell Biochem. , vol.33 , pp. 53-63
    • Tang, J.1    Wang, R.N.S.2
  • 32
    • 0027968068 scopus 로고
    • The 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., Gibson T.J. The CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 33
    • 0024339693 scopus 로고
    • The processing of a cathepsin L precursor in vitro
    • Wiederanders B., Kirschke H. The processing of a cathepsin L precursor in vitro. Arch. Biochem. Biophys. 272:1989;516-521.
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 516-521
    • Wiederanders, B.1    Kirschke, H.2
  • 34
    • 0027651593 scopus 로고
    • Specificity and molecular properties of penicillolysin, a metalloproteinase from Penicillium citrinum
    • Yamaguchi M., Hanzawa S., Hirano K., Yamagata Y., Ichishima E. Specificity and molecular properties of penicillolysin, a metalloproteinase from Penicillium citrinum. Phytochemistry. 33:1993;1317-1321.
    • (1993) Phytochemistry , vol.33 , pp. 1317-1321
    • Yamaguchi, M.1    Hanzawa, S.2    Hirano, K.3    Yamagata, Y.4    Ichishima, E.5
  • 35
    • 0032790483 scopus 로고    scopus 로고
    • Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin e and cathepsin D
    • Yasuda Y., Kageyama T., Akamine A., Shibata M., Kominami E., Uchiyama Y., et al. Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D. J. Biochem. 125:1999;1137-1143.
    • (1999) J. Biochem. , vol.125 , pp. 1137-1143
    • Yasuda, Y.1    Kageyama, T.2    Akamine, A.3    Shibata, M.4    Kominami, E.5    Uchiyama, Y.6


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