ArticleBritish journal of cancer2010
Two novel human anti-ErbB2 immunoagents are active on trastuzumab-resistant tumours.
Article in British journal of cancer, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 17 papers.
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17 citing papers in PubMed, 39 citations in OpenAlex.
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- Article
- Effects of a second-generation human anti-ErbB2 ImmunoRNase on trastuzumab-resistant tumors and cardiac cells.Protein engineering, design & selection : PEDS · 2014Article
- Effects of a human compact anti-ErbB2 antibody on gastric cancer.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2014Article
- A novel fully human antitumor immunoRNase resistant to the RNase inhibitor.Protein engineering, design & selection : PEDS · 2013Article
- Novel antibody-based proteins for cancer immunotherapy.Cancers · 2011Article
- A novel fully human antitumour immunoRNase targeting ErbB2-positive tumours.British journal of cancer · 2011Article
Corrections and comments
- Expression of concern
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundOverexpression of ErbB2 receptor in breast cancer is associated with disease progression and poor prognosis. Trastuzumab, the only humanised anti-ErbB2 antibody currently used in breast cancer, has proven to be effective; however, a relevant problem for clinical practice is that a high fraction of breast cancer patients shows primary or acquired resistance to trastuzumab treatment.
methodsWe tested on trastuzumab-resistant cells two novel human anti-tumour immunoconjugates engineered in our laboratory by fusion of a human anti-ErbB2 scFv, termed Erbicin, with either a human RNase or the Fc region of a human IgG1. Both Erbicin-derived immunoagents (EDIAs) are selectively cytotoxic for ErbB2-positive cancer cells in vitro and vivo, target an ErbB2 epitope different from that recognised by trastuzumab and do not show cardiotoxic effects.
resultsWe report that EDIAs are active also on trastuzumab-resistant tumour cells both in vitro and in vivo, most likely because of the different epitope recognised, as EDIAs, unlike trastuzumab, were found to be able to inhibit the signalling pathway downstream of ErbB2.
conclusionThese results suggest that EDIAs are immunoagents that could not only fulfil the therapeutic need of patients ineligible to trastuzumab treatment due to cardiac dysfunction but also prove to be useful for breast cancer patients unresponsive to trastuzumab treatment.
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