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Cantuzumab Mertansine, a Maytansinoid Immunoconjugate Directed to the CanAg Antigen: A Phase I, Pharmacokinetic, and Biologic Correlative Study
Abstract
Purpose: To determine the maximum tolerated dose and pharmacokinetics of cantuzumab mertansine, an immunoconjugate of the potent maytansine derivative (DM1) and the humanized monoclonal antibody (huC242) directed to CanAg, intravenously (IV) once every 3 weeks and to seek evidence of antitumor activity. Patients and Methods: Patients with CanAg-expressing solid malignancies were treated with escalating doses of cantuzumab mertansine administered IV every 3 weeks. The pharmacokinetic parameters of cantuzumab mertansine, the presence of plasma-shed CanAg, and the development of both human antihuman and human anti-DM1 conjugate antibodies also were characterized. Results: Thirty-seven patients received 110 courses of cantuzumab mertansine at doses ranging from 22 to 295 mg/m 2. Acute, transient, and reversible elevations of hepatic transaminases were the principal toxic effects. Nausea, vomiting, fatigue, and diarrhea were common but rarely severe at the highest dose levels. Dose, peak concentration, and area under the concentration–time curve correlated with the severity of transaminase elevation. The mean (± SD) clearance and terminal elimination half-life values for cantuzumab mertansine averaged 39.5 (±13.1) mL/h/m 2 and 41.1 (±16.1) hours, respectively. Strong expression (3+) of CanAg was documented in 68% of patients. Two patients with chemotherapy-refractory colorectal carcinoma had minor regressions, and four patients had persistently stable disease for more than six courses. Conclusion: The recommended dose for cantuzumab mertansine is 235 mg/m 2 IV every 3 weeks. The absence of severe hematologic toxic effects, preliminary evidence of cantuzumab mertansine tumor localization, and encouraging biologic activity in chemotherapy-refractory patients warrant further broad clinical development of this immunoconjugate in CanAg-expressing tumors.
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“the majority of clinical trials that tested ADCs targeting carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5; CEA), EGFR and trophoblast cell surface antigen-2 (TROP2) with various cytotoxic payloads showed the insufficiency of ADCs to overcome therapy resistance or have been highly toxic.7178”
From Current and emerging concepts for systemic treatment of metastatic colorectal cancer (2025) · cites this paper as [78]
Citations
Cites
Vogel, C. L., Cobleigh, M. A., Tripathy, D., Gutheil, J. C., Harris, L. N., Fehrenbacher, L., Slamon, D. J., Murphy, M., Novotny, W. F., Burchmore, M., et al. (2002) · Journal of Clinical Oncology · doi:10.1200/jco.2002.20.3.719 · Cited by 1,860
Sievers, E. L., Larson, R. A., Stadtmauer, E. A., Estey, E. H., Löwenberg, B., Dombret, H., Karanes, C., Theobald, M., Bennett, J. M., Sherman, M. L., et al. (2001) · Journal of Clinical Oncology · doi:10.1200/jco.2001.19.13.3244 · Cited by 899
Coiffier, B., Haïoun, C., Ketterer, N., Engert, A., Tilly, H., F., D. D., Johnson, P., Lister, A., Feuring‐Buske, M., Radford, J. A., et al. (1998) · PubMed · doi:10.1182/blood.v92.6.1927 · Cited by 892
Immunoconjugates containing novel maytansinoids: promising anticancer drugs.
CHARI, R. V. J., Martell, B., Gross, J. L., Cook, S., Shah, S. A., Blättler, W. A., McKenzie, S. J., & Goldmacher, V. S. (1992) · PubMed · Cited by 266
Self-citationHumanization of murine monoclonal antibodies through variable domain resurfacing.
Roguska, M., Pedersen, J. T., Keddy, C., Henry, A. H., Searle, S. J., Lambert, J. M., Goldmacher, V. S., Blättler, W. A., Rees, A. R., & Guild, B. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.969 · Cited by 208
Self-citationEradication of large colon tumor xenografts by targeted delivery of maytansinoids.
Liu, C., Tadayoni, B. M., Bourret, L. A., Mattocks, K. M., Derr, S. M., Widdison, W. C., Kedersha, N., Ariniello, P. D., Goldmacher, V. S., Lambert, J. M., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8618 · Cited by 196
Self-citationIssell, B. F., & Crooke, S. T. (1978) · Cancer Treatment Reviews · doi:10.1016/s0305-7372(78)80014-0 · Cited by 152
Baeckström, D., Hansson, G. C., Nilsson, O., Johansson, C., Gendler, S. J., & Lindholm, L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54672-x · Cited by 148
Ajani, J. A., Komaki, R. U., Putnam, J. B., Walsh, G. L., Nesbitt, J., Pisters, P. W. T., Lynch, P. M., Vaporciyan, A. A., Smythe, R. W., Lahoti, S., et al. (2001) · Cancer · doi:10.1002/1097-0142(20010715)92:2 · Cited by 117
Multani, P. S., O'Day, S. J., Nadler, L. M., & Grossbard, M. L. (1998) · PubMed · Cited by 61
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Items 101–200 of 206
Current and emerging concepts for systemic treatment of metastatic colorectal cancer
Steup, C., Kennel, K. B., Neurath, M. F., Fichtner-Feigl, S., & Greten, F. R. (2025) · Gut · doi:10.1136/gutjnl-2025-335412 · Cited by 39
“78 Theoretically, the ideal target surface antigen for an ADC would be expressed exclusively on tumour cells at a sufficient density and would be rapidly internalised on ADC binding.”
Anti‐EGFR antibody‐drug conjugate for triple‐negative breast cancer therapy
Si, Y., Xu, Y., Guan, J.-S., Chen, K., Kim, S., Yang, E. S.-H., Zhou, L., & Liu, M. (2020) · Engineering in Life Sciences · doi:10.1002/elsc.202000027 · Cited by 37
“In addition to the FDA approved Trastuzumab emtansine [39], several DM1-based ADCs, bivatuzumabmertansine [40], cantuzumab mertansine [41] and lorvotuzumab mertansine [42], are under clinical trial evaluation for the treatment of head, neck and lung cancers.”
BackgroundLu, S. X., Takach, E. J., Solomon, M. S., Zhu, Q., Law, S., & Hsieh, F. Y. (2005) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20289 · Cited by 38
Cantuzumab mertansine in a three-times a week schedule: a phase I and pharmacokinetic study
Rodon, J. A., Garrison, M. A., Hammond, L. A., Bono, J. S. D., Smith, L. S., Forero, L., Hao, D., Takimoto, C. H. M., Lambert, J. M., Pandite, L. N., et al. (2008) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-007-0672-8 · Cited by 37
“In the previous trials with cantuzumab mertansine, antitumor activity was reported in patients with colorectal carcinoma, pancreatic cancer, and adenocarcinoma of unknown primary that had strong homogeneous staining for CanAg on the tumors [ 11 , 12].”
BackgroundMethodResultInfluentialSelf-citationCancer Therapy with Radiolabeled and Drug/Toxin-conjugated Antibodies
Govindan, S. V., Griffiths, G. L., Hansen, H. J., Horak, I. D., & Goldenberg, D. M. (2005) · Technology in Cancer Research & Treatment · doi:10.1177/153303460500400406 · Cited by 37
Ma, Z., He, H., Sun, F., Xu, Y., Huang, X., Ma, Y., Zhao, H., Wang, Y., Wang, M., & Zhang, J. (2017) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-017-2436-0 · Cited by 36
An Integrated Multiplatform Bioanalytical Strategy for Antibody–Drug Conjugates: A Novel Case Study
Myler, H. A., Rangan, V. S., Wang, J., Kozhich, A. T., Cummings, J., Neely, R. J., Dail, D., Liu, A., Wang, B., Vezina, H. E., et al. (2015) · Bioanalysis · doi:10.4155/bio.15.80 · Cited by 35
Analytical Methods for the Detection and Quantification of ADCs in Biological Matrices
Cahuzac, H., & Devel, L. (2020) · Pharmaceuticals · doi:10.3390/ph13120462 · Cited by 36
Antibody Delivery of Drugs and Radionuclides: Factors Influencing Clinical Pharmacology
Prabhu, S., Boswell, C. A., Leipold, D. D., Khawli, L. A., Li, D., Lü, D., Theil, F., Joshi, A., & Lum, B. L. (2011) · Therapeutic Delivery · doi:10.4155/tde.11.41 · Cited by 35
Antibody drug conjugates in gastrointestinal cancer: From lab to clinical development
Singh, D., Dheer, D., Samykutty, A. K., & Shankar, R. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.10.006 · Cited by 35
Jackson, D., & Stover, D. R. (2014) · Pharmaceutical Research · doi:10.1007/s11095-014-1536-7 · Cited by 34
“The DLT for the huC242-SPP-DM1 ADC was elevated hepatic transaminase and the DLT for the huC242-SPDB-DM4ADCwas ocular toxicity, which was only observed in patients with low serum levels of CanAg (56).”
BackgroundInfluentialSelective Delivery of PEGylated Compounds to Tumor Cells by Anti-PEG Hybrid Antibodies
Tung, H.-Y., Su, Y.-C., Chen, B., Burnouf, P., Huang, W.-C., Chuang, K.-H., Yan, Y.-T., Cheng, T., & Roffler, S. R. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0151 · Cited by 33
“Chemical conjugation is complicated by potential damage to the targeting ligand and cargo (10, 37) as well as by generation of immunogenic epitopes.”
BackgroundHearn, B. R., Shaw, S. J., & Myles, D. C. (2007) · Elsevier eBooks · doi:10.1016/b0-08-045044-x/00205-4 · Cited by 36
The success story of trastuzumab emtansine, a targeted therapy in HER2-positive breast cancer
Dieras, V. C., & Bachelot, T. (2013) · Targeted Oncology · doi:10.1007/s11523-013-0287-4 · Cited by 32
“The first ADCs used disulphide linkers [36, 39].”
ResultInfluentialAntibody Expression and Production
Al‐Rubeai, M. (2011) · Cell engineering · doi:10.1007/978-94-007-1257-7 · Cited by 33
Epothilones and new analogues of the microtubule modulators in taxane-resistant disease
Harrison, M., & Swanton, C. (2008) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.17.4.523 · Cited by 32
“Tolcher AW, Ochoa L, Hammond LA, et al. Cantuzumab mertansine, a maytansinoid immunoconjugate directed to the CanAg antigen: a phase I, pharmacokinetic, and biologic correlative study.”
BackgroundModern Antibody Technology: The Impact on Drug Development
Moroney, S. E., & Plückthun, A. (2005) · Wiley eBooks · doi:10.1002/9783527620982.ch48 · Cited by 32
A “Dual” Cell-Level Systems PK-PD Model to Characterize the Bystander Effect of ADC
Singh, A. P., & Shah, D. K. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.01.034 · Cited by 31
Heudi, O., Barteau, S., Picard, F., & Kretz, O. (2015) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2015.12.026 · Cited by 29
López-Galindo, M. P., Sebastián, J. V. B., Jimenez-Soriano, Y., Alpiste, F., & Camps, C. (2006) · PubMed · Cited by 29
Amani, N., Dorkoosh, F. A., & Mobedi, H. (2019) · Current Drug Delivery · doi:10.2174/1567201816666191121145109 · Cited by 27
Antibodies for angiogenesis inhibition, vascular targeting and endothelial cell transcytosis
Trachsel, E., & Neri, D. (2006) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.11.002 · Cited by 26
Trends in immunoconjugate and ligand-receptor based targeting development for cancer therapy
Brumlik, M. J., Daniel, B. J., Waehler, R., Curiel, D. T., Giles, F. J., & Curiel, T. J. (2007) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.5.1.87 · Cited by 26
“Cantuzumab mertansine DM1 Microtubules CanAg I CanAg + tumours [59]”
BackgroundLiu, Y., Zhou, F., Sang, H., Ye, H., Chen, Q., Yao, L., Ni, P., Wang, G., & Zhang, J. (2017) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2017.01.011 · Cited by 25
Goli, N., Bolla, P. K., & Talla, V. (2018) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2018.08.022 · Cited by 26
A Mechanism-Based PK/PD Model for Hematological Toxicities Induced by Antibody-Drug Conjugates
Ait‐Oudhia, S., Zhang, W., & Mager, D. E. (2017) · The AAPS Journal · doi:10.1208/s12248-017-0113-5 · Cited by 27
“T-DM1 consists of the anti HER2 mAb (trastuzumab or TmAb, Herceptin®) linked to the cytotoxic agent emtansine (DM1) via lysine side chains (5,26).”
BackgroundInfluentialCostoplus, J. A., Veale, K. H., Qiu, Q., Ponte, J. F., Lanieri, L., Setiady, Y. Y., Dong, L., Skaletskaya, A., Bartle, L. M., Salomon, P. L., et al. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00310 · Cited by 24
Self-citationWilliams, M. B., Spreafico, A., Vashisht, K., & Hinrichs, M. J. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0993 · Cited by 24
“Heterogeneity of target expression in the tumor may have contributed to the absence of clinical activity for CanAg (47, 48).”
BackgroundIn vivobehaviour of antibody–drug conjugates for the targeted treatment of cancer
Xie, H., & Blättler, W. A. (2006) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.6.3.281 · Cited by 24
“In the case of huC242–DM1, the shed antigen could be removed without side effects with the first conjugate dose, and newly shed antigen was not generated fast enough to interfere with the second dose of the same immunoconjugate [16].”
BackgroundInfluentialTrastuzumab emtansine: a novel antibody-drug conjugate for HER2-positive breast cancer
Burris, H. A. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.580273 · Cited by 24
“Because of their high antitumor potency but unacceptable toxicity as free drugs, the maytansines auristatins, and calicheamicins are promising agents for ADCs.”
ResultInfluentialHepatotoxicity with antibody maytansinoid conjugates: A review of preclinical and clinical findings
Taplin, S., Vashisht, K., Walles, M., Calise, D. V., Kluwe, W. M., Bouchard, P. R., & Johnson, R. C. (2018) · Journal of Applied Toxicology · doi:10.1002/jat.3582 · Cited by 24
“…is a humanized monoclonal antibody huC242 which binds to the extracellular domain of the tumor‐associated carbohydrate antigen known as CanAg (a novel glycoform of membrane mucin MUC1 and linked to DM1 (average of about four molecules) via the cleavable linker, SPP (Tolcher et al., 2003).”
BackgroundSelf-citationFleming, M. S., Zhang, W., Lambert, J. M., & Amphlett, G. W. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.02.010 · Cited by 23
Self-citationPharmacokinetics and ADME Characterizations of Antibody–Drug Conjugates
Lin, K., Tibbitts, J., & Shen, B. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-541-5_7 · Cited by 23
Toxicities and management strategies of emerging antibody–drug conjugates in breast cancer
Kang, S., & Kim, S. (2025) · Therapeutic Advances in Medical Oncology · doi:10.1177/17588359251324889 · Cited by 24
“58 The incidence of all grades of peripheral neuropathy in patients treated with T-DM1 was reported to range from 5% to 18.3% in phase III trials, with grade 3 peripheral neuropathy occurring in 0.5%–2.2% of cases.”
InfluentialAntibody-drug conjugates targeting prostate-specific membrane antigen
Olson, W. C. (2014) · Frontiers in bioscience · doi:10.2741/4193 · Cited by 20
Murali, M., Kumar, A. R., Nair, B., Pavithran, K., Devan, A. R., Pradeep, G., & Nath, L. R. (2021) · Clinical & Translational Oncology · doi:10.1007/s12094-021-02707-5 · Cited by 21
MUC1 Antibody-Based Therapeutics: The Promise of Cancer Immunotherapy
Pourjafar, M., Samadi, P., & Saidijam, M. (2020) · Immunotherapy · doi:10.2217/imt-2020-0019 · Cited by 19
Molecular mechanisms in allergy and clinical immunology
Shearer, W. T., Rosenwasser, L. J., Bochner, B. S., Gern, J. E., Rosenthal, L. A., Sorkness, R. L., & Lemanske, R. F. (2005) · Cited by 19
World Antibody-Drug Conjugate Summit, October 15–16, 2013, San Francisco, CA
Klinguer, C., Strop, P., Shah, D. K., Ducry, L., Xu, A., & Beck, A. (2013) · mAbs · doi:10.4161/mabs.27437 · Cited by 17
Wei, D., Sullivan, M., Espinosa, O., & Yang, L. (2011) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2011.05.010 · Cited by 15
Lin, J. H., Guo, Y., & Wang, W. (2018) · Current Pharmacology Reports · doi:10.1007/s40495-018-0122-9 · Cited by 15
Jabbour, S. K., Kumar, R. N., Anderson, B. M., Chino, J., Jethwa, K. R., McDowell, L. J., Lo, A., Owen, D., Pollom, E. L., Tree, A. C., et al. (2024) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2024.01.010 · Cited by 14
Determination of ADC Concentration by Ligand-Binding Assays
Chang, H., & Shah, D. K. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9929-3_26 · Cited by 13
Ricart, A. D. (2014) · doi:10.4155/ebo.13.634 · Cited by 13
Optimising the Delivery of Tubulin Targeting Agents through Antibody Conjugation
Stack, G. D., & Walsh, J. J. (2012) · Pharmaceutical Research · doi:10.1007/s11095-012-0810-9 · Cited by 12
Typical Antibody–Drug Conjugates
Lambert, J. M. (2016) · doi:10.1002/9781119060727.ch1 · Cited by 12
Self-citationAntibody-Drug Conjugates Targeting Tumor-Specific Mucin Glycoepitopes
Brassard, J., Hughes, M. R., Roskelley, C. D., & McNagny, K. M. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2711301 · Cited by 11
“The therapeutic potential of the huC242-DM1 ADC (SB-408075: cantuzumab mertansine) was tested by Immuno-Gen (USA) in partnership with GlaxoSmithKline (UK) in a Phase 1 clinical trial to determine the optimal treatment schedule and the limiting dose toxicity [95–97].”
MethodAntibody–Cytotoxic Compound Conjugates for Oncology
Vater, C. A., & Goldmacher, V. S. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0507-9_9 · Cited by 11
Linker Technology and Impact of Linker Design on ADC Properties
Goldmacher, V. S., Singh, R., Chittenden, T. D., & Kovtun, Y. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5456-4_7 · Cited by 10
“IMGN242 exhibited a signi fi cantly longer terminal half-life of 4–5 days (for patients with low CanAg plasma levels) compared to about 2 days reported for cantuzumab mertansine [ 55, 56 ] which mirrors similar differences in the pharmacokinetics of ADCs employing these cleavable linker formats in preclinical studies…”
BackgroundResultKispal, Z. F., Kardos, D. J., Jilling, T., Kereskai, L., Isaacs, M., Balogh, D. L., Pintér, A., Till, H., & Vajda, P. (2015) · Journal of Pediatric Urology · doi:10.1016/j.jpurol.2015.04.037 · Cited by 10
Yao, Y., Cheng, Z., Ye, H., Xie, Y., He, J., Tang, M., Shen, T., Wang, J., Zhou, Y., Lu, Z., et al. (2010) · Journal of Separation Science · doi:10.1002/jssc.200900746 · Cited by 9
The Chemical Methods of Disulfide Bond Formation and Their Applications to Drug Conjugates
He, R., Pan, J. H., Mayer, J. P., & Liu, F. (2019) · Current Organic Chemistry · doi:10.2174/1385272823666191202111723 · Cited by 9
Molecular biological design of novel antineoplastic therapies
Vulfovich, M., & Saba, N. F. (2004) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.13.6.577 · Cited by 9
Chapter 23. Recent advances in antibody drug conjugates for cancer therapy
Meyer, D. L., & Senter, P. D. (2003) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(03)38024-8 · Cited by 9
Mass Spectrometry of Antibody–Drug Conjugates in Plasma and Tissue in Drug Development
Kaur, S., Xu, K., Saad, O. M., Liu, L., Slattery, T., & Dere, R. C. (2013) · Springer eBooks · doi:10.1007/978-1-4419-7862-2_7 · Cited by 8
Monoclonal Antibody Drug Conjugates for Cancer Therapy
Senter, P. D., & Meyer, D. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-49785-3_14 · Cited by 8
Xiong, Y., Li, W., Huang, W., Xiao, B., Long, J., Wang, Q., Wang, G., Wang, C., Yu, M., Yu, J., et al. (2025) · The AAPS Journal · doi:10.1208/s12248-024-01007-4 · Cited by 7
“Additionally, ELISA has limitations, such as restricted reagent and method versatility, lengthy development times, a narrow linear range, and the inability to simultaneously analyze multiple compounds (3, 16–18).”
[Bioanalysis in the development of antibody-drug conjugates].
Li, X., Chen, X.-Y., & Zhong, D. (2016) · PubMed · Cited by 6
Payloads of Antibody-Drug Conjugates
Tan, C. (2015) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-319-13081-1_2 · Cited by 6
Discovery and development of ADCs: obstacles and opportunities
Chang, H., Cheung, Y. K., & Shah, D. K. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-817134-9.00005-2 · Cited by 6
(2012) · Elsevier eBooks · doi:10.1533/9781908818096.345 · Cited by 6
Engineering Antibodies for Cancer Therapy
Goldsmith, L. E., & Robinson, M. K. (2011) · Cell engineering · doi:10.1007/978-94-007-1257-7_10 · Cited by 5
Assay Methodologies and Challenges
Kozak, K. R., & Raab, H. E. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5456-4_3 · Cited by 5
Prochaska, L., Damjanov, I., Ash, R. M., Olson, J. C., Khan, Q. J., & Sharma, P. (2015) · Cancer Treatment Communications · doi:10.1016/j.ctrc.2015.11.008 · Cited by 5
Huang, H., Deckert, J., Mysliwy, J. H., Lodge, A., Lutz, R. J., & Thurber, G. M. (2025) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-25-0484 · Cited by 4
Shao, R., & Zhen, Y. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-397833-2.00007-8 · Cited by 4
Improving the Safety Profile of ADCs
Guffroy, M., Falahatpisheh, H., & Finkelstein, M. B. (2018) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-78154-9_3 · Cited by 4
Design Factors Important for Antibody–Drug Conjugate (ADC) Payloads
Lambert, J. M. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788012898-00031 · Cited by 4
Self-citationWu, X., Kilpatrick, T., & Chau, I. (2018) · Cancer Drug Resistance · doi:10.20517/cdr.2018.16 · Cited by 4
“Best response was SD, lasting 4-5 months on average([73,75,76]).”
BackgroundImmunoconjugate Anticancer Therapeutics
Govindan, S. V., & Goldenberg, D. M. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0507-9_10 · Cited by 4
“A Phase I clinical trial of DM1-huC242 conjugate (cantuzumab mertansine) in CanAg-expressing cancers showed tolerability and evidence of antitumor activity [ 68 ].”
BackgroundSchmidt, B. J., Pan, C., Vezina, H. E., Sun, H., Leipold, D. D., & Gupta, M. (2016) · Wiley eBooks · doi:10.1002/9781119060727.ch9 · Cited by 4
Specificity Delivers: Therapeutic Role of Tumor Antigen-Specific Antibodies in Pancreatic Cancer
Jhaveri, D. T., Zheng, L., & Jaffee, E. M. (2014) · Seminars in Oncology · doi:10.1053/j.seminoncol.2014.07.001 · Cited by 3
“Cantuzumab mertansine is an ADC that links the humanized huC242 monoclonal antibody to DM1.(134) HuC242 binds specifically to CanAg, an antigen that is predominantly expressed on pancreatic, colon, and biliary tumors but is expressed at very low levels on normal tissues.”
Antibody‐Drug Conjugate Therapy
Alley, S. C., Benjamin, D. R., & Law, C. (2009) · doi:10.1002/9780470485408.ch35 · Cited by 3
Non-cleavable Linkers: Permanently Linked, for Better or for Worse
Dugal‐Tessier, J., & Jain, N. F. (2021) · Royal Society of Chemistry eBooks · doi:10.1039/9781839165153-00136 · Cited by 2
Bioanalytical Assay for Characterization of Antibody-Drug Conjugates (ADCs)
Xie, C., & Wang, Z. K. (2015) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-319-13081-1_6 · Cited by 2
Immunogenicity Assessment of Antibody Therapeutics
Stas, P., Pletinckx, J., Gansemans, Y., & Lasters, I. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511596773.005 · Cited by 2
Rugo, H. S., Krop, I. E., & Chu, Y. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5456-4_11 · Cited by 2
Antibody–Drug Conjugates in Oncology
Hamann, P. R., & Dushin, R. G. (2010) · Royal Society of Chemistry eBooks · doi:10.1039/9781849732178-00224 · Cited by 2
Antibody–Drug Conjugates: Design and Development of Trastuzumab Emtansine (T‐DM1)
Girish, S., Phillips, G. D. L., Jacobson, F. S., Junutula, J. R., & Guardino, E. (2015) · doi:10.1002/9783527678433.ch11 · Cited by 2
Pharmacokinetics/Pharmacodynamics and Disposition of Antibody–Drug Conjugates
Sukumaran, S., & Lin, K. (2025) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-031-83005-1_7 · Cited by 1
Payloads of Antibody: Drug Conjugates
Tan, C. (2025) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-031-83005-1_2 · Cited by 2
Pharmacokinetics/Pharmacodynamics and Disposition of Antibody-Drug Conjugates
Sukumaran, S., & Lin, K. (2015) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-319-13081-1_7 · Cited by 1
Studies on the Metabolism of Antibody–Drug Conjugates
Sun, X., & Erickson, H. K. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5456-4_17 · Cited by 1
(2012) · Elsevier eBooks · doi:10.1016/b978-1-907568-37-4.50029-4 · Cited by 1
Immunogenicity Assessment of Antibody Therapeutics
Stas, P., Gansemans, Y., & Lasters, I. (2009) · Springer eBooks · doi:10.1007/978-0-387-76643-0_16 · Cited by 1
Investigational Anticancer Agents Targeting the Microtubule
Vereshchagina, L. A., Scharf, O., & Colevas, A. D. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-336-3_17
Monoclonal Antibodies for the Delivery of Cytotoxic Drugs
King, D. J. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511596773.015
Empowered Antibodies for Cancer Therapy
Alley, S. C., Jeger, S., Lyon, R. P., Sussman, D. R., & Senter, P. D. (2011) · Wiley eBooks · doi:10.1002/9783527634057.ch10
Antibody‐Targeted Drugs: From Chemical Immunoconjugates to Recombinant Fusion Proteins
Mavratzas, A., Arndt, M. A. E., Kiesgen, S., & Krauß, J. (2014) · doi:10.1002/9783527682423.ch14
Targeted Toxins in Cancer Immunotherapy
Mahalingam, D., Brumlik, M. J., Waehler, R., Curiel, D. T., & Curiel, T. J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4732-0_12
[Progress on pharmacokinetic study of antibody-drug conjugates].
Guo, J., Gao, R., Quan, T.-F., Ling-yu, Z., Shi, B., Zhao, Y.-Y., Zhu, J., Li, M.-S., & Haizhi, B. (2015) · PubMed
Occupational Health and Safety Aspects of ADCs and Their Toxic Payloads
Sussman, R. G., & Farris, J. (2016) · doi:10.1002/9781119060727.ch7
Bioanalytical Strategies Enabling Successful ADC Translation
Han, X., Hansel, S. B., & King, L. (2016) · doi:10.1002/9781119060727.ch8
Intracellular Activation of SGN-35, a Potent Anti-CD30
Okeley, N. M., Miyamoto, J. B., Zhang, X., Sanderson, R. J., Benjamin, D. R., Sievers, E. L., Senter, P. D., & Alley, S. C. (2010)
Natural Product Synthesis for Drug Discovery and Chemical Biology
Yao, Z., & Wei, W. (2018) · doi:10.1002/9781118940228.ch10
Antibody–drug conjugate immunogenicity evaluation
Manning, M. S., & Hock, M. B. (2015) · doi:10.4155/fseb2013.13.48
Application of ligand-binding assays for bioanalysis of antibody–drug conjugates
Kumar, S., & Gorovits, B. (2015) · doi:10.4155/fseb2013.14.20
The Design and Development of Antibody–Drug Conjugates (ADC s ) for the Treatment of Cancer
Tumey, L. N. (2021) · Burger's Medicinal Chemistry and Drug Discovery · doi:10.1002/0471266949.bmc283
Physiologically Based Pharmacokinetic Modeling of Monoclonal Antibodies in Children
Malik, P. R. V. (2021) · UWSpace (University of Waterloo)
Metadata
- Authors
- Tolcher, A. W., Ochoa, L., Hammond, L. A., Patnaik, A., Edwards, T., Takimoto, C., Smith, L., de Bono, J., Schwartz, G., Mays, T., Jonak, Z. L., Johnson, R., DeWitte, M., Martino, H., Audette, C., Maes, K., Chari, R. V. J., Lambert, J. M., & Rowinsky, E. K.
- Affiliations
- Brooke Army Medical Center (US)
- From the Institute for Drug Development, Cancer Therapy and Research Center and The University of Texas Health Science Center at San Antonio; and Brooke Army Medical Center, San Antonio, TX; GlaxoSmithKline, Collegeville, PA; and ImmunoGen Inc., Cambridge, MA.
- ORCID
- Venue
- Journal of Clinical Oncology
- Published
- 2003-01-15
- Volume
- 21
- Issue
- 2
- Pages
- 211-222
- ISSN
- 0732-183X (ISSN-L)
- 1527-7755
- OpenAlex
- W2121080375
- Cited by
- 206
- References
- 16
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 1 · 2023: 5 · 2022: 3 · 2021: 7 · 2020: 8 · 2019: 7 · 2018: 8 · 2017: 5 · 2016: 8 · 2015: 19 · 2014: 9 · 2013: 10 · 2012: 16
- FWCI
- 10.49
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Clinical Oncology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Keywords
- DM1, pharmacokinetics, maximum tolerated dose, hepatotoxicity, colorectal cancer, solid tumors, tumor localization, anticancer activity
- MeSH terms
- Adult, Aged, Antibodies, Monoclonal, Antineoplastic Agents, Phytogenic, Dose-Response Relationship, Drug, Female, Half-Life, Humans, Infusions, Intravenous, Male, Maytansine, Middle Aged, Neoplasms, Mucin-1, Immunoconjugates, Maximum Tolerated Dose
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