Intracellular released payload influences potency and bystander-killing effects of antibody-drug conjugates in preclinical models

Cancer Research

Volumn 76, Issue 9, 2016, Pages 2710-2719

  Li, Fu ^a   Emmerton, Kim K ^a   Jonas, Mechthild ^a   Zhang, Xinqun ^a   Miyamoto, Jamie B ^a   Setter, Jocelyn R ^a   Nicholas, Nicole D ^a   Okeley, Nicole M ^a   Lyon, Robert P ^a   Benjamin, Dennis R ^a   Law, Che Leung ^a  

^a SEATTLE GENETICS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD30 ANTIGEN; MONOCLONAL ANTIBODY; VEDOTIN; ANTIBODY CONJUGATE; ANTINEOPLASTIC AGENT; OLIGOPEPTIDE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTINEOPLASTIC ACTIVITY; ARTICLE; BYSTANDER EFFECT; CANCER CELL CULTURE; CANCER INHIBITION; CELL VIABILITY; CONTROLLED STUDY; DRUG CONJUGATION; DRUG CYTOTOXICITY; DRUG EFFECT; DRUG POTENCY; IC50; LARGE CELL LYMPHOMA; MOUSE; NONHUMAN; PRIORITY JOURNAL; ANIMAL; DRUG DELIVERY SYSTEM; DRUG SCREENING; FLOW CYTOMETRY; HUMAN; IMMUNOHISTOCHEMISTRY; LIQUID CHROMATOGRAPHY; LYMPHOMA; MASS SPECTROMETRY; PATHOLOGY; PROCEDURES; SCID MOUSE; TUMOR CELL LINE;

ANIMALS; ANTIBODIES, MONOCLONAL; ANTINEOPLASTIC AGENTS; CELL LINE, TUMOR; CHROMATOGRAPHY, LIQUID; DRUG DELIVERY SYSTEMS; FLOW CYTOMETRY; HUMANS; IMMUNOCONJUGATES; IMMUNOHISTOCHEMISTRY; LYMPHOMA; MASS SPECTROMETRY; MICE; MICE, SCID; OLIGOPEPTIDES; XENOGRAFT MODEL ANTITUMOR ASSAYS;

EID: 84969745074     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-15-1795     Document Type: Article

References (33)

1. Mullard A. Maturing antibody-drug conjugate pipeline hits 30. Nat Rev Drug Discov 2013;12:329-32.
2. Younes A, Bartlett NL, Leonard JP, Kennedy DA, Lynch CM, Sievers EL, et al. Brentuximab vedotin (SGN-35) for relapsed CD30-positive lymphomas. N Engl J Med 2010;363:1812-21.
3. Gerber HP, Koehn FE, Abraham RT. The antibody-drug conjugate: an enabling modality for natural product-based cancer therapeutics. Nat Prod Rep 2013;30:625-39.
4. Polson AG, Calemine-Fenaux J, Chan P, Chang W, Christensen E, Clark S, et al. Antibody-drug conjugates for the treatment of non-Hodgkin's lymphoma: target and linker-drug selection. Cancer Res 2009;69: 2358-64.
5. Kung Sutherland MS, Walter RB, Jeffrey SC, Burke PJ, Yu C, Kostner H, et al. SGN-CD33A: A novel CD33-targeting antibody-drug conjugate using a pyrrolobenzodiazepine dimer is active in models of drug-resistant AML. Blood 2013;122:1455-63.
6. Doronina SO,Mendelsohn BA, Bovee TD, Cerveny CG, Alley SC, Meyer DL, et al. Enhanced activity of monomethylauristatin F through monoclonal antibody delivery: effects of linker technology on efficacy and toxicity. Bioconjug Chem 2006;17:114-24.
7. Carter PJ, Senter PD. Antibody-drug conjugates for cancer therapy. Cancer J 2008;14:154-69.
8. Li D, Poon KA, Yu SF, Dere R,GoM, Lau J, et al. DCDT2980S, an anti-CD22-monomethyl auristatin E antibody-drug conjugate, is a potential treatment for non-Hodgkin lymphoma. Mol Cancer Ther 2013;12:1255-65.
9. Polson AG, Williams M, Gray AM, Fuji RN, Poon KA, McBride J, et al. Anti-CD22-MCC-DM1: an antibody-drug conjugate with a stable linker for the treatment of non-Hodgkin's lymphoma. Leukemia 2010;24: 1566-73.
10. Sahin U, Hartmann F, Senter P, Pohl C, Engert A, Diehl V, et al. Specific activation of the prodrug mitomycin phosphate by a bispecific anti-CD30/anti-alkaline phosphatase monoclonal antibody. Cancer Res 1990;50: 6944-8.
11. Kovtun YV, Audette CA, Ye Y, Xie H, Ruberti MF, Phinney SJ, et al. Antibody-drug conjugates designed to eradicate tumors with homogeneous and heterogeneous expression of the target antigen. Cancer Res 2006;66:3214-21.
12. Okeley NM, Miyamoto JB, Zhang X, Sanderson RJ, Benjamin DR, Sievers EL, et al. Intracellular activation of SGN-35, a potent anti-CD30 antibodydrug conjugate. Clin Cancer Res 2010;16:888-97.
13. Breij EC, de Goeij BE, Verploegen S, Schuurhuis DH, Amirkhosravi A, Francis J, et al. An antibody-drug conjugate that targets tissue factor exhibits potent therapeutic activity against a broad range of solid tumors. Cancer Res 2014;74:1214-26.
14. Oflazoglu E, Stone IJ, Gordon K, Wood CG, Repasky EA, Grewal IS, et al. Potent anticarcinoma activity of the humanized anti-CD70 antibody h1F6 conjugated to the tubulin inhibitor auristatin via an uncleavable linker. Clin Cancer Res 2008;14:6171-80.
15. Doronina SO, Toki BE, Torgov MY, Mendelsohn BA, Cerveny CG, Chace DF, et al. Development of potent monoclonal antibody auristatin conjugates for cancer therapy. Nat Biotechnol 2003;21:778-84.
16. Jeffrey SC, Burke PJ, Lyon RP, Meyer DW, Sussman D, AndersonM, et al. A potent anti-CD70 antibody-drug conjugate combining a dimeric pyrrolobenzodiazepine drug with site-specific conjugation technology. Bioconjug Chem 2013;24:1256-63.
17. Jeffrey SC, Andreyka JB, Bernhardt SX, Kissler KM, Kline T, Lenox JS, et al. Development and properties of beta-glucuronide linkers for monoclonal antibody-drug conjugates. Bioconjug Chem 2006;17:831-40.
18. Erickson HK, Park PU, Widdison WC, Kovtun YV, Garrett LM, Hoffman K, et al. Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing. Cancer Res 2006;66:4426-33.
19. Alley SC, Zhang X, Okeley NM, Anderson M, Law CL, Senter PD, et al. The pharmacologic basis for antibody-auristatin conjugate activity. J Pharmacol Exp Ther 2009;330:932-8.
20. Merz H, Lange K, Gaiser T, Muller A, Kapp U, Bittner C, et al. Characterization of a novel human anaplastic large cell lymphoma cell line tumorigenic in SCID mice. Leuk Lymphoma 2002;43:165-72.
21. Hamblett KJ, Senter PD, Chace DF, Sun MM, Lenox J, Cerveny CG, et al. Effects of drug loading on the antitumor activity of a monoclonal antibody drug conjugate. Clin Cancer Res 2004;10:7063-70.
22. Francisco JA, Cerveny CG, Meyer DL, Mixan BJ, Klussman K, Chace DF, et al. cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity. Blood 2003;102:1458-65.
23. Lewis TS, Gordon K, Li F, Weimann A, Bruders R, Miyamoto J, et al. Characterization and circumvention of drug resistance mechanisms in SGN-35-resistant HL and ALCL clonal cell lines. In: Proceedings of the 105th Annual Meeting of the American Association for Cancer Research; 2014 Apr 5-9; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2014;74(19 Suppl):Abstract nr 688.
24. Jacobsen ED, Sharman JP, Oki Y, Advani RH, Winter JN, Bello CM, et al. Brentuximab vedotin demonstrates objective responses in a phase 2 study of relapsed/refractory DLBCL with variable CD30 expression. Blood 2015;125:1394-402.
25. Teicher BA, Chari RV. Antibody conjugate therapeutics: challenges and potential. Clin Cancer Res 2011;17:6389-97.
26. Lyon RP, Setter JR, Bovee TD, Doronina SO, Hunter JH, Anderson ME, et al. Self-hydrolyzing maleimides improve the stability and pharmacological properties of antibody-drug conjugates. Nat Biotechnol 2014;32:1059-62.
27. Lin K, Tibbitts J, Shen BQ. Pharmacokinetics and ADME characterizations of antibody-drug conjugates. Methods Mol Biol 2013;1045:117-31.
28. Sapra P, Betts A, Boni J. Preclinical and clinical pharmacokinetic/pharmacodynamic considerations for antibody-drug conjugates. Expert Rev Clin Pharmacol 2013;6:541-55.
29. Deng C, Pan B, O'Connor OA. Brentuximab vedotin. Clin Cancer Res 2013;19:22-7.
30. Boghaert ER, Khandke K, Sridharan L, Armellino D, Dougher M, Dijoseph JF, et al. Tumoricidal effect of calicheamicin immuno-conjugates using a passive targeting strategy. Int J Oncol 2006;28:675-84.
31. Golfier S, Kopitz C, Kahnert A, Heisler I, Schatz CA, Stelte-Ludwig B, et al. Anetumab ravtansine: A novel mesothelin-targeting antibody-drug conjugate cures tumors with heterogeneous target expression favored by bystander effect. Mol Cancer Ther 2014;13:1537-48.
32. Erickson HK, Lewis Phillips GD, Leipold DD, Provenzano CA, Mai E, Johnson HA, et al. The effect of different linkers on target cell catabolism and pharmacokinetics/pharmacodynamics of trastuzumab maytansinoid conjugates. Mol Cancer Ther 2012;11:1133-42.
33. Olejniczak SH, Stewart CC, Donohue K, Czuczman MS. A quantitative exploration of surface antigen expression in common B-cell malignancies using flow cytometry. Immunol Invest 2006;35:93-114.