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Phase IIa Study of Nimotuzumab to Treat Colorectal Cancer

ABSTRACT: Nimotuzumab is an IgG1 humanized monoclonal antibody that recognized an epitope located in the extra cellular domain of the human epidermal growth factor receptor (EGFR). Clinical efficacy has been shown in adult with head and neck cancer. The study assessed the safety, and efficacy of the combination of Nimotuzumab administered concomitantly with chemotherapy in patients with advanced colorectal cancer.

DISEASE(S): Colorectal Cancer,Colorectal Neoplasms

PROVIDER: 2709250 | ecrin-mdr-crc |

REPOSITORIES: ECRIN MDR

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Study of Nimotuzumab to Treat Colorectal Cancer

Project description:Nimotuzumab is an IgG1 humanized monoclonal antibody that recognized an epitope located in the extra cellular domain of the human epidermal growth factor receptor (EGFR). Clinical efficacy has been shown in adult with head and neck cancer. The study assessed the safety, and efficacy of the combination of Nimotuzumab administered concomitantly with chemotherapy in patients with advanced colorectal cancer.

| 2077668 | ecrin-mdr-crc

Study of Nimotuzumab and Irinotecan in Metastatic Colorectal Cancer

Project description:This study will determine if nimotuzumab provides a benefit in this type of cancer when given in combination with irinotecan. The study will test: * How long any good effects last. * How bad any side effects are. Objectives: Primary: The primary goal is to assess the Objective Response Rate (ORR) that the combination of irinotecan and nimotuzumab will produce in patients with irinotecan-refractory metastatic colorectal cancer Secondary: * To assess the incidence of Grade 2 or greater acneiform rash or infusion reaction, allergic reaction or anaphylactoid reaction AEs in patients with irinotecan-refractory metastatic colorectal cancer following weekly or 2-weekly nimotuzumab schedules; * To assess Progression-Free Survival (PFS), defined as time from date of randomization until date of disease progression (clinical or radiological) or death due to any cause, for the two nimotuzumab schedules; * To assess the rates and durations of Stable Disease (SD) following weekly or 2-weekly nimotuzumab schedules; * To assess the Time to Disease Progression (TTP) following weekly or 2-weekly nimotuzumab schedules; * To evaluate ORR in patients who are identified as having "primary" irinotecan resistance following weekly or 2-weekly nimotuzumab schedules; * To evaluate Overall Survival (OS) following weekly or 2-weekly nimotuzumab schedules; * To compare the two dosing schedules of nimotuzumab with respect to objective response rates and safety; * To evaluate the overall safety and toxicity profiles of these two dose regimens of nimotuzumab; * To evaluate trough levels and accumulation of nimotuzumab in serum of patients receiving the drug on weekly or 2-weekly regimens.

| 2041525 | ecrin-mdr-crc

Nimotuzumab for EGFR-amplified Advanced Pan Solid Tumors

Project description:To evaluate the efficacy and safety of nimotuzumab in the treatment of EGFR-amplified advanced pan solid tumors (Lung/Esophageal/Gastric/Pancreatic /Colorectal / Head and neck Cervical).

| 90799 | ecrin-mdr-crc

Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies

Project description:Many human monoclonal antibodies that neutralize multiple clades of HIV-1 are polyreactive and bind avidly to mammalian autoantigens. Indeed, the generation of neutralizing antibodies to the 2F5 and 4E10 epitopes of HIV-1 gp41 in man may be proscribed by immune tolerance since mice expressing the VH and VL regions of 2F5 have a block in B-cell development characteristic of central tolerance. This developmental blockade implies the presence of tolerizing autoantigens that are mimicked by the membrane-proximal external region of HIV-1 gp41. Here we identify human kynureninase (KYNU) and splicing factor 3b subunit 3 (SF3B3) as the primary conserved, vertebrate self-antigens recognized by the 2F5 and 4E10 antibodies, respectively. 2F5 binds the H4 domain of KYNU which contains the complete 2F5 linear epitope (ELDKWA). 4E10 recognizes a conformational epitope of SF3B3 that is strongly dependent on hydrophobic interactions. Opossums carry a rare KYNU H4 domain that abolishes 2F5 binding, but retain all SF3B3 4E10 epitopes. Immunization of opossums with HIV-1 gp140 induced extraordinary titers of serum antibody to the 2F5 ELDKWA epitope but little or nothing to the 4E10 determinant. Identification of structural motif shared by vertebrates and HIV-1 provides direct evidence that immunological tolerance can impair humoral responses to HIV-1. The invitrogen protoarray that contains >9,400 recombinant human proteins was used to identify self-ligands that are recognized by broadly neutralizing HIV-1 antibodies 2F5 and 4E10. An isotype-matched human myeloma protein (151K, Southern Biotech) was used as control.

2012-12-03 | E-GEOD-42673 | biostudies-arrayexpress

Xenograft mouse study in C57BL6/SCID mice using A431 cells

Project description:In this study four groups involving, Control arm, Rapamycin arm, Nimotuzumab arm and the Combination group were involved. Four tumors from each group was evaluated for microarray analysis they were the two largest and two smallest from each group. Agilent one-color experiment,Organism: Human ,Agilent-Custom Whole Genome Human 8x60k designed by Genotypic Technology Pvt. Ltd. (AMADID: 027114) , Labeling kit: Agilent Quick-Amp labeling Kit (p/n5190-0442) 4 groups: control, rapamycin, nimotuzumab, and rapamycin and nimotuzumab

2011-10-19 | E-GEOD-32333 | biostudies-arrayexpress

Evaluation of 89Zr-DFO-nimotuzumab for Non-invasive Imaging of EGFR+ Cancers by Positron Emission Tomography (PET)

Project description:Over-expression of Epidermal Growth Factor Receptor (EGFR) on cells occurs in all aggressive cancers of epithelial origin. Existing tests for monitoring EGFR expression are invasive and not reliable. There needs to be a better way to measure EGFR expression in cancerous tumors to better tailor cancer treatments. This clinical trial aims to demonstrate the feasibility of imaging cancers that express EGFR using 89Zr-DFO-nimotuzumab and Positron Emission Tomography (PET)/Computerized Tomography (CT). By non-invasively imaging the status of EGFR, 89Zr-DFO-nimotuzumab could be used to assist in the identification of patients who are likely to respond to anti-EGFR treatments, including nimotuzumab. The hypothesis is that 89Zr-DFO-nimotuzumab will accumulate to tumors over-expressing EGFR making them visible when imaged with PET/CT. This hypothesis will be tested in this study, along with the optimal imaging time and diagnostic ability.

| 2327461 | ecrin-mdr-crc

An open, single-center, Phase ? basket study of EGFR-based nimotuzumab combined with PD-1 in the treatment of advanced esophageal cancer, advanced pancreatic cancer, advanced head and neck cancer, and RAS-wt colorectal cancer

Project description:Interventions: Advanced esophageal cancer:PD-1 monoclonal antibody+nimotuzumab;Advanced pancretic cancer:PD-1 monoclonal antibody+nimotuzumab;Advanced head and neck tumor:PD-1 monoclonal antibody+nimotuzumab;RAS-WT-Advanced colorectal cancer:PD-1 monoclonal antibody+nimotuzumab Primary outcome(s): Objective response rate,ORR Study Design: Non randomized control

| 85179 | ecrin-mdr-crc

VHH D4 target identification by Mass Spectrometry

Project description:Using a synthetic library of humanized llama single domain antibodies, we identified a novel surface marker for human naturally-occuring monocyte-derived DCs. Proteomics Mass-spectrometry was used to idenitfy the target of this antibody. We found that our antibody targets an extra-cellular domain of LSP-1.

2020-05-26 | PXD015647 | Pride

Commensal bacteria and the lung environment are responsible for Th2-mediated memory yielding natural IgE in MyD88-deficient mice

Project description:IgE antibody is known as a common mediator of allergic responses, generally produced in type 2 immune responses to allergens. It is known that IgE binding to FcεRI without allergen binding promotes survival or proliferation of mast cells, basophils and other cells. Thus, spontaneously produced IgE, namely natural IgE, can increase an individual’s susceptibility to allergic diseases. Mice with a genetic defect in MyD88, a major signaling molecule downstream of Toll-like receptors, have a high level of serum natural IgE, the mechanism for which remains unknown. Here, we demonstrated that the maintenance of high serum IgE levels depends on memory B cells (MBCs). IgE from plasma cells and the sera from most of Myd88–/– mice, but none of Myd88+/– mice, recognized Streptococcus azizii (S. azizii), a commensal bacterium over-represented in the lung of Myd88–/– mice. IgG1+ MBCs from spleen also recognized S. azizii. The serum IgE levels declined by administration of antibiotics and were boosted by challenge with S. azizii in Myd88–/– mice. Moreover, bulk IgH repertoire analysis revealed that CDR3 sequences were highly shared between IgE+ PCs and IgG1+ or IgG2+ MBCs, indicating the contribution of S. azizii-specific IgG1+ MBCs to the natural IgE production.

2023-01-27 | GSE220657 | GEO

Highly selective humanized DDR1 mAb reverses immune exclusion by disrupting collagen fiber alignment in breast cancer

Project description:Discoidin domain-containing receptor 1 (DDR1) plays an important role in cancer progression. However, the DDR1 function in tumors is still elusive. We recently reported that DDR1 promoted collagen fiber alignment and formation of a physical barrier, which causes immune exclusion from tumors. We also demonstrated that our DDR1 ECD-targeting mAbs can disrupt collagen fiber alignment and increase T Cell infiltration in tumors. In this study, we humanized a DDR1 ECD-targeting mAb and showed significant antitumor efficacy in an immunocompetent mouse model. We determined the binding epitope using gene mutagenesis, hydrogen-deuterium exchange mass spectrometry (HDX-MS), and X-ray crystallography. Mechanistically, we showed that the humanized mAb inhibited DDR1 phosphorylation and, more importantly, blocked DDR1 shedding and disrupted a physical barrier formed by collagen fiber alignment in tumors. This study not only paves a pathway for development of PRTH-101 as a cancer therapeutic, but also broaden our understanding of the roles of DDR1 in modulation of collagen alignments in tumor extracellular matrix and tumor immune microenvironment.

2023-06-19 | PXD042971 | Pride

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