메뉴 건너뛰기




Volumn 6, Issue 2, 1997, Pages 173-181

Cysteine proteinase 1 (CP1), a cathepsin L-like enzyme expressed in the Drosophila melanogaster haemocyte cell line mbn-2

Author keywords

cathepsin; cysteine proteinase; Drosophila; haemocyte; lysosome

Indexed keywords

ANIMALIA; DROSOPHILA MELANOGASTER; HEXAPODA; INSECTA; MELANOGASTER;

EID: 0031149558     PISSN: 09621075     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2583.1997.tb00085.x     Document Type: Article
Times cited : (66)

References (27)
  • 1
    • 0029278804 scopus 로고
    • Identification of early genes in the Drosophila immune response by PCR-based differential display: The Attacin a gene and the evolution of attacin-like proteins
    • Åsling, B., Dushay, M.S. and Hultmark, D. (1995) Identification of early genes in the Drosophila immune response by PCR-based differential display: the Attacin A gene and the evolution of attacin-like proteins. Insect Biochem Mol Biol 25: 511-518.
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 511-518
    • Åsling, B.1    Dushay, M.S.2    Hultmark, D.3
  • 2
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti, P.J. and Storer, A.C. (1995) Alignment/phylogeny of the papain superfamily of cysteine proteases. J Mol Biol 246: 273-283.
    • (1995) J Mol Biol , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 4
    • 0029840669 scopus 로고    scopus 로고
    • Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila
    • Dushay, M.S., Åsling B. and Hultmark, D. (1996) Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila. Proc Natl Acad Sci USA 93: 10,343-10,347.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10343-10347
    • Dushay, M.S.1    Åsling, B.2    Hultmark, D.3
  • 5
    • 0002571649 scopus 로고
    • Characterization of two tumorous blood cell lines of Drosophila melanogaster and the viruses they contain
    • Kurstak, E., Maramorosch, K. and Dübendorfer, A., eds, Elsevier/ North-Holland Biomedical Press, Amsterdam
    • Gateff, E., Gissmann, L., Shrestha, R., Plus, N., Pfister, H., Schröder, J. and zur Hausen, H. (1980) Characterization of two tumorous blood cell lines of Drosophila melanogaster and the viruses they contain. Invertebrate systems in Vitro (Kurstak, E., Maramorosch, K. and Dübendorfer, A., eds), pp. 517-533. Elsevier/ North-Holland Biomedical Press, Amsterdam.
    • (1980) Invertebrate Systems in Vitro , pp. 517-533
    • Gateff, E.1    Gissmann, L.2    Shrestha, R.3    Plus, N.4    Pfister, H.5    Schröder, J.6    Zur Hausen, H.7
  • 7
    • 0028243651 scopus 로고
    • Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly), and its involvement in the differentiation of imaginai discs
    • Homma, K., Kurata, S. and Natori, S. (1994) Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly), and its involvement in the differentiation of imaginai discs. J Biol Chem 269: 15,258-15,264.
    • (1994) J Biol Chem , vol.269 , pp. 15258-15264
    • Homma, K.1    Kurata, S.2    Natori, S.3
  • 8
    • 0022109611 scopus 로고
    • Selective translation of heat shock mRNA in Drosophila melanogaster depends on sequence information in the leader
    • Klemenz, R., Hultmark, D. and Gehring, W.J. (1985) Selective translation of heat shock mRNA in Drosophila melanogaster depends on sequence information in the leader. EMBO J 4: 2053-2060.
    • (1985) EMBO J , vol.4 , pp. 2053-2060
    • Klemenz, R.1    Hultmark, D.2    Gehring, W.J.3
  • 9
    • 0024971481 scopus 로고
    • Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus)
    • Laycock, M.V., Hirama, T., Hasnain, S., Watson, D. and Storer, A.C. (1989) Purification and characterization of a digestive cysteine proteinase from the American lobster (Homarus americanus). Biochem J 263: 439-444.
    • (1989) Biochem J , vol.263 , pp. 439-444
    • Laycock, M.V.1    Hirama, T.2    Hasnain, S.3    Watson, D.4    Storer, A.C.5
  • 10
    • 0026001237 scopus 로고
    • Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus)
    • Laycock, M.V., MacKay, R.M., Di Fruscio, M. and Gallant, J.W. (1991) Molecular cloning of three cDNAs that encode cysteine proteinases in the digestive gland of the American lobster (Homarus americanus). FEBS Lett 292: 115-120.
    • (1991) FEBS Lett , vol.292 , pp. 115-120
    • Laycock, M.V.1    MacKay, R.M.2    Di Fruscio, M.3    Gallant, J.W.4
  • 11
    • 0028999492 scopus 로고
    • Molecular cloning and sequencing of two cDNAs encoding cathepsin L-related cysteine proteinases in the nervous system and in the stomach of the Norway lobster (Nephrops norvegicus)
    • Le Boulay, C., Van Wormhoudt, A. and Sellos, D. (1995) Molecular cloning and sequencing of two cDNAs encoding cathepsin L-related cysteine proteinases in the nervous system and in the stomach of the Norway lobster (Nephrops norvegicus). Comp Biochem Physiol B 111: 353-359.
    • (1995) Comp Biochem Physiol B , vol.111 , pp. 353-359
    • Le Boulay, C.1    Van Wormhoudt, A.2    Sellos, D.3
  • 13
    • 0028840144 scopus 로고
    • A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut
    • Matsumoto, I., Watanabe, H., Abe, K., Arai, S. and Emori, Y. (1995) A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut. Eur J Biochem 227: 582-587.
    • (1995) Eur J Biochem , vol.227 , pp. 582-587
    • Matsumoto, I.1    Watanabe, H.2    Abe, K.3    Arai, S.4    Emori, Y.5
  • 14
    • 0028806557 scopus 로고
    • The endosomal-lysosomal system of neurons: New roles
    • Nixon, R.A. and Cataldo, A.M. (1995) The endosomal-lysosomal system of neurons: new roles. Trends Neurosci 18: 489-496.
    • (1995) Trends Neurosci , vol.18 , pp. 489-496
    • Nixon, R.A.1    Cataldo, A.M.2
  • 15
    • 0021760534 scopus 로고
    • Sequence, structure, and codon preference of the Drosophila ribosomal protein 49 gene
    • O'Connell, P.O. and Rosbash, M. (1984) Sequence, structure, and codon preference of the Drosophila ribosomal protein 49 gene. Nucleic Acids Res 12: 5495-5513.
    • (1984) Nucleic Acids Res , vol.12 , pp. 5495-5513
    • O'Connell, P.O.1    Rosbash, M.2
  • 16
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings, N.D. and Barrett, A.J. (1994) Families of cysteine peptidases. Methods Enzymol 244: 461-486.
    • (1994) Methods Enzymol , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 17
    • 0029379847 scopus 로고
    • Processing of procathepsin from Musca domestica eggs
    • Ribolla, P.E.M. and De Blanchi, A.G. (1995) Processing of procathepsin from Musca domestica eggs. Insect Biochem Mol Biol 25: 1011-1017.
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 1011-1017
    • Ribolla, P.E.M.1    De Blanchi, A.G.2
  • 18
    • 0026480587 scopus 로고
    • In vitro induction of cecropin genes: An immune response in a Drosophila blood cell line
    • Samakovlis, C., Åsling, B., Boman, H.G., Gateff, E. and Hultmark, D. (1992) In vitro induction of cecropin genes: an immune response in a Drosophila blood cell line. Biochem Biophys Res Commun 188: 1169-1175.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 1169-1175
    • Samakovlis, C.1    Åsling, B.2    Boman, H.G.3    Gateff, E.4    Hultmark, D.5
  • 20
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro, M.B. and Senapathy, P. (1987) RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucleic Acids Res 15: 7155-7174.
    • (1987) Nucleic Acids Res , vol.15 , pp. 7155-7174
    • Shapiro, M.B.1    Senapathy, P.2
  • 21
    • 0024284551 scopus 로고
    • A ZAP: A bacteriophage a expression vector with in vivo excision properties
    • Short, J.M., Fernandez, J.M., Sorge, J.A. and Huse, W.D. (1988) A ZAP: a bacteriophage A expression vector with in vivo excision properties. Nucleic Acids Res 16: 7583-7600.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7583-7600
    • Short, J.M.1    Fernandez, J.M.2    Sorge, J.A.3    Huse, W.D.4
  • 23
    • 0027493068 scopus 로고
    • Molecular cloning of cDNA for the 29 kDa proteinase participating in decomposition of the larval fat body during metamorphosis of Sarcophaga peregrina (flesh fly)
    • Takahashi, N., Kurata, S. and Natori, S. (1993a) Molecular cloning of cDNA for the 29 kDa proteinase participating in decomposition of the larval fat body during metamorphosis of Sarcophaga peregrina (flesh fly). FEBS Lett 334: 153-157.
    • (1993) FEBS Lett , vol.334 , pp. 153-157
    • Takahashi, N.1    Kurata, S.2    Natori, S.3
  • 24
    • 0027177631 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: Identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro
    • Takahashi, S.Y., Yamamoto, Y., Shionoya, Y. and Kageyama, T. (1993b) Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro. J Biochem 114: 267-272.
    • (1993) J Biochem , vol.114 , pp. 267-272
    • Takahashi, S.Y.1    Yamamoto, Y.2    Shionoya, Y.3    Kageyama, T.4
  • 25
    • 0001573128 scopus 로고
    • Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme
    • Takahashi, S.Y., Zhao, X., Kageyama, T. and Yamamoto, Y. (1992) Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: tissue distribution, developmental changes and the sites of synthesis for the enzyme. Insect Biochem Mol Biol 22: 369-377.
    • (1992) Insect Biochem Mol Biol , vol.22 , pp. 369-377
    • Takahashi, S.Y.1    Zhao, X.2    Kageyama, T.3    Yamamoto, Y.4
  • 26
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14: 4683-4690.
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 27
    • 0028606210 scopus 로고
    • Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori
    • Yamamoto, Y., Takimoto, K., Izumi, S., Toriyama-Sakurai, M., Kageyama, T. and Takahashi, S.Y. (1994) Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori. J Biochem 116: 1330-1335.
    • (1994) J Biochem , vol.116 , pp. 1330-1335
    • Yamamoto, Y.1    Takimoto, K.2    Izumi, S.3    Toriyama-Sakurai, M.4    Kageyama, T.5    Takahashi, S.Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.