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Volumn 10, Issue 9, 2011, Pages

Alterations in glycopeptides associated with herceptin treatment of human breast carcinoma MCF-7 and T-lymphoblastoid cells

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; TRASTUZUMAB; ANTINEOPLASTIC AGENT; LIPID; LIPOFECTAMINE; MONOCLONAL ANTIBODY; TRYPSIN;

EID: 80052770403     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.007765     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • DOI 10.1126/science.1059820
    • Bertozzi, C. R., and Kiessling, L. L. (2001) Chemical glycobiology. Science 291, 2357-2364 (Pubitemid 32231790)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 2
    • 0028918745 scopus 로고
    • Tumor-associated sialylated antigens are constitutively expressed in normal human colonic mucosa
    • Ogata, S., Ho, I., Chen, A., Dubois, D., Maklansky, J., Singhal, A., Hakomori, S., and Itzkowitz, S. H. (1995) Tumor-associated sialylated antigens are constitutively expressed in normal human colonic mucosa. Cancer Res. 55, 1869-1874
    • (1995) Cancer Res. , vol.55 , pp. 1869-1874
    • Ogata, S.1    Ho, I.2    Chen, A.3    Dubois, D.4    Maklansky, J.5    Singhal, A.6    Hakomori, S.7    Itzkowitz, S.H.8
  • 3
    • 0034599121 scopus 로고    scopus 로고
    • From the laboratory to the clinic: A retrospective on fully synthetic carbohydrate-based anticancer vaccines
    • DOI 10.1002/(SICI)1521-3773(20000303)39:5<836::AID-ANIE836>3.0. CO;2-I
    • Danishefsky, S. J., and Allen, J. R. (2000) From the laboratory to the clinic: a retrospective on fully synthetic carbohydrate-based anticancer vaccines frequently used abbreviations are listed in the appendix. Angew. Chem. Int. Ed. Engl. 39, 836-863 (Pubitemid 30217267)
    • (2000) Angewandte Chemie - International Edition , vol.39 , Issue.5 , pp. 836-863
    • Danishefsky, S.J.1    Allen, J.R.2
  • 4
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi, A. J. (2000) Protein glucosylation and its role in protein folding. Annu. Rev. Biochem. 69, 69-93
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 5
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • DOI 10.1038/nbt1252, PII NBT1252
    • Walsh, G., and Jefferis, R. (2006) Post-translational modifications in the context of therapeutic proteins. Nat. Biotechnol. 24, 1241-1252 (Pubitemid 44564769)
    • (2006) Nature Biotechnology , vol.24 , Issue.10 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 6
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types
    • DOI 10.1093/glycob/cwl057
    • Kanda, Y., Yamada, T., Mori, K., Okazaki, A., Inoue, M., Kitajima-Miyama, K., Kuni-Kamochi, R., Nakano, R., Yano, K., Kakita, S., Shitara, K., and Satoh, M. (2007) Comparison of biological activity among nonfucosylated therapeutic igg1 antibodies with three different n-linked fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology 17, 104-118 (Pubitemid 44932818)
    • (2007) Glycobiology , vol.17 , Issue.1 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10    Shitara, K.11    Satoh, M.12
  • 7
    • 34247854443 scopus 로고    scopus 로고
    • A nonfucosylated anti-HER2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients
    • DOI 10.1158/1078-0432.CCR-06-1335
    • Suzuki, E., Niwa, R., Saji, S., Muta, M., Hirose, M., Iida, S., Shiotsu, Y., Satoh, M., Shitara, K., Kondo, M., and Toi, M. (2007) A nonfucosylated anti-her2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients. Clin. Cancer Res. 13, 1875-1882 (Pubitemid 46952958)
    • (2007) Clinical Cancer Research , vol.13 , Issue.6 , pp. 1875-1882
    • Suzuki, E.1    Niwa, R.2    Saji, S.3    Muta, M.4    Hirose, M.5    Iida, S.6    Shiotsu, Y.7    Satoh, M.8    Shitara, K.9    Kondo, M.10    Toi, M.11
  • 8
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action
    • Jefferis, R. (2009) Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol. Sci. 30, 356-362
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 356-362
    • Jefferis, R.1
  • 9
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis, R. (2005) Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 21, 11-16
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 10
    • 4644253531 scopus 로고    scopus 로고
    • Profiling analysis of oligosaccharides in antibody pharmaceuticals by capillary electrophoresis
    • DOI 10.1016/j.chroma.2004.08.049, PII S0021967304013998
    • Kamoda, S., Nomura, C., Kinoshita, M., Nishiura, S., Ishikawa, R., Kakehi, K., Kawasaki, N., and Hayakawa, T. (2004) Profiling analysis of oligosaccharides in antibody pharmaceuticals by capillary electrophoresis. J Chromatogr A 1050, 211-216 (Pubitemid 39286246)
    • (2004) Journal of Chromatography A , vol.1050 , Issue.2 , pp. 211-216
    • Kamoda, S.1    Nomura, C.2    Kinoshita, M.3    Nishiura, S.4    Ishikawa, R.5    Kakehi, K.6    Kawasaki, N.7    Hayakawa, T.8
  • 11
    • 60549114878 scopus 로고    scopus 로고
    • Glycosylation of antibody therapeutics: Optimisation for purpose
    • Jefferis, R. (2009) Glycosylation of antibody therapeutics: optimisation for purpose. Methods Mol. Biol. 483, 223-238
    • (2009) Methods Mol. Biol. , vol.483 , pp. 223-238
    • Jefferis, R.1
  • 13
    • 0042835706 scopus 로고    scopus 로고
    • Expression of Her-2/neu on acute lymphoblastic leukemias: Implications for the development of immunotherapeutic approaches
    • Müller, M. R., Grünebach, F., Kayser, K., Vogel, W., Nencioni, A., Brugger, W., Kanz, L., and Brossart, P. (2003) Expression of her-2/neu on acute lymphoblastic leukemias: implications for the development of immunotherapeutic approaches. Clin. Cancer Res. 9, 3448-3453 (Pubitemid 37082743)
    • (2003) Clinical Cancer Research , vol.9 , Issue.9 , pp. 3448-3453
    • Muller, M.R.1    Grunebach, F.2    Kayser, K.3    Vogel, W.4    Nencioni, A.5    Brugger, W.6    Kanz, L.7    Brossart, P.8
  • 15
    • 0346338203 scopus 로고    scopus 로고
    • Combining trastuzumab (herceptin) with hormonal therapy in breast cancer: What can be expected and why?
    • Jones, A. (2003) Combining trastuzumab (herceptin) with hormonal therapy in breast cancer: what can be expected and why?. Ann. Oncol. 14, 1697-1704
    • (2003) Ann. Oncol. , vol.14 , pp. 1697-1704
    • Jones, A.1
  • 19
    • 77949808518 scopus 로고    scopus 로고
    • N-glycomic changes in human breast carcinoma mcf-7 and t-lymphoblastoid cells after treatment with herceptin and herceptin/lipoplex
    • Lattová, E., Tomanek, B., Bartusik, D., and Perreault, H. (2010) N-glycomic changes in human breast carcinoma mcf-7 and t-lymphoblastoid cells after treatment with herceptin and herceptin/lipoplex. J. Proteome Res. 9, 1533-1540
    • (2010) J. Proteome Res. , vol.9 , pp. 1533-1540
    • Lattová, E.1    Tomanek, B.2    Bartusik, D.3    Perreault, H.4
  • 20
    • 0035884155 scopus 로고    scopus 로고
    • Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptide to yield complementary sequence information
    • DOI 10.1021/ac0103470
    • Håkansson, K., Cooper, H. J., Emmett, M. R., Costello, C. E., Marshall, A. G., and Nilsson, C. L. (2001) Electron capture dissociation and infrared multiphoton dissociation ms/ms of an n-glycosylated tryptic peptic to yield complementary sequence information. Anal. Chem. 73, 4530-4536 (Pubitemid 32868256)
    • (2001) Analytical Chemistry , vol.73 , Issue.18 , pp. 4530-4536
    • Hakansson, K.1    Cooper, H.J.2    Emmett, M.R.3    Costello, C.E.4    Marshall, A.G.5    Nilsson, C.L.6
  • 21
    • 33646541985 scopus 로고    scopus 로고
    • Method for investigation of oligosaccharides from glycopeptides: Direct determination of glycosylation sites in proteins
    • DOI 10.1021/ac0519918
    • Lattová, E., Kapková, P., Krokhin, O., and Perreault, H. (2006) Method for investigation of oligosaccharides from glycopeptides: direct determination of glycosylation sites in proteins. Anal. Chem. 78, 2977-2984 (Pubitemid 43726115)
    • (2006) Analytical Chemistry , vol.78 , Issue.9 , pp. 2977-2984
    • Lattova, E.1    Kapkova, P.2    Krokhin, O.3    Perreault, H.4
  • 23
    • 66749092934 scopus 로고    scopus 로고
    • Systematic lc-ms analysis of labile post-translational modifications in complex mixtures
    • Carapito, C., Klemm, C., Aebersold, R., and Domon, B. (2009) Systematic lc-ms analysis of labile post-translational modifications in complex mixtures. J. Proteome Res. 8, 2608-2614
    • (2009) J. Proteome Res. , vol.8 , pp. 2608-2614
    • Carapito, C.1    Klemm, C.2    Aebersold, R.3    Domon, B.4
  • 24
    • 44449098820 scopus 로고    scopus 로고
    • A two-dimensional array for simultaneous sequencing of n- And o-glycans and their glycoforms on specific glycosylation sites
    • Tzur, Y., Markovich, A., and Lichtenstein, R. G. (2008) A two-dimensional array for simultaneous sequencing of n- and o-glycans and their glycoforms on specific glycosylation sites. J. Proteome Res. 7, 1188-1198
    • (2008) J. Proteome Res. , vol.7 , pp. 1188-1198
    • Tzur, Y.1    Markovich, A.2    Lichtenstein, R.G.3
  • 25
    • 66149102040 scopus 로고    scopus 로고
    • Characterization of n-linked glycosylation on recombinant glycoproteins produced in pichia pastoris using esi-ms and maldi-tof
    • Gong, B., Cukan, M., Fisher, R., Li, H., Stadheim, T. A., and Gerngross, T. (2009) Characterization of n-linked glycosylation on recombinant glycoproteins produced in pichia pastoris using esi-ms and maldi-tof. Methods Mol. Biol. 534, 213-223
    • (2009) Methods Mol. Biol. , vol.534 , pp. 213-223
    • Gong, B.1    Cukan, M.2    Fisher, R.3    Li, H.4    Stadheim, T.A.5    Gerngross, T.6
  • 26
    • 61849103543 scopus 로고    scopus 로고
    • Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics
    • Dodds, E. D., Seipert, R. R., Clowers, B. H., German, J. B., and Lebrilla, C. B. (2009) Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics. J. Proteome Res. 8, 502-512
    • (2009) J. Proteome Res. , vol.8 , pp. 502-512
    • Dodds, E.D.1    Seipert, R.R.2    Clowers, B.H.3    German, J.B.4    Lebrilla, C.B.5
  • 27
    • 77950631561 scopus 로고    scopus 로고
    • Mass spectrometric identification of aberrantly glycosylated human apolipoprotein c-iii peptides in urine from schistosoma mansoni-infected individuals
    • Balog, C. I., Mayboroda, O. A., Wuhrer, M., Hokke, C. H., Deelder, A. M., and Hensbergen, P. J. (2010) Mass spectrometric identification of aberrantly glycosylated human apolipoprotein c-iii peptides in urine from schistosoma mansoni-infected individuals. Mol. Cell Proteomics 9, 667-681
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 667-681
    • Balog, C.I.1    Mayboroda, O.A.2    Wuhrer, M.3    Hokke, C.H.4    Deelder, A.M.5    Hensbergen, P.J.6
  • 28
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by cid, higher energy collisional dissociation, and electron transfer dissociation ms applied to the nlinked glycoproteome of campylobacter jejuni
    • Scott, N. E., Parker, B. L., Connolly, A. M., Paulech, J., Edwards, A. V. G., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S. P., Højrup, P., Packer, N. H., Larsen, M. R., and Cordwell, S. J. (2011) Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by cid, higher energy collisional dissociation, and electron transfer dissociation ms applied to the nlinked glycoproteome of campylobacter jejuni. Mol. Cell Proteomics 10, M000031MCP201
    • (2011) Mol. Cell Proteomics , vol.10
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.G.5    Crossett, B.6    Falconer, L.7    Kolarich, D.8    Djordjevic, S.P.9    Højrup, P.10    Packer, N.H.11    Larsen, M.R.12    Cordwell, S.J.13
  • 29
    • 70349336682 scopus 로고    scopus 로고
    • Combined treatment of human mcf-7 breast carcinoma with antibody, cationic lipid and hyaluronic acid using ex vivo assays
    • Bartusik, D., Tomanek, B., Lattová, E., Perreault, H., and Fallone, G. (2010) Combined treatment of human mcf-7 breast carcinoma with antibody, cationic lipid and hyaluronic acid using ex vivo assays. J Pharm Biomed Anal 51, 192-201
    • (2010) J Pharm Biomed Anal , vol.51 , pp. 192-201
    • Bartusik, D.1    Tomanek, B.2    Lattová, E.3    Perreault, H.4    Fallone, G.5
  • 30
    • 77954309626 scopus 로고    scopus 로고
    • Ex vivo assays of cem cells cultured and treated in the three dimensional cultures
    • Bartusik, D., Tomanek, B., Lattová, E., Perreault, H., and Fallone, G. (2010) Ex vivo assays of cem cells cultured and treated in the three dimensional cultures. Biomed. Pharmacother. 64, 390-395
    • (2010) Biomed. Pharmacother. , vol.64 , pp. 390-395
    • Bartusik, D.1    Tomanek, B.2    Lattová, E.3    Perreault, H.4    Fallone, G.5
  • 31
    • 0032928189 scopus 로고    scopus 로고
    • Determination of optimal freezing parameters of human prostate cancer in a nude mouse model
    • DOI 10.1002/(SICI)1097-0045(19990201)38:2<137::AID-PROS7>3.0.CO;2-5
    • Turk, T. M., Rees, M. A., Pietrow, P., Myers, C. E., Mills, S. E., and Gillenwater, J. Y. (1999) Determination of optimal freezing parameters of human prostate cancer in a nude mouse model. Prostate 38, 137-143 (Pubitemid 29052952)
    • (1999) Prostate , vol.38 , Issue.2 , pp. 137-143
    • Turk, T.M.T.1    Rees, M.A.2    Pietrow, P.3    Myers, C.E.4    Mills, S.E.5    Gillenwater, J.Y.6
  • 33
    • 0034124238 scopus 로고    scopus 로고
    • A tandem quadrupole/time-of-flight mass spectrometer with a matrix- assisted laser desorption/ionization source: Design and performance
    • DOI 10.1002/1097-0231(20000630)14:12<1047::AID-RCM990>3.0.CO;2-E
    • Loboda, A. V., Krutchinsky, A. N., Bromirski, M., Ens, W., and Standing, K. G. (2000) A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance. Rapid Commun. Mass Spectrom. 14, 1047-1057 (Pubitemid 30409412)
    • (2000) Rapid Communications in Mass Spectrometry , vol.14 , Issue.12 , pp. 1047-1057
    • Loboda, A.V.1    Krutchinsky, A.N.2    Bromirski, M.3    Ens, W.4    Standing, K.G.5
  • 34
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff, P., and Fohlman, J. (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11, 601
    • (1984) Biomed. Mass Spectrom. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 35
    • 34249729414 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization on-target method for the investigation of oligosaccharides and glycosylation sites in glycopeptides and glycoproteins
    • DOI 10.1002/rcm.3007
    • Lattová, E., Chen, V. C., Varma, S., Bezabeh, T., and Perreault, H. (2007) Matrix-assisted laser desorption/ionization on-target method for the investigation of oligosaccharides and glycosylation sites in glycopeptides and glycoproteins. Rapid Commun. Mass Spectrom. 21, 1644-1650 (Pubitemid 46827113)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.10 , pp. 1644-1650
    • Lattova, E.1    Chen, V.C.2    Varma, S.3    Bezabeh, T.4    Perreault, H.5
  • 36
    • 2342585497 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization tandem mass spectrometry and post-source decay fragmentation study of phenylhydrazones of N-linked oligosaccharides from ovalbumin
    • DOI 10.1016/j.jasms.2004.01.012, PII S1044030504000911
    • Lattova, E., Perreault, H., and Krokhin, O. (2004) Matrix-assisted laser desorption/ionization tandem mass spectrometry and post-source decay fragmentation study of phenylhydrazones of n-linked oligosaccharides from ovalbumin. J. Am. Soc. Mass Spectrom. 15, 725-735 (Pubitemid 38581099)
    • (2004) Journal of the American Society for Mass Spectrometry , vol.15 , Issue.5 , pp. 725-735
    • Lattova, E.1    Perreault, H.2    Krokhin, O.3
  • 37
    • 70349762761 scopus 로고    scopus 로고
    • Electrospray ionization quadrupole ion-mobility time-of-flight mass spectrometry as a tool to distinguish the lot-to-lot heterogeneity in n-glycosylation profile of the therapeutic monoclonal antibody trastuzumab
    • Damen, C. W., Chen, W., Chakraborty, A. B., Van Oosterhout, M., Mazzeo, J. R., Gebler, J. C., Schellens, J. H., Rosing, H., and Beijnen, J. H. (2009) Electrospray ionization quadrupole ion-mobility time-of-flight mass spectrometry as a tool to distinguish the lot-to-lot heterogeneity in n-glycosylation profile of the therapeutic monoclonal antibody trastuzumab. J. Am. Soc. Mass Spectrom. 20, 2021-2033
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 2021-2033
    • Damen, C.W.1    Chen, W.2    Chakraborty, A.B.3    Van Oosterhout, M.4    Mazzeo, J.R.5    Gebler, J.C.6    Schellens, J.H.7    Rosing, H.8    Beijnen, J.H.9
  • 38
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by lc-esi-ms of glycopeptides and oligosaccharides
    • Stadlmann, J., Pabst, M., Kolarich, D., Kunert, R., and Altmann, F. (2008) Analysis of immunoglobulin glycosylation by lc-esi-ms of glycopeptides and oligosaccharides. Proteomics 8, 2858-2871
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 40
    • 34447296997 scopus 로고    scopus 로고
    • Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys
    • DOI 10.1093/glycob/cwm017
    • Jones, A. J., Papac, D. I., Chin, E. H., Keck, R., Baughman, S. A., Lin, Y. S., Kneer, J., and Battersby, J. E. (2007) Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal n-acetylglucosamine is similar in humans and cynomolgus monkeys. Glycobiology 17, 529-540 (Pubitemid 47049940)
    • (2007) Glycobiology , vol.17 , Issue.5 , pp. 529-540
    • Jones, A.J.S.1    Papac, D.I.2    Chin, E.H.3    Keck, R.4    Baughman, S.A.5    Lin, Y.S.6    Kneer, J.7    Battersby, J.E.8


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