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Volumn 85, Issue 10, 2003, Pages 1033-1039

cDNA cloning, identification and characterization of a novel cystatin from the tentacle of Cyanea capillata

Author keywords

Cystatin; Inhibitory activity; Jellyfish; Stability; Tentacle

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; CYSTATIN; CYSTATIN J; HYBRID PROTEIN; PAPAIN; PROTEIN; SERINE; SIGNAL PEPTIDE; THIOREDOXIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0346888726     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(03)00132-9     Document Type: Article
Times cited : (8)

References (26)
  • 1
    • 0028925634 scopus 로고
    • Purification and properties of a cytolytic toxin in venom of the jellyfish Carybdea marsupialis
    • G. Rottini, L. Gusmani, E. Parovel, M. Avian, P. Patriarca, Purification and properties of a cytolytic toxin in venom of the jellyfish Carybdea marsupialis, Toxicon 33 (1995) 315-326.
    • (1995) Toxicon , vol.33 , pp. 315-326
    • Rottini, G.1    Gusmani, L.2    Parovel, E.3    Avian, M.4    Patriarca, P.5
  • 2
    • 0031959933 scopus 로고    scopus 로고
    • Toxicity of sea nettle toxin to human hepatocytes and the protective effects of phosphorylating and alkylating agents
    • C.J. Cao, M.E. Eldefrawi, A.T. Eldefrawi, J.W. Burnett, R.J. Mioduszewski, D.E. Menking, J.J. Valdes, Toxicity of sea nettle toxin to human hepatocytes and the protective effects of phosphorylating and alkylating agents, Toxicon 36 (1998) 269-281.
    • (1998) Toxicon , vol.36 , pp. 269-281
    • Cao, C.J.1    Eldefrawi, M.E.2    Eldefrawi, A.T.3    Burnett, J.W.4    Mioduszewski, R.J.5    Menking, D.E.6    Valdes, J.J.7
  • 3
    • 0036135874 scopus 로고    scopus 로고
    • Apoptosis induced by box jellyfish (Chiropsalmus quadrigatus) toxin in glioma and vascular endothelial cell lines
    • L.K. Sun, Y. Yoshii, A. Hyodo, H. Tsurushima, A. Saito, T. Harakuni, Y.P. Li, M. Nozaki, N. Morine, Apoptosis induced by box jellyfish (Chiropsalmus quadrigatus) toxin in glioma and vascular endothelial cell lines, Toxicon 40 (2002) 441-446.
    • (2002) Toxicon , vol.40 , pp. 441-446
    • Sun, L.K.1    Yoshii, Y.2    Hyodo, A.3    Tsurushima, H.4    Saito, A.5    Harakuni, T.6    Li, Y.P.7    Nozaki, M.8    Morine, N.9
  • 4
    • 0035401326 scopus 로고    scopus 로고
    • Partial purification and characterization of a hemolysin (CAH1) from Hawaiian box jellyfish (Carybdea alata) venom
    • J.J. Chung, L.A. Ratnapala, I.M. Cooke, A.A. Yanagihara, Partial purification and characterization of a hemolysin (CAH1) from Hawaiian box jellyfish (Carybdea alata) venom, Toxicon 39 (2001) 981-990.
    • (2001) Toxicon , vol.39 , pp. 981-990
    • Chung, J.J.1    Ratnapala, L.A.2    Cooke, I.M.3    Yanagihara, A.A.4
  • 6
    • 0023822857 scopus 로고
    • Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae
    • C.J. Grimmelikhuijzen, M. Hahn, K.L. Rinehart, A.N. Spencer, Isolation of pyroGlu-Leu-Leu-Gly-Gly-Arg-Phe-NH2 (Pol-RFamide), a novel neuropeptide from hydromedusae, Brain Res. 475 (1988) 198-203.
    • (1988) Brain Res. , vol.475 , pp. 198-203
    • Grimmelikhuijzen, C.J.1    Hahn, M.2    Rinehart, K.L.3    Spencer, A.N.4
  • 7
    • 0031591656 scopus 로고    scopus 로고
    • Isolation of three novel neuropeptides, the Cyanea-RFamides I-III, from Scyphomedusae
    • A. Moosler, K.L. Rinehart, C.J. Grimmelikhuijzen, Isolation of three novel neuropeptides, the Cyanea-RFamides I-III, from Scyphomedusae, Biochem. Biophys. Res. Commun. 236 (1997) 743-749.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 743-749
    • Moosler, A.1    Rinehart, K.L.2    Grimmelikhuijzen, C.J.3
  • 8
    • 0033039015 scopus 로고    scopus 로고
    • The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C
    • S.L. Olsson, B. Ek, I. Bjork, The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C, Biochim. Biophys. Acta 1432 (1999) 73-81.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 73-81
    • Olsson, S.L.1    Ek, B.2    Bjork, I.3
  • 9
    • 0031674515 scopus 로고    scopus 로고
    • Purification and characterization of two cysteine proteinase inhibitors from the skin of Atlantic salmon (Salmo salar L.)
    • M. Synnes, Purification and characterization of two cysteine proteinase inhibitors from the skin of Atlantic salmon (Salmo salar L.), Comp. Biochem. Physiol. B Biochem. Mol. Biol. 121 (1998) 257-264.
    • (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.121 , pp. 257-264
    • Synnes, M.1
  • 11
    • 0025301658 scopus 로고
    • The refined 2.4 A X-ray cystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • M.T. Stubbs, B. Laber, W. Bode, R. Huber, R. Jerala, B. Lenarcic, V. Turk, The refined 2.4 A X-ray cystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction, EMBO J. 9 (1990) 1939-1947.
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 14
    • 0040020321 scopus 로고    scopus 로고
    • Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    • B. Lenarcic, A. Ritonja, B. Strukelj, B. Turk, V. Turk, Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain, J. Biol. Chem. 272 (1997) 13899-13903.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13899-13903
    • Lenarcic, B.1    Ritonja, A.2    Strukelj, B.3    Turk, B.4    Turk, V.5
  • 15
    • 85030918569 scopus 로고
    • B. Stellmach (Ed.); The People Publishers of China, Beijing
    • B. Stellmach (Ed.), The Mensuration of Enzyme, The People Publishers of China, Beijing, 1988, pp. 243-255.
    • (1988) The Mensuration of Enzyme , pp. 243-255
  • 16
    • 0033834190 scopus 로고    scopus 로고
    • Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants
    • J. Wu, N.F. Haard, Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants, Comp. Biochem. Physiol. C Toxicol. Pharmacol. 127 (2000) 209-220.
    • (2000) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.127 , pp. 209-220
    • Wu, J.1    Haard, N.F.2
  • 17
    • 85030923356 scopus 로고
    • G. Chen, R.Q. Chou (Eds.); The Science and Technology Publishers, Hunan
    • G. Chen, R.Q. Chou (Eds.), Enzymology, The Science and Technology Publishers, Hunan, 1987, pp. 311-350.
    • (1987) Enzymology , pp. 311-350
  • 18
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs
    • M. Kozak, Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs, Nucleic Acids Res. 12 (1984) 857-872.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 857-872
    • Kozak, M.1
  • 19
    • 0017089669 scopus 로고
    • 3′ non-coding region sequences in eukaryotic messenger RNA
    • N.J. Proudfoot, G.G. Brownlee, 3′ non-coding region sequences in eukaryotic messenger RNA, Nature 263 (1976) 211-214.
    • (1976) Nature , vol.263 , pp. 211-214
    • Proudfoot, N.J.1    Brownlee, G.G.2
  • 20
    • 0034032289 scopus 로고    scopus 로고
    • A peptidyl derivative structurally based on the inhibitory center of cystatin C inhibits bone resorption in vitro
    • L. Johansson, A. Grubb, M. Abrahamson, F. Kasprzykowski, R. Kasprzykowska, Z. Grzonka, U.H. Lerner, A peptidyl derivative structurally based on the inhibitory center of cystatin C inhibits bone resorption in vitro, Bone 26 (2000) 451-459.
    • (2000) Bone , vol.26 , pp. 451-459
    • Johansson, L.1    Grubb, A.2    Abrahamson, M.3    Kasprzykowski, F.4    Kasprzykowska, R.5    Grzonka, Z.6    Lerner, U.H.7
  • 21
    • 0031030180 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer
    • G. Sotiropoulou, A. Anisowicz, R. Sager, Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J. Biol. Chem. 272 (1997) 903-910.
    • (1997) J. Biol. Chem. , vol.272 , pp. 903-910
    • Sotiropoulou, G.1    Anisowicz, A.2    Sager, R.3
  • 23
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • W. Bode, R. Engh, D. Musil, U. Thiele, R. Huber, A. Karshikov, J. Brzin, J. Kos, V. Turk, The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases, EMBO J. 7 (1988) 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 24
    • 0030067774 scopus 로고    scopus 로고
    • A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif
    • M. Yamashita, S. Konagaya, A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif, J. Biol. Chem. 271 (1996) 1282-1284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1282-1284
    • Yamashita, M.1    Konagaya, S.2
  • 25
    • 0032810627 scopus 로고    scopus 로고
    • A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens
    • N.N. Ulusu, M.S. Kus, N.L. Acan, E.F. Tezcan, A rapid method for the purification of glucose-6-phosphate dehydrogenase from bovine lens, Int. J. Biochem. Cell Biol. 31 (1999) 787-796.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 787-796
    • Ulusu, N.N.1    Kus, M.S.2    Acan, N.L.3    Tezcan, E.F.4
  • 26
    • 0028968170 scopus 로고
    • Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases
    • A. Hall, K. Hakansson, R.W. Mason, A. Grubb, M. Abrahamson, Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases, J. Biol. Chem. 270 (1995) 5115-5121.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5115-5121
    • Hall, A.1    Hakansson, K.2    Mason, R.W.3    Grubb, A.4    Abrahamson, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.