Borriello, Marianna (2010) A Novel Fully Human Antitumor ImmunoRNase Targeting ErbB2-Positive Tumors. [Tesi di dottorato] (Unpublished)
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Item Type: | Tesi di dottorato |
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Resource language: | English |
Title: | A Novel Fully Human Antitumor ImmunoRNase Targeting ErbB2-Positive Tumors |
Creators: | Creators Email Borriello, Marianna marianna.borriello@gmail.com |
Date: | 25 November 2010 |
Number of Pages: | 39 |
Institution: | Università degli Studi di Napoli Federico II |
Department: | Biologia strutturale e funzionale |
Scuola di dottorato: | Scienze biologiche |
Dottorato: | Biochimica e biologia cellulare e molecolare |
Ciclo di dottorato: | 23 |
Coordinatore del Corso di dottorato: | nome email Arcari, Paolo arcari@unina.it |
Tutor: | nome email De Lorenzo, Claudia cladelo@unina.it D'Alessio, Giuseppe dalessio@unina.it |
Date: | 25 November 2010 |
Number of Pages: | 39 |
Keywords: | antitumor; ImmunoRNase; ErbB2; Erb-hcAb-RNase |
Settori scientifico-disciplinari del MIUR: | Area 05 - Scienze biologiche > BIO/10 - Biochimica |
Date Deposited: | 09 Dec 2010 16:47 |
Last Modified: | 30 Apr 2014 19:43 |
URI: | http://www.fedoa.unina.it/id/eprint/7963 |
DOI: | 10.6092/UNINA/FEDOA/7963 |
Collection description
A second generation anti-ErbB2 ImmunoRNase, called Erb-hcAb-RNase, was obtained by the fusion of Erb-hcAb, a human compact anti-ErbB2 antibody, with human pancreatic ribonuclease (HP-RNase or RNase 1). We show herein that Erb-hcAb-RNase retains the enzymatic activity of human pancreatic RNase and specifically binds to ErbB2-positive cells with an affinity comparable to that of the parental Erb-hcAb. Moreover, this novel immunoRNase is endowed with an effective and selective antiproliferative action for ErbB2-positive tumor cells both in vitro and in vivo. Its antitumor activity is more potent than that of the parental Erb-hcAb as the novel immunoconjugate has acquired RNase-based cytotoxicity in addition to the inhibitory growth effects, antibody-dependent and complement-dependent cytotoxicity of the compact antibody. Erb-hcAb-RNase could be a promising candidate for the immunotherapy of ErbB2-positive tumours as it combines the advantages of the first generation scFv-based immunoRNase with those of a fully functional antibody
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