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 [Tesi di dottorato] (Unpublished)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
Language: English
Title: A Novel Fully Human Antitumor ImmunoRNase Targeting ErbB2-Positive Tumors
Creators:
CreatorsEmail
Borriello, Mariannamarianna.borriello@gmail.com
Date: 25 November 2010
Number of Pages: 39
Institution: Università degli Studi di Napoli Federico II
Department: Biologia strutturale e funzionale
Doctoral School: Scienze biologiche
PHD name: Biochimica e biologia cellulare e molecolare
PHD cycle: 23
PHD Coordinator:
nameemail
Arcari, Paoloarcari@unina.it
Tutor:
nameemail
De Lorenzo, Claudiacladelo@unina.it
D'Alessio, Giuseppedalessio@unina.it
Date: 25 November 2010
Number of Pages: 39
Uncontrolled Keywords: antitumor; ImmunoRNase; ErbB2; Erb-hcAb-RNase
MIUR S.S.D.: 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

Abstract

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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