ArticleTranslational cancer research2023
Bioactivity of recombinant humanized monoclonal antibody against HER2
Article in Translational cancer research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Recent Technological and Intellectual Property Trends in Antibody-Drug Conjugate Research.Pharmaceutics · 2024Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Human epidermal growth factor receptor 2 (HER2) protein is overexpressed on the surface of various epithelial ovarian cancer tissues, mediates the proliferation, differentiation, metastasis, and signal transduction of tumor cells, and thus is a potential cancer therapeutic target. However, its research in ovarian cancer is still limited, and how to quickly obtain a large number of antibodies remains a concern for researchers. Methods: In this study, we expressed the recombinant anti-HER2 humanized monoclonal antibody (rhHER2-mAb) in human embryonic kidney 293 (HEK293) cells through transient gene expression (TGE) technology by constructing a mammalian cell expression vector. Firstly, the transfection conditions has been optimized, the ratio of light chain (LC) and heavy chain (HC) was optimized in the range of 4:1 to 1:2 and the ration DNA and polyethyleneimine was optimized in the range of 4:1 to 1:1. The antibody was purified by rProtein A affinity chromatography, and its mediated antibody-dependent cellular cytotoxicity (ADCC) was identified by lactate dehydrogenase release assays. The anti-tumor activity of rhHER2-mAb was evaluated in non-obese diabetic/severe combined immunodeficiency mice. Results: The expression of rhHER2-mAb in the HEK293F cells was at the highest level (100.5 mg/L) when the DNA/polyethyleneimine and light-chain/heavy-chain ratios were 1:4 and 1:2, respectively. The half-maximal inhibitory concentration of the ADCC of the antibodies against the SK-OV-3, OVCAR-3, and A-2780 cells were 12.36, 5.43, and 102.90 ng/mL, respectively. The animal experiments with the mice showed that rhHER2-mAb effectively inhibited the growth (P<0.01) of the SK-OV-3 tumors at a dose of 10 mg/kg. Conclusions: TGE technology allows us to quickly obtain a large number of anti-HER2 antibodies compared to the traditional method of constructing stable cell lines, and its
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.