메뉴 건너뛰기




Volumn 40, Issue 2, 2011, Pages 130-149

Antitumor activity of glycosylated molluscan hemocyanins via Guerin ascites tumor

Author keywords

GAT; Helix lucorum; Hemocyanin; Rapana venosa

Indexed keywords

HELIX VULGARIS HEMOCYANIN; HEMOCYANIN; IMMUNOLOGICAL ADJUVANT; KEYHOLE LIMPET HEMOCYANIN; RAPANA VENOSA HEMOCYANIN; UNCLASSIFIED DRUG;

EID: 78650960236     PISSN: 08820139     EISSN: 15324311     Source Type: Journal    
DOI: 10.3109/08820139.2010.513408     Document Type: Article
Times cited : (24)

References (49)
  • 2
    • 34447095813 scopus 로고    scopus 로고
    • Oligosaccharide structure of a functional unit RvH1-b of Rapana venosa hemocyanin using HPLC/electrospray ionization mass spectrometry
    • Beck, A., Hillen, N., Dolashki, A., Stevanovic, S., Salvato, B., Voelter, W., Dolashka-Angelova, P. (2007). Oligosaccharide structure of a functional unit RvH1-b of Rapana venosa hemocyanin using HPLC/electrospray ionization mass spectrometry. Biochimie 89(8):938-949.
    • (2007) Biochimie , vol.89 , Issue.8 , pp. 938-949
    • Beck, A.1    Hillen, N.2    Dolashki, A.3    Stevanovic, S.4    Salvato, B.5    Voelter, W.6    Dolashka-Angelova, P.7
  • 4
    • 77957212137 scopus 로고
    • Hemocyanins relationships in their structure, function and assembly
    • Bonaventura, J., Bonaventura, C. (1980). Hemocyanins relationships in their structure, function and assembly. Amer. Zool., 20(1):7-17.
    • (1980) Amer. Zool. , vol.20 , Issue.1 , pp. 7-17
    • Bonaventura, J.1    Bonaventura, C.2
  • 5
    • 0027462384 scopus 로고
    • Selective identification and differentiation of N-and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry
    • Carr, S. A., Huddleston, M. J., Bean, M. F. (1993). Selective identification and differentiation of N-and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry. Protein Sci. 2:183-196.
    • (1993) Protein Sci. , vol.2 , pp. 183-196
    • Carr, S.A.1    Huddleston, M.J.2    Bean, M.F.3
  • 6
    • 77955716770 scopus 로고    scopus 로고
    • Antigenic features of protein carriers commonly used in immunisation trials
    • Chiarella, P., Edelmann, B., Fazio, V. M., Sawyer, A. M., de Marco, A. (2010). Antigenic features of protein carriers commonly used in immunisation trials. Biotechnol. Lett. 32(9):1215-1221.
    • (2010) Biotechnol. Lett. , vol.32 , Issue.9 , pp. 1215-1221
    • Chiarella, P.1    Edelmann, B.2    Fazio, V.M.3    Sawyer, A.M.4    De Marco, A.5
  • 7
    • 0030048724 scopus 로고    scopus 로고
    • Peptide-pulsed dendritic cells induce antigen-specific CTL-mediated protective tumor immunity
    • Celluzzi, C. M., Mayordomo, I. J., Storkus, J. W., Lotze, T. M., Falo, D. L. (1996). Peptide-pulsed dendritic cells induce antigen-specific CTL-mediated protective tumor immunity. J. Exp. Med. 183:283-287.
    • (1996) J. Exp. Med. , vol.183 , pp. 283-287
    • Celluzzi, C.M.1    Mayordomo, I.J.2    Storkus, J.W.3    Lotze, T.M.4    Falo, D.L.5
  • 12
    • 0034102578 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin immunotherapy of bladder cancer: Laboratory and clinical studies
    • Donald, L., Jean, I., Dehaven, R., Riggs, D. (2000). Keyhole limpet hemocyanin immunotherapy of bladder cancer: Laboratory and clinical studies. Eur. Urol. (37):41-44.
    • (2000) Eur. Urol. , Issue.37 , pp. 41-44
    • Donald, L.1    Jean, I.2    Dehaven, R.3    Riggs, D.4
  • 13
    • 1242277875 scopus 로고    scopus 로고
    • Glycosylation sites of hemocyanins of Helix pomatia and Sepia officinalis
    • Gielens, C., De Geest, N., Compernolle, F., Préaux, G. (2004). Glycosylation sites of hemocyanins of Helix pomatia and Sepia officinalis. Micron 35:99-100.
    • (2004) Micron , vol.35 , pp. 99-100
    • Gielens, C.1    De Geest, N.2    Compernolle, F.3    Préaux, G.4
  • 14
    • 0033485264 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH): A biomedical review
    • Harris, J. R., Markl, J. (1999). Keyhole limpet hemocyanin (KLH): A biomedical review. Micron 30(6):597-623.
    • (1999) Micron , vol.30 , Issue.6 , pp. 597-623
    • Harris, J.R.1    Markl, J.2
  • 15
    • 0034064793 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin: Molecular structure of a potent marine immunoactivator
    • Harris, R. J., Markl, J. (2000). Keyhole limpet hemocyanin: Molecular structure of a potent marine immunoactivator. Eur. Urol. 37:24-33.
    • (2000) Eur. Urol. , vol.37 , pp. 24-33
    • Harris, R.J.1    Markl, J.2
  • 16
    • 1242338977 scopus 로고    scopus 로고
    • Small-angle X-ray scattering-based three-dimensional reconstruction of the immunogen KLH1 reveals different oxygen-dependent conformations
    • Hartmann, H., Bongers, A., Decker, H. (2004). Small-angle X-ray scattering-based three-dimensional reconstruction of the immunogen KLH1 reveals different oxygen-dependent conformations. J. Biol. Chem. 279(4):2841-2845.
    • (2004) J. Biol. Chem. , vol.279 , Issue.4 , pp. 2841-2845
    • Hartmann, H.1    Bongers, A.2    Decker, H.3
  • 17
    • 0015254620 scopus 로고
    • Immunochemical and immunogenic properties of a purified keyhold limpet haemocyanin
    • Herscowitz, H. B., Harold, W. W., Stravitzky, B. A. (1972). Immunochemical and immunogenic properties of a purified keyhold limpet haemocyanin. Immunology 22:51-61.
    • (1972) Immunology , vol.22 , pp. 51-61
    • Herscowitz, H.B.1    Harold, W.W.2    Stravitzky, B.A.3
  • 18
    • 70349101617 scopus 로고    scopus 로고
    • Abnormal glycosylation of dystroglycan in human genetic disease. Review
    • Hewitt, J. (2009). Abnormal glycosylation of dystroglycan in human genetic disease. Review. Biochim. Biophys. Acta.
    • (2009) Biochim. Biophys. Acta
    • Hewitt, J.1
  • 19
    • 57749091352 scopus 로고    scopus 로고
    • Maleimide conjugation markedly enhances the immunogenicity of both human and murine idiotype-KLH vaccines
    • Kafi, K., Betting, D. J., Yamada, R. E., Bacica, M., Steward, K. K., Timmerman, J. M. (2009). Maleimide conjugation markedly enhances the immunogenicity of both human and murine idiotype-KLH vaccines. Mol Immunol. 46(3):448-456.
    • (2009) Mol Immunol , vol.46 , Issue.3 , pp. 448-456
    • Kafi, K.1    Betting, D.J.2    Yamada, R.E.3    Bacica, M.4    Steward, K.K.5    Timmerman, J.M.6
  • 20
    • 0031968122 scopus 로고    scopus 로고
    • The immunogenic properties of melanoma-associated antigens recognized by cytotoxic T lymphocytes
    • Kirkin, A., Dzhandzhugazyan, K., Zeuthen, J. (1998). The immunogenic properties of melanoma-associated antigens recognized by cytotoxic T lymphocytes. Exp. Clin. Immunogen. 15(1):19-32.
    • (1998) Exp. Clin. Immunogen. , vol.15 , Issue.1 , pp. 19-32
    • Kirkin, A.1    Dzhandzhugazyan, K.2    Zeuthen, J.3
  • 21
    • 0036439590 scopus 로고    scopus 로고
    • Hemocyanin from the keyhole limpet Megathura crenulata (KLH) carries a novel type of N-glycans with Gal(á1-6)Man-motifs
    • Kurokawa, T., Wuhrer, M., Lochnit, G., Geyer, H., Markl, J., Geyer, R. (2002). Hemocyanin from the keyhole limpet Megathura crenulata (KLH) carries a novel type of N-glycans with Gal(á1-6)Man-motifs. Eur. J. Biochem. 269:5459-5473.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5459-5473
    • Kurokawa, T.1    Wuhrer, M.2    Lochnit, G.3    Geyer, H.4    Markl, J.5    Geyer, R.6
  • 22
    • 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 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0030588577 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis of basic residues (Arg 94, Lys 95, Lys 99) of lipopolysaccharide (LPS)-binding protein on binding and transfer of LPS and subsequent immune cell activation
    • Lamping, N., Hoess, A., Yu, B., Park, T. C., Kirschning, C.J., Pfeil, D., Reuter, D., Wright, S. D., Herrmann, F., Schumann, R. R. (1996). Effects of site-directed mutagenesis of basic residues (Arg 94, Lys 95, Lys 99) of lipopolysaccharide (LPS)-binding protein on binding and transfer of LPS and subsequent immune cell activation. J. Immunol. 157(10):4648-4656.
    • (1996) J. Immunol. , vol.157 , Issue.10 , pp. 4648-4656
    • Lamping, N.1    Hoess, A.2    Yu, B.3    Park, T.C.4    Kirschning, C.J.5    Pfeil, D.6    Reuter, D.7    Wright, S.D.8    Herrmann, F.9    Schumann, R.R.10
  • 24
    • 0030860309 scopus 로고    scopus 로고
    • Primary structure of 21 novel monoantennary and diantennary N-linked carbohydrate chains from a-hemocyanin of Helix pomatia
    • Lommerse, J. P. M., Thomas-Oates, J. E., Gielens, C., Preaux, G., Kamerling, J. P., Vliegenthart, J. F. G. (1997). Primary structure of 21 novel monoantennary and diantennary N-linked carbohydrate chains from a-hemocyanin of Helix pomatia. Eur. J. Biochem. 249:195-222.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 195-222
    • Lommerse, J.P.M.1    Thomas-Oates, J.E.2    Gielens, C.3    Preaux, G.4    Kamerling, J.P.5    Vliegenthart, J.F.G.6
  • 25
    • 0042931206 scopus 로고    scopus 로고
    • Dendritic cells mediate NK cell help for Th1 and CTL responses: Two-signal requirement for the induction of NK cell helper function
    • Mailliard, R., Son, Y., Redlinger, R., Coates, P., Giermasz, A., Morel, P., Storkus, W., Kalinski, P. (2003). Dendritic cells mediate NK cell help for Th1 and CTL responses: Two-signal requirement for the induction of NK cell helper function. J. Immunol. 171:2366-2373.
    • (2003) J. Immunol. , vol.171 , pp. 2366-2373
    • Mailliard, R.1    Son, Y.2    Redlinger, R.3    Coates, P.4    Giermasz, A.5    Morel, P.6    Storkus, W.7    Kalinski, P.8
  • 26
    • 0025009399 scopus 로고
    • Reduced lymphocyte responses to mitogens in natural and experimental trichomoniasis
    • Masson, P. R., Gwanzura, L. (1990). Reduced lymphocyte responses to mitogens in natural and experimental trichomoniasis. Infect. Immun. 58:3553-3557.
    • (1990) Infect. Immun. , vol.58 , pp. 3553-3557
    • Masson, P.R.1    Gwanzura, L.2
  • 27
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele, D., Campbell, K. (2003). Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function. J. Biol. Chem. 278(18):15457-15460.
    • (2003) J. Biol. Chem. , vol.278 , Issue.18 , pp. 15457-15460
    • Michele, D.1    Campbell, K.2
  • 28
    • 33751024089 scopus 로고    scopus 로고
    • Immunotherapeutic effect of concholepas hemocyanin in the murine bladder cancer model: Evidence for conserved antitumor properties among hemocyanins
    • Moltedo, B., Faunes, F., Haussmann, D., De Ioannes, P., De Ioannes, A., Puente, J., Becker, M. (2006). Immunotherapeutic effect of concholepas hemocyanin in the murine bladder cancer model: Evidence for conserved antitumor properties among hemocyanins. J. Urol. 176(6):2690-2695.
    • (2006) J. Urol. , vol.176 , Issue.6 , pp. 2690-2695
    • Moltedo, B.1    Faunes, F.2    Haussmann, D.3    De Ioannes, P.4    De Ioannes, A.5    Puente, J.6    Becker, M.7
  • 29
    • 0030988969 scopus 로고    scopus 로고
    • Polymerization of unprotected synthetic peptides: A view toward synthetic peptide vaccines
    • O'Brien-Simpson, N. M., Ede, N. J., Brown, L. E. (1997). Polymerization of unprotected synthetic peptides: A view toward synthetic peptide vaccines. J. Am. Chem. Soc. 119:1183-1188.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1183-1188
    • O'Brien-Simpson, N.M.1    Ede, N.J.2    Brown, L.E.3
  • 30
    • 77951819743 scopus 로고    scopus 로고
    • Evaluation of human antibody responses to keyhole limpet hemocyanin on a carbohydrate microarray
    • Oyelaran, O., Gildersleeve, J. (2010). Evaluation of human antibody responses to keyhole limpet hemocyanin on a carbohydrate microarray. PROTEOMICS Clin. Appl. 4(3):285-294.
    • (2010) PROTEOMICS Clin. Appl. , vol.4 , Issue.3 , pp. 285-294
    • Oyelaran, O.1    Gildersleeve, J.2
  • 31
    • 0017794782 scopus 로고
    • In vitro and in vivo investigations on antibody-dependent cellular cytotoxicity
    • Pearson, G. R. (1978). In vitro and in vivo investigations on antibody-dependent cellular cytotoxicity. Curr. Topics Microbiol. Immunol. 80:65-96.
    • (1978) Curr. Topics Microbiol. Immunol. , vol.80 , pp. 65-96
    • Pearson, G.R.1
  • 32
    • 0017111687 scopus 로고
    • Specific tumor immunity induced with soluble materials: Purification of antigens inducing tumor resistance
    • Pellis, N. R., Shulan, D. J., Kahan, B. D. (1976). Specific tumor immunity induced with soluble materials: Purification of antigens inducing tumor resistance. Biochem. Biophys. Res. Commun. 71:1251-1258.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 1251-1258
    • Pellis, N.R.1    Shulan, D.J.2    Kahan, B.D.3
  • 33
    • 77449147123 scopus 로고    scopus 로고
    • The T-dependent antibody response to keyhole limpet hemocyanin in rodents
    • Plitnick, L. M., Herzyk, D. J. (2010). The T-dependent antibody response to keyhole limpet hemocyanin in rodents. Meth. Mol Biol. 598:159-171.
    • (2010) Meth. Mol Biol. , vol.598 , pp. 159-171
    • Plitnick, L.M.1    Herzyk, D.J.2
  • 34
    • 0022472020 scopus 로고
    • Heterogeneity among T cells in intracellular free calcium responses after mitogen stimulation with PHA or anti-CD3. Simultaneous use of indo-1 and immunofluorescence with flow cytometry
    • Rabinovitch, P. S., June, C. H., Grossmann, A., Ledbetter, J. A. (1986). Heterogeneity among T cells in intracellular free calcium responses after mitogen stimulation with PHA or anti-CD3. Simultaneous use of indo-1 and immunofluorescence with flow cytometry. J. Immunol. 137(3):952-961.
    • (1986) J. Immunol. , vol.137 , Issue.3 , pp. 952-961
    • Rabinovitch, P.S.1    June, C.H.2    Grossmann, A.3    Ledbetter, J.A.4
  • 35
    • 0002256973 scopus 로고
    • Hemocyanins: Molecular architecture, structure and reactivity of the binuclear copper active site
    • Salvato, B., Beltramini, M. (1990). Hemocyanins: molecular architecture, structure and reactivity of the binuclear copper active site. Life Chem. Rep. 8:1-47.
    • (1990) Life Chem. Rep. , vol.8 , pp. 1-47
    • Salvato, B.1    Beltramini, M.2
  • 36
    • 33846513029 scopus 로고    scopus 로고
    • New insights in Rapana venosa hemocyani N-glycosylation resulting from on-line mass spectrometric analyses
    • Sandra, K., Dolashka-Angelova, P., Devreese, B., Van Beeumen, J. (2007). New insights in Rapana venosa hemocyani N-glycosylation resulting from on-line mass spectrometric analyses. Glycobiology 17(2):141-156.
    • (2007) Glycobiology , vol.17 , Issue.2 , pp. 141-156
    • Sandra, K.1    Dolashka-Angelova, P.2    Devreese, B.3    Van Beeumen, J.4
  • 37
    • 0035418241 scopus 로고    scopus 로고
    • Tumor cell lysate pulsed dendritic cells induce a T-cell response against pancreatic carcinoma cells: An in vitro model for tumor vaccines
    • Schnurr, M., Galambus, P., Scholz, C., Then, F., Dauer, M., Endres, S., Eigler, A. (2001). Tumor cell lysate pulsed dendritic cells induce a T-cell response against pancreatic carcinoma cells: an in vitro model for tumor vaccines. Cancer Res. 61:6445-6450.
    • (2001) Cancer Res. , vol.61 , pp. 6445-6450
    • Schnurr, M.1    Galambus, P.2    Scholz, C.3    Then, F.4    Dauer, M.5    Endres, S.6    Eigler, A.7
  • 38
    • 0035490350 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH) conjugate vaccines as novel therapeutic tools in malignant disorders
    • Schumacher, K. (2001). Keyhole limpet hemocyanin (KLH) conjugate vaccines as novel therapeutic tools in malignant disorders. J. Cancer Res. Clin. Oncol. 127(Suppl. 2): R1-R2.
    • (2001) J. Cancer Res. Clin. Oncol. , vol.127 , Issue.SUPPL. 2
    • Schumacher, K.1
  • 39
    • 0035820352 scopus 로고    scopus 로고
    • Isolation and spectroscopic characterization of the structural subunits of keyhole limpet hemocyanin
    • Schütz, J., Dolashka-Angelova, P., Abrashev, R., Nicolov, P., Voelter, W. (2001). Isolation and spectroscopic characterization of the structural subunits of keyhole limpet hemocyanin. Biochim. Biophys. Acta 1546:325-336.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 325-336
    • Schütz, J.1    Dolashka-Angelova, P.2    Abrashev, R.3    Nicolov, P.4    Voelter, W.5
  • 40
    • 55249091808 scopus 로고    scopus 로고
    • Dendritic cells pulsed with keyhole limpet hemocyanin and cryopreserved maintain anti-tumor activity in a murine melanoma model
    • Teitz-Tennenbaum, S., Li, Q., Davis, M. A., Chang, A. E. (2008). Dendritic cells pulsed with keyhole limpet hemocyanin and cryopreserved maintain anti-tumor activity in a murine melanoma model.Clin. Immunol. 129(3):482-491.
    • (2008) Clin. Immunol. , vol.129 , Issue.3 , pp. 482-491
    • Teitz-Tennenbaum, S.1    Li, Q.2    Davis, M.A.3    Chang, A.E.4
  • 41
    • 0032053156 scopus 로고    scopus 로고
    • Functional adaptations of oxygen-transport proteins
    • Terwilliger, N. B. (1998). Functional adaptations of oxygen-transport proteins. J. Exp. Biol. 201:1085-1098.
    • (1998) J. Exp. Biol. , vol.201 , pp. 1085-1098
    • Terwilliger, N.B.1
  • 42
    • 0034192089 scopus 로고    scopus 로고
    • Linkage of foreign carrier protein to a self-tumor antigen enhances the immunogenicity of a pulsed dendritic cell vaccine
    • Timmerman, J. M., Levy, R. (2000). Linkage of foreign carrier protein to a self-tumor antigen enhances the immunogenicity of a pulsed dendritic cell vaccine. J. Immunol. 164(9):4797-4803.
    • (2000) J. Immunol. , vol.164 , Issue.9 , pp. 4797-4803
    • Timmerman, J.M.1    Levy, R.2
  • 43
    • 0035844294 scopus 로고    scopus 로고
    • Hemocyanins and invertebrate evolution
    • Van Holde K., Miller, K., Decker, H. (2001). Hemocyanins and invertebrate evolution. J. Biol. Chem. 276:15563-15566.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15563-15566
    • Van Holde, K.1    Miller, K.2    Decker, H.3
  • 44
    • 0022378743 scopus 로고
    • Primary structure of the low-molecular-weight carbohydrate chains of Helix pomatia alphahemocyanin. Xylose as a constituent of N-linked oligosaccharides in an animal glycoprotein
    • Van Kuik, J. A., van Halbeek, H., Kamerling, J. P., Vliegenthart, J. F. (1985). Primary structure of the low-molecular-weight carbohydrate chains of Helix pomatia alphahemocyanin. Xylose as a constituent of N-linked oligosaccharides in an animal glycoprotein. J. Biol. Chem. 260(26):13984-13988.
    • (1985) J. Biol. Chem. , vol.260 , Issue.26 , pp. 13984-13988
    • Van Kuik, J.A.1    Van Halbeek, H.2    Kamerling, J.P.3    Vliegenthart, J.F.4
  • 47
    • 0029060612 scopus 로고
    • Keyhole limpet hemocyanin contains Gal(b1-3)-GalNAc determinants that are cross-reactive with the T antigen
    • Wirguin, I., Suturkova, M., Milosevic, L., Briani, C., Latov, N. (1995). Keyhole limpet hemocyanin contains Gal(b1-3)-GalNAc determinants that are cross-reactive with the T antigen. Cancer Immunol. 40:307-310.
    • (1995) Cancer Immunol. , vol.40 , pp. 307-310
    • Wirguin, I.1    Suturkova, M.2    Milosevic, L.3    Briani, C.4    Latov, N.5
  • 48
    • 1642383648 scopus 로고    scopus 로고
    • A novel Gal(b1-4)Gal(b1-4)Fuc(a1-6)-core modification attached to the proximal N-acetylglucosamine of keyhole limpet hemocyanin (KLH) N-glycans
    • Wuhrer, M., Robijn, M. L. M., Koeleman, C. A. M., Balog, C. I. A., Geyer, R., Deelder, A. M., Hokke, C. H. (2004). A novel Gal(b1-4)Gal(b1-4)Fuc(a1-6)- core modification attached to the proximal N-acetylglucosamine of keyhole limpet hemocyanin (KLH) N-glycans. Biochem. J. 378:625-632.
    • (2004) Biochem. J. , vol.378 , pp. 625-632
    • Wuhrer, M.1    Robijn, M.L.M.2    Koeleman, C.A.M.3    Balog, C.I.A.4    Geyer, R.5    Deelder, A.M.6    Hokke, C.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.