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Volumn 13, Issue 2, 2014, Pages 375-385

Increasing the antitumor effect of an EpCAM-targeting fusion toxin by facile click PEgylation

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BACTERIAL TOXIN; CELL ADHESION MOLECULE; EPCAM PROTEIN, HUMAN; EXOTOXIN; HYBRID PROTEIN; MACROGOL DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; TOXA PROTEIN, PSEUDOMONAS AERUGINOSA; TUMOR ANTIGEN; VIRULENCE FACTOR;

EID: 84894219315     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-13-0523     Document Type: Article
Times cited : (35)

References (51)
  • 2
    • 84858416256 scopus 로고    scopus 로고
    • Antibody-based immunotherapy of cancer
    • Weiner LM, Murray JC, Shuptrine CW. Antibody-based immunotherapy of cancer. Cell 2012;148:1081-4
    • (2012) Cell , vol.148 , pp. 1081-1084
    • Weiner, L.M.1    Murray, J.C.2    Shuptrine, C.W.3
  • 4
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz HK, Amstutz P, Pleuckthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 2005;23:1257-68
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pleuckthun, A.3
  • 5
    • 80054856259 scopus 로고    scopus 로고
    • DARPins and other repeat protein scaffolds: Advances in engineering and applications
    • Boersma YL, Pleuckthun A. DARPins and other repeat protein scaffolds: advances in engineering and applications. Curr Opin Biotechnol 2011;22:849-57
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 849-857
    • Boersma, Y.L.1    Pleuckthun, A.2
  • 6
    • 80054098573 scopus 로고    scopus 로고
    • Antibody conjugate therapeutics: Challenges and potential
    • Teicher BA, Chari RV. Antibody conjugate therapeutics: challenges and potential. Clin Cancer Res 2011;17:6389-97
    • (2011) Clin Cancer Res , vol.17 , pp. 6389-6397
    • Teicher, B.A.1    Chari, R.V.2
  • 7
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz HK, Stumpp MT, Forrer P, Amstutz P, Pleuckthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J Mol Biol 2003;332:489-503
    • (2003) J Mol Biol , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Pleuckthun, A.5
  • 9
    • 84855591894 scopus 로고    scopus 로고
    • Facile double-functionalization of designed ankyrin repeat proteins using click and thiol chemistries
    • Simon M, Zangemeister-Wittke U, Pleuckthun A. Facile double- functionalization of designed ankyrin repeat proteins using click and thiol chemistries. Bioconj Chem 2012;23:279-86
    • (2012) Bioconj Chem , vol.23 , pp. 279-286
    • Simon, M.1    Zangemeister-Wittke, U.2    Pleuckthun, A.3
  • 10
    • 84888605787 scopus 로고    scopus 로고
    • Orthogonal Assembly of a Designed Ankyrin Repeat Protein-cytotoxin conjugate with a clickable serum albumin module for half-life extension
    • Simon M, Frey R, Zangemeister-Wittke U, Pleuckthun A. Orthogonal Assembly of a Designed Ankyrin Repeat Protein-cytotoxin conjugate with a clickable serum albumin module for half-life extension. Bioconjug Chem 2013;24:1955-66
    • (2013) Bioconjug Chem , vol.24 , pp. 1955-66
    • Simon, M.1    Frey, R.2    Zangemeister-Wittke, U.3    Pleuckthun, A.4
  • 11
    • 51349091340 scopus 로고    scopus 로고
    • Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display
    • Steiner D, Forrer P, Pleuckthun A. Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display. J Mol Biol 2008;382:1211-27
    • (2008) J Mol Biol , vol.382 , pp. 1211-1227
    • Steiner, D.1    Forrer, P.2    Pleuckthun, A.3
  • 12
    • 33845939857 scopus 로고    scopus 로고
    • Selection and characterization of Her2-binding designed ankyrin repeat proteins
    • Zahnd C, Pecorari F, Straumann N, Wyler E, Pleuckthun A. Selection and characterization of Her2-binding designed ankyrin repeat proteins. J Biol Chem 2006;281:35167-75
    • (2006) J Biol Chem , vol.281 , pp. 35167-35175
    • Zahnd, C.1    Pecorari, F.2    Straumann, N.3    Wyler, E.4    Pleuckthun, A.5
  • 13
    • 80054870896 scopus 로고    scopus 로고
    • DARPins recognizing the tumorassociated antigen EpCAM selected by phage and ribosome display and engineered for multivalency
    • Stefan N, Martin-Killias P, Wyss-Stoeckle S, Honegger A, Zangemeister-Wittke U, Pleuckthun A. DARPins recognizing the tumorassociated antigen EpCAM selected by phage and ribosome display and engineered for multivalency. J Mol Biol 2011;413: 826-43
    • (2011) J Mol Biol , vol.413 , pp. 826-843
    • Stefan, N.1    Martin-Killias, P.2    Wyss-Stoeckle, S.3    Honegger, A.4    Zangemeister-Wittke, U.5    Pleuckthun, A.6
  • 16
    • 33846804010 scopus 로고    scopus 로고
    • EpCAM (CD326) finding its role in cancer
    • Baeuerle PA, Gires O. EpCAM (CD326) finding its role in cancer. Br J Cancer 2007;96:417-23
    • (2007) Br J Cancer , vol.96 , pp. 417-423
    • Baeuerle, P.A.1    Gires, O.2
  • 18
    • 6044259206 scopus 로고    scopus 로고
    • Tumor cells circulate in the peripheral blood of all major carcinomas but not in healthy subjects or patients with nonmalignant diseases
    • Allard WJ, Matera J, Miller MC, Repollet M, Connelly MC, Rao C, et al. Tumor cells circulate in the peripheral blood of all major carcinomas but not in healthy subjects or patients with nonmalignant diseases. Clin Cancer Res 2004;10:6897-904
    • (2004) Clin Cancer Res , vol.10 , pp. 6897-6904
    • Allard, W.J.1    Matera, J.2    Miller, M.C.3    Repollet, M.4    Connelly, M.C.5    Rao, C.6
  • 19
    • 42649100970 scopus 로고    scopus 로고
    • Detection, clinical relevance and specific biological properties of disseminating tumour cells
    • Pantel K, Brakenhoff RH, Brandt B. Detection, clinical relevance and specific biological properties of disseminating tumour cells. Nat Rev Cancer 2008;8:329-40
    • (2008) Nat Rev Cancer , vol.8 , pp. 329-340
    • Pantel, K.1    Brakenhoff, R.H.2    Brandt, B.3
  • 20
    • 33748956628 scopus 로고    scopus 로고
    • A phase i study with adecatumumab, a human antibody directed against epithelial cell adhesion molecule, in hormone refractory prostate cancer patients
    • Oberneder R, Weckermann D, Ebner B, Quadt C, Kirchinger P, RaumT, et al. A phase I study with adecatumumab, a human antibody directed against epithelial cell adhesion molecule, in hormone refractory prostate cancer patients. Eur J Cancer 2006;42:2530-8
    • (2006) Eur J Cancer , vol.42 , pp. 2530-2538
    • Oberneder, R.1    Weckermann, D.2    Ebner, B.3    Quadt, C.4    Raumt, K.P.5
  • 21
    • 78650991636 scopus 로고    scopus 로고
    • Phase II study of the human anti-epithelial cell adhesion molecule antibody adecatumumab in prostate cancer patients with increasing serum levels of prostate-specific antigen after radical prostatectomy
    • Marschner N, Ruettinger D, Zugmaier G, Nemere G, Lehmann J, Obrist P, et al. Phase II study of the human anti-epithelial cell adhesion molecule antibody adecatumumab in prostate cancer patients with increasing serum levels of prostate-specific antigen after radical prostatectomy. Urol Int 2010;85:386-95
    • (2010) Urol Int , vol.85 , pp. 386-395
    • Marschner, N.1    Ruettinger, D.2    Zugmaier, G.3    Nemere, G.4    Lehmann, J.5    Obrist, P.6
  • 22
    • 84860142832 scopus 로고    scopus 로고
    • Therapeutic potential of amanitin-conjugated anti-epithelial cell adhesion molecule monoclonal antibody against pancreatic carcinoma
    • Moldenhauer G, Salnikov AV, Leuttgau S, Herr I, Anderl J, Faulstich H. Therapeutic potential of amanitin-conjugated anti-epithelial cell adhesion molecule monoclonal antibody against pancreatic carcinoma. J Natl Cancer Inst 2012;104:622-34
    • (2012) J Natl Cancer Inst , vol.104 , pp. 622-634
    • Moldenhauer, G.1    Salnikov, A.V.2    Leuttgau, S.3    Herr, I.4    Anderl, J.5    Faulstich, H.6
  • 23
    • 0037478897 scopus 로고    scopus 로고
    • A recombinant immunotoxin derived from a humanized epithelial cell adhesion molecule-specific single-chain antibody fragment has potent and selective antitumor activity
    • Di Paolo C, Willuda J, Kubetzko S, Schubiger A, Stahel R, Zangemeister-Wittke U, et al. A recombinant immunotoxin derived from a humanized epithelial cell adhesion molecule-specific single-chain antibody fragment has potent and selective antitumor activity. Clin Cancer Res 2003;9:2837-48
    • (2003) Clin Cancer Res , vol.9 , pp. 2837-2848
    • Di Paolo, C.1    Willuda, J.2    Kubetzko, S.3    Schubiger, A.4    Stahel, R.5    Zangemeister-Wittke, U.6
  • 24
    • 70349512496 scopus 로고    scopus 로고
    • EpCAM-targeted delivery of nanocomplexed siRNA to tumor cells with designed ankyrin repeat proteins
    • Winkler J, Martin-Killias P, Pleuckthun A, Zangemeister-Wittke U. EpCAM-targeted delivery of nanocomplexed siRNA to tumor cells with designed ankyrin repeat proteins. Mol Cancer Ther 2009;8:2674-83
    • (2009) Mol Cancer Ther , vol.8 , pp. 2674-2683
    • Winkler, J.1    Martin-Killias, P.2    Pleuckthun, A.3    Zangemeister-Wittke, U.4
  • 25
    • 78751503899 scopus 로고    scopus 로고
    • A novel fusion toxin derived from an EpCAM-specific designed ankyrin repeat protein has potent antitumor activity
    • Martin-Killias P, Stefan N, Rothschild S, Pleuckthun A, Zangemeister-Wittke U. A novel fusion toxin derived from an EpCAM-specific designed ankyrin repeat protein has potent antitumor activity. Clin Cancer Res 2011;17:100-10
    • (2011) Clin Cancer Res , vol.17 , pp. 100-110
    • Martin-Killias, P.1    Stefan, N.2    Rothschild, S.3    Pleuckthun, A.4    Zangemeister-Wittke, U.5
  • 27
    • 81555214408 scopus 로고    scopus 로고
    • A guide to taming a toxin -Recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer
    • Weldon JE, Pastan I. A guide to taming a toxin -recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer. FEBS 2011;278:4683-700
    • (2011) FEBS , vol.278 , pp. 4683-4700
    • Weldon, J.E.1    Pastan, I.2
  • 28
    • 0038290547 scopus 로고    scopus 로고
    • Immunotoxins containing Pseudomonas exotoxin A: A short history
    • Pastan I. Immunotoxins containing Pseudomonas exotoxin A: a short history. Cancer Immunol Immunother 2003;52:338-41
    • (2003) Cancer Immunol Immunother , vol.52 , pp. 338-341
    • Pastan, I.1
  • 29
    • 80054037204 scopus 로고    scopus 로고
    • Treatment of hematologic malignancies with immunotoxins and antibody-drug conjugates
    • FitzGerald DJ, Wayne AS, Kreitman RJ, Pastan I. Treatment of hematologic malignancies with immunotoxins and antibody-drug conjugates. Cancer Res 2011;71:6300-9
    • (2011) Cancer Res , vol.71 , pp. 6300-6309
    • Fitzgerald, D.J.1    Wayne, A.S.2    Kreitman, R.J.3    Pastan, I.4
  • 31
    • 0034682480 scopus 로고    scopus 로고
    • Sitespecific chemical modification with polyethylene glycol of recombinant immunotoxin anti-Tac(Fv)-PE38 (LMB-2) improves antitumor activity and reduces animal toxicity and immunogenicity
    • Tsutsumi Y, Onda M, Nagata S, Lee B, Kreitman RJ, Pastan I. Sitespecific chemical modification with polyethylene glycol of recombinant immunotoxin anti-Tac(Fv)-PE38 (LMB-2) improves antitumor activity and reduces animal toxicity and immunogenicity. Proc Natl Acad Sci U S A 2000;97:8548-53
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8548-8553
    • Tsutsumi, Y.1    Onda, M.2    Nagata, S.3    Lee, B.4    Kreitman, R.J.5    Pastan, I.6
  • 32
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese FM, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov Today 2005;10:1451-8
    • (2005) Drug Discov Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 33
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates
    • Caliceti P, Veronese F. Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates. Adv Drug Del Rev 2003; 55:1261-77
    • (2003) Adv Drug Del Rev , vol.55 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.2
  • 34
    • 80051753313 scopus 로고    scopus 로고
    • FDA-Approved poly(ethylene glycol)-protein conjugate drugs
    • Alconcel SNS, Baas AS, Maynard HD. FDA-Approved poly(ethylene glycol)-protein conjugate drugs. Polym Chem 2011;2:1442-8
    • (2011) Polym Chem , vol.2 , pp. 1442-1448
    • Sns, A.1    Baas, A.S.2    Maynard, H.D.3
  • 35
    • 0026536995 scopus 로고
    • Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kurfeurst MM. Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem 1992;200: 244-8
    • (1992) Anal Biochem , vol.200 , pp. 244-248
    • Kurfeurst, M.M.1
  • 36
    • 10744227326 scopus 로고    scopus 로고
    • Tailoring structure-function and pharmacokinetic properties of single-chain Fv proteins by site-specific PEGylation
    • Yang K, Basu A, Wang M, Chintala R, Hsieh M-C, Liu S, et al. Tailoring structure-function and pharmacokinetic properties of single-chain Fv proteins by site-specific PEGylation. Protein Eng 2003; 16:761-70
    • (2003) Protein Eng , vol.16 , pp. 761-770
    • Yang, K.1    Basu, A.2    Wang, M.3    Chintala, R.4    Hsieh, M.-C.5    Liu, S.6
  • 37
    • 27544496736 scopus 로고    scopus 로고
    • Protein PEGylation decreases observed target association rates via a dual blocking mechanism
    • Kubetzko S, Sarkar CA, Pleuckthun A. Protein PEGylation decreases observed target association rates via a dual blocking mechanism. Mol Pharmacol 2005;68:1439-54
    • (2005) Mol Pharmacol , vol.68 , pp. 1439-1454
    • Kubetzko, S.1    Sarkar, C.A.2    Pleuckthun, A.3
  • 38
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • Veronese FM. Peptide and protein PEGylation: a review of problems and solutions. Biomaterials 2001;22:405-17
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 39
    • 0034000453 scopus 로고    scopus 로고
    • Tumor vascular permeability and the EPR effect in macromolecular therapeutics: A review
    • Maeda H, Wu J, Sawa T, Matsumura Y, Hori K. Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review. J Controlled Release 2000;65:271-84
    • (2000) J Controlled Release , vol.65 , pp. 271-284
    • Maeda, H.1    Wu, J.2    Sawa, T.3    Matsumura, Y.4    Hori, K.5
  • 40
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris JM, Chess RB. Effect of PEGylation on pharmaceuticals. Nat Rev Drug Discov 2003;2:214-21
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 42
    • 34347325240 scopus 로고    scopus 로고
    • Releasable PEGylation of mesothelin targeted immunotoxin SS1P achieves single dosage complete regression of a human carcinoma in mice
    • Filpula D, Yang K, Basu A, Hassan R, Xiang L, Zhang Z, et al. Releasable PEGylation of mesothelin targeted immunotoxin SS1P achieves single dosage complete regression of a human carcinoma in mice. Bioconj Chem 2007;18:773-84
    • (2007) Bioconj Chem , vol.18 , pp. 773-784
    • Filpula, D.1    Yang, K.2    Basu, A.3    Hassan, R.4    Xiang, L.5    Zhang, Z.6
  • 43
    • 84863012529 scopus 로고    scopus 로고
    • Conjugation site modulates the in vivo stability and therapeutic activity of antibodydrug conjugates
    • Shen B-Q, Xu K, Liu L, Raab H, Bhakta S, Kenrick M, et al. Conjugation site modulates the in vivo stability and therapeutic activity of antibodydrug conjugates. Nat Biotechnol 2012;30:184-9
    • (2012) Nat Biotechnol , vol.30 , pp. 184-189
    • Shen, B.-Q.1    Xu, K.2    Liu, L.3    Raab, H.4    Bhakta, S.5    Kenrick, M.6
  • 44
    • 0037343846 scopus 로고    scopus 로고
    • Mutants of immunotoxin anti-Tac (dsFv)-PE38 with variable number of lysine residues as candidates for site-specific chemical modification
    • Onda M, Vincent JJ, Lee B, Pastan I. Mutants of immunotoxin anti-Tac (dsFv)-PE38 with variable number of lysine residues as candidates for site-specific chemical modification. Bioconj Chem 2003;14: 480-7
    • (2003) Bioconj Chem , vol.14 , pp. 480-487
    • Onda, M.1    Vincent, J.J.2    Lee, B.3    Pastan, I.4
  • 45
    • 77949762340 scopus 로고    scopus 로고
    • Targeting of drugs and nanoparticles to tumors
    • Ruoslahti E, Bhatia SN, Sailor MJ. Targeting of drugs and nanoparticles to tumors. J Cell Biol 2010;188:759-68
    • (2010) J Cell Biol , vol.188 , pp. 759-768
    • Ruoslahti, E.1    Bhatia, S.N.2    Sailor, M.J.3
  • 46
    • 82755197856 scopus 로고    scopus 로고
    • Strategies for extended serum half-life of protein therapeutics
    • Kontermann RE. Strategies for extended serum half-life of protein therapeutics. Curr Opin Biotechnol 2011;22:868-76
    • (2011) Curr Opin Biotechnol , vol.22 , pp. 868-876
    • Kontermann, R.E.1
  • 47
    • 79953012996 scopus 로고    scopus 로고
    • Convergent potency of internalized gelonin immunotoxins across varied cell lines, antigens, and targeting moieties
    • PirieCM, Hackel BJ, Rosenblum MG, Wittrup KD.Convergent potency of internalized gelonin immunotoxins across varied cell lines, antigens, and targeting moieties. J Biol Chem 2011;286:4165-72
    • (2011) J Biol Chem , vol.286 , pp. 4165-4172
    • Piriecm Hackel, B.J.1    Rosenblum, M.G.2    Wittrup, K.D.3
  • 48
    • 36549039553 scopus 로고    scopus 로고
    • Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase
    • Fontana A, Spolaore B, Mero A, Veronese FM. Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase. Adv Drug Del Rev 2008;60:13-28
    • (2008) Adv Drug Del Rev , vol.60 , pp. 13-28
    • Fontana, A.1    Spolaore, B.2    Mero, A.3    Veronese, F.M.4
  • 49
    • 0036083609 scopus 로고    scopus 로고
    • PEGylation: Engineering improved pharmaceuticals for enhanced therapy
    • Molineux G. PEGylation: engineering improved pharmaceuticals for enhanced therapy. Cancer Treat Rev 2002;28:13-6
    • (2002) Cancer Treat Rev , vol.28 , pp. 13-16
    • Molineux, G.1
  • 50
    • 60849116672 scopus 로고    scopus 로고
    • Pseudomonas exotoxin A: From virulence factor to anti-cancer agent
    • Wolf P, Elseasser-Beile U. Pseudomonas exotoxin A: from virulence factor to anti-cancer agent. Int J Med Microbiol 2009;299:161-76
    • (2009) Int J Med Microbiol , vol.299 , pp. 161-176
    • Wolf, P.1    Elseasser-Beile, U.2
  • 51
    • 77956322010 scopus 로고    scopus 로고
    • Proteolysis of Pseudomonas exotoxin A within hepatic endosomes by cathepsins B and D produces fragments displaying in vitro ADPribosylating and apoptotic effects
    • Hage El T, Lorin S, Decottignies P, Djavaheri-Mergny M, Authier F. Proteolysis of Pseudomonas exotoxin A within hepatic endosomes by cathepsins B and D produces fragments displaying in vitro ADPribosylating and apoptotic effects. FEBS J 2010;277:3735-49.
    • (2010) FEBS J , vol.277 , pp. 3735-3749
    • Hage El, T.1    Lorin, S.2    Decottignies, P.3    Djavaheri-Mergny, M.4    Authier, F.5


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