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David M. Goldenberg - One of the best experts on this subject based on the ideXlab platform.

  • targeting lgr5 cells with an Antibody Drug Conjugate for the treatment of colon cancer
    Science Translational Medicine, 2015
    Co-Authors: Melissa R Junttila, David M. Goldenberg, Xi Wang, Bu Er Wang, Thinh S Pham, John A Flygare, Shang Fan Yu, Carter Fields, Jeffrey Easthamanderson, Mallika Singh
    Abstract:

    Cancer stem cells (CSCs) are hypothesized to actively maintain tumors similarly to how their normal counterparts replenish differentiated cell types within tissues, making them an attractive therapeutic target for the treatment of cancer. Because most CSC markers also label normal tissue stem cells, it is unclear how to selectively target them without compromising normal tissue homeostasis. We evaluated a strategy that targets the cell surface leucine-rich repeat–containing G protein–coupled receptor 5 (LGR5), a well-characterized tissue stem cell and CSC marker, with an Antibody Conjugated to distinct cytotoxic Drugs. One Antibody-Drug Conjugate (ADC) demonstrated potent tumor efficacy and safety in vivo. Furthermore, the ADC decreased tumor size and proliferation, translating to improved survival in a genetically engineered model of intestinal tumorigenesis. These data demonstrate that ADCs can be leveraged to exploit differences between normal and cancer stem cells to successfully target gastrointestinal cancers.

  • sacituzumab govitecan immu 132 an anti trop 2 sn 38 Antibody Drug Conjugate characterization and efficacy in pancreatic gastric and other cancers
    Bioconjugate Chemistry, 2015
    Co-Authors: Thomas M Cardillo, Serengulam V Govindan, Robert M Sharkey, Preeti Trisal, Roberto Arrojo, Edmund A Rossi, Chienhsing Chang, David M. Goldenberg
    Abstract:

    Sacituzumab govitecan (IMMU-132) is an AntibodyDrug Conjugate (ADC) made from a humanized anti-Trop-2 monoclonal Antibody (hRS7) Conjugated with the active metabolite of irinotecan, SN-38. In addition to its further characterization, as the clinical utility of IMMU-132 expands to an ever-widening range of Trop-2-expressing solid tumor types, its efficacy in new disease models needs to be explored in a nonclinical setting. Unlike most ADCs that use ultratoxic Drugs and stable linkers, IMMU-132 uses a moderately toxic Drug with a moderately stable carbonate bond between SN-38 and the linker. Flow cytometry and immunohistochemistry disclosed that Trop-2 is expressed in a wide range of tumor types, including gastric, pancreatic, triple-negative breast (TNBC), colonic, prostate, and lung. While cell-binding experiments reveal no significant differences between IMMU-132 and parental hRS7 Antibody, surface plasmon resonance analysis using a Trop-2 CM5 chip shows a significant binding advantage for IMMU-132 over...

  • epratuzumab sn 38 a new Antibody Drug Conjugate for the therapy of hematologic malignancies
    Molecular Cancer Therapeutics, 2012
    Co-Authors: Robert M Sharkey, Thomas M Cardillo, Serengulam V Govindan, David M. Goldenberg
    Abstract:

    We previously found that slowly internalizing antibodies Conjugated with SN-38 could be used successfully when prepared with a linker that allows approximately 50% of the IgG-bound SN-38 to dissociate in serum every 24 hours. In this study, the efficacy of SN-38 Conjugates prepared with epratuzumab (rapidly internalizing) and veltuzumab (slowly internalizing), humanized anti-CD22 and anti-CD20 IgG, respectively, was examined for the treatment of B-cell malignancies. Both AntibodyDrug Conjugates had similar nanomolar activity against a variety of human lymphoma/leukemia cell lines, but slow release of SN-38 compromised potency discrimination in vitro even against an irrelevant Conjugate. When SN-38 was stably linked to the anti-CD22 Conjugate, its potency was reduced 40- to 55-fold. Therefore, further studies were conducted only with the less stable, slowly dissociating linker. In vivo , similar antitumor activity was found between CD22 and CD20 AntibodyDrug Conjugate in mice-bearing Ramos xenografts, even though Ramos expressed 15-fold more CD20 than CD22, suggesting that the internalization of the epratuzumab–SN-38 Conjugate (Emab–SN-38) enhanced its activity. Emab–SN-38 was more efficacious than a nonbinding, irrelevant IgG–SN-38 Conjugate in vivo , eliminating a majority of well-established Ramos xenografts at nontoxic doses. In vitro and in vivo studies showed that Emab–SN-38 could be combined with unConjugated veltuzumab for a more effective treatment. Thus, Emab–SN-38 is active in lymphoma and leukemia at doses well below toxic levels and therefore represents a new promising agent with therapeutic potential alone or combined with anti-CD20 Antibody therapy. Mol Cancer Ther; 11(1); 224–34. ©2011 AACR .

Robert M Sharkey - One of the best experts on this subject based on the ideXlab platform.

  • efficacy of sacituzumab govitecan anti trop 2 sn 38 Antibody Drug Conjugate for treatment refractory hormone receptor positive hr her2 metastatic breast cancer mbc
    Journal of Clinical Oncology, 2018
    Co-Authors: Aditya Bardia, Jennifer R Diamond, Rebecca Moroose, Ingrid A Mayer, Vandana G Abramson, Dejan Juric, Sara M. Tolaney, Linda T Vahdat, Joyce Oshaughnessy, Robert M Sharkey
    Abstract:

    1004Background: Sacituzumab govitecan is a novel Antibody-Drug Conjugate consisting of SN-38, the active metabolite of irinotecan, Conjugated to a humanized mAb targeting Trop-2 (trophoblastic anti...

  • efficacy of sacituzumab govitecan anti trop 2 sn 38 Antibody Drug Conjugate for treatment refractory hormone receptor positive hr her2 metastatic breast cancer mbc
    Journal of Clinical Oncology, 2018
    Co-Authors: Aditya Bardia, Jennifer R Diamond, Rebecca Moroose, Ingrid A Mayer, Vandana G Abramson, Dejan Juric, Sara M. Tolaney, Linda T Vahdat, Joyce Oshaughnessy, Robert M Sharkey
    Abstract:

    1004Background: Sacituzumab govitecan is a novel Antibody-Drug Conjugate consisting of SN-38, the active metabolite of irinotecan, Conjugated to a humanized mAb targeting Trop-2 (trophoblastic antigen-2), which is highly expressed in many epithelial cancers. A phase I/II basket trial (NCT01631552) investigated its activity in patients (pts) with advanced cancers, and we previously reported on pts with triple-negative mBC. Results in HR+/ HER2 negative (as per ASCO/CAP guidelines) mBC pts who had ≥ 1 prior hormonal therapy are presented here. Methods: Pts received sacituzumab govitecan at a dose of 10 mg/kg on days 1 & 8 of a 21-day cycle until progression or unacceptable toxicity. Eligibility included ≥ 1 prior line of standard therapy for metastatic disease, measurable disease by CT or MRI. Efficacy was assessed locally by RECIST 1.1. Adverse events (AE) were evaluated according to CTCAE v4.0, Results: Fifty-four pts with HR+/HER2- mBC (all female; median age 54 yrs, range 33-79) were accrued between 2/2...

  • sacituzumab govitecan immu 132 an anti trop 2 sn 38 Antibody Drug Conjugate characterization and efficacy in pancreatic gastric and other cancers
    Bioconjugate Chemistry, 2015
    Co-Authors: Thomas M Cardillo, Serengulam V Govindan, Robert M Sharkey, Preeti Trisal, Roberto Arrojo, Edmund A Rossi, Chienhsing Chang, David M. Goldenberg
    Abstract:

    Sacituzumab govitecan (IMMU-132) is an AntibodyDrug Conjugate (ADC) made from a humanized anti-Trop-2 monoclonal Antibody (hRS7) Conjugated with the active metabolite of irinotecan, SN-38. In addition to its further characterization, as the clinical utility of IMMU-132 expands to an ever-widening range of Trop-2-expressing solid tumor types, its efficacy in new disease models needs to be explored in a nonclinical setting. Unlike most ADCs that use ultratoxic Drugs and stable linkers, IMMU-132 uses a moderately toxic Drug with a moderately stable carbonate bond between SN-38 and the linker. Flow cytometry and immunohistochemistry disclosed that Trop-2 is expressed in a wide range of tumor types, including gastric, pancreatic, triple-negative breast (TNBC), colonic, prostate, and lung. While cell-binding experiments reveal no significant differences between IMMU-132 and parental hRS7 Antibody, surface plasmon resonance analysis using a Trop-2 CM5 chip shows a significant binding advantage for IMMU-132 over...

  • epratuzumab sn 38 a new Antibody Drug Conjugate for the therapy of hematologic malignancies
    Molecular Cancer Therapeutics, 2012
    Co-Authors: Robert M Sharkey, Thomas M Cardillo, Serengulam V Govindan, David M. Goldenberg
    Abstract:

    We previously found that slowly internalizing antibodies Conjugated with SN-38 could be used successfully when prepared with a linker that allows approximately 50% of the IgG-bound SN-38 to dissociate in serum every 24 hours. In this study, the efficacy of SN-38 Conjugates prepared with epratuzumab (rapidly internalizing) and veltuzumab (slowly internalizing), humanized anti-CD22 and anti-CD20 IgG, respectively, was examined for the treatment of B-cell malignancies. Both AntibodyDrug Conjugates had similar nanomolar activity against a variety of human lymphoma/leukemia cell lines, but slow release of SN-38 compromised potency discrimination in vitro even against an irrelevant Conjugate. When SN-38 was stably linked to the anti-CD22 Conjugate, its potency was reduced 40- to 55-fold. Therefore, further studies were conducted only with the less stable, slowly dissociating linker. In vivo , similar antitumor activity was found between CD22 and CD20 AntibodyDrug Conjugate in mice-bearing Ramos xenografts, even though Ramos expressed 15-fold more CD20 than CD22, suggesting that the internalization of the epratuzumab–SN-38 Conjugate (Emab–SN-38) enhanced its activity. Emab–SN-38 was more efficacious than a nonbinding, irrelevant IgG–SN-38 Conjugate in vivo , eliminating a majority of well-established Ramos xenografts at nontoxic doses. In vitro and in vivo studies showed that Emab–SN-38 could be combined with unConjugated veltuzumab for a more effective treatment. Thus, Emab–SN-38 is active in lymphoma and leukemia at doses well below toxic levels and therefore represents a new promising agent with therapeutic potential alone or combined with anti-CD20 Antibody therapy. Mol Cancer Ther; 11(1); 224–34. ©2011 AACR .

Qing Sheng - One of the best experts on this subject based on the ideXlab platform.

  • abstract 4743 using genome wide crispr screen to understand resistance mechanisms to pca062 a p cadherin targeting Antibody Drug Conjugate
    Cancer Research, 2019
    Co-Authors: Mark Zambrowski, Katherine Seiss, Tinya Abrams, Giordano Caponigro, William R Tschantz, Tony Dalessio, Jennifer Campbell, Qing Sheng
    Abstract:

    P-cadherin (PCAD) is a member of the cadherin family that mediates calcium dependent cell-cell contacts in adherens-type junctions of epithelium. Expression of P-cadherin is high in malignant tumors of epithelial origin, such as breast, esophagus, head and neck cancers, but low in normal tissues. This expression pattern makes P-cadherin a potential good target for Antibody-Drug Conjugates (ADCs). PCA062 is a first-in-class Antibody Drug Conjugate targeting P-cadherin. PCA062 consists of a fully human anti-P-cadherin Antibody of the IgG1/κ subtype, a non-cleavable bi-functional linker (SMCC) and a maytansine-derived cytotoxic payload (DM1, with a target average Drug to Antibody ratio (DAR) of 3.8). PCA062 activity was examined in a collection of cell lines expressing high level of PCAD. A subset of these PCAD high cell lines are resistant to PCA062 treatment while they remain sensitive to DM1, suggesting defects in the process of PCA062 uptake or the processing and release of DM1 into the cytoplasmic compartment. PCA062 internalization rate was measured by the uptake of a fluorescent dye labeled anti-PCAD Antibody (CQY684, the Ab portion of PCA062) in both PCA062 sensitive and resistant lines. PCA062 resistant lines show slower CQY684 internalization as compared to PCA062 sensitive lines, indicating a defect in ADC internalization may contribute to PCA062 resistance. To explore additional resistance mechanisms to PCA062 as well as to find critical components for PCA062 internalization, a genome wide CRISPR screen was performed in PCA062 sensitive HCC1954 and in PCA062 resistant KYSE510 cell line in the presence and absence of PCA062 and DM1 to look for genes that when knocked out may specifically modulate PCA062 sensitivity. The multi-Drug resistant gene MRP1 is a strong hit for PCA062 sensitization in both PCA062 resistant KYSE510 and PCA062 sensitive HCC1954 cells. Lysosomal transporter SLC46A3 and Saga transcription complex components are strong rescue hits for PCA062 in HCC1954. These data suggest that in addition to target expression level and cell intrinsic sensitivity to payload, genes involved in ADC internalization and payload cytoplasmic accumulation will also impact tumor cell sensitivity to ADCs. Citation Format: Angela Tam, Mark Zambrowski, Katherine Seiss, Si-Qi Liu, Tinya Abrams, Giordano Caponigro, William Tschantz, Jennifer Campbell, Tony DAlessio, Qing Sheng. Using genome-wide CRISPR screen to understand resistance mechanisms to PCA062, a P-cadherin targeting Antibody-Drug Conjugate [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 4743.

  • abstract 4743 using genome wide crispr screen to understand resistance mechanisms to pca062 a p cadherin targeting Antibody Drug Conjugate
    Cancer Research, 2019
    Co-Authors: Mark Zambrowski, Katherine Seiss, Tinya Abrams, Giordano Caponigro, William R Tschantz, Tony Dalessio, Jennifer Campbell, Qing Sheng
    Abstract:

    P-cadherin (PCAD) is a member of the cadherin family that mediates calcium dependent cell-cell contacts in adherens-type junctions of epithelium. Expression of P-cadherin is high in malignant tumors of epithelial origin, such as breast, esophagus, head and neck cancers, but low in normal tissues. This expression pattern makes P-cadherin a potential good target for Antibody-Drug Conjugates (ADCs). PCA062 is a first-in-class Antibody Drug Conjugate targeting P-cadherin. PCA062 consists of a fully human anti-P-cadherin Antibody of the IgG1/κ subtype, a non-cleavable bi-functional linker (SMCC) and a maytansine-derived cytotoxic payload (DM1, with a target average Drug to Antibody ratio (DAR) of 3.8). PCA062 activity was examined in a collection of cell lines expressing high level of PCAD. A subset of these PCAD high cell lines are resistant to PCA062 treatment while they remain sensitive to DM1, suggesting defects in the process of PCA062 uptake or the processing and release of DM1 into the cytoplasmic compartment. PCA062 internalization rate was measured by the uptake of a fluorescent dye labeled anti-PCAD Antibody (CQY684, the Ab portion of PCA062) in both PCA062 sensitive and resistant lines. PCA062 resistant lines show slower CQY684 internalization as compared to PCA062 sensitive lines, indicating a defect in ADC internalization may contribute to PCA062 resistance. To explore additional resistance mechanisms to PCA062 as well as to find critical components for PCA062 internalization, a genome wide CRISPR screen was performed in PCA062 sensitive HCC1954 and in PCA062 resistant KYSE510 cell line in the presence and absence of PCA062 and DM1 to look for genes that when knocked out may specifically modulate PCA062 sensitivity. The multi-Drug resistant gene MRP1 is a strong hit for PCA062 sensitization in both PCA062 resistant KYSE510 and PCA062 sensitive HCC1954 cells. Lysosomal transporter SLC46A3 and Saga transcription complex components are strong rescue hits for PCA062 in HCC1954. These data suggest that in addition to target expression level and cell intrinsic sensitivity to payload, genes involved in ADC internalization and payload cytoplasmic accumulation will also impact tumor cell sensitivity to ADCs. Citation Format: Angela Tam, Mark Zambrowski, Katherine Seiss, Si-Qi Liu, Tinya Abrams, Giordano Caponigro, William Tschantz, Jennifer Campbell, Tony DAlessio, Qing Sheng. Using genome-wide CRISPR screen to understand resistance mechanisms to PCA062, a P-cadherin targeting Antibody-Drug Conjugate [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 4743.

Joohee Yi - One of the best experts on this subject based on the ideXlab platform.

Toshimi Takano - One of the best experts on this subject based on the ideXlab platform.