Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer

The epidermal growth factor receptor 2 (HER2) is a tyrosine kinase overexpressed in nearly 20% to 25% of invasive breast cancers. Trastuzumab is a humanized monoclonal antibody that targets HER2. The majority of patients with metastatic breast cancer initially respond to trastuzumab, however, within...

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Main Authors: Gabriel L. Fiszman, María A. Jasnis
Format: Article
Language:English
Published: Wiley 2011-01-01
Series:International Journal of Breast Cancer
Online Access:http://dx.doi.org/10.4061/2011/352182
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author Gabriel L. Fiszman
María A. Jasnis
author_facet Gabriel L. Fiszman
María A. Jasnis
author_sort Gabriel L. Fiszman
collection DOAJ
description The epidermal growth factor receptor 2 (HER2) is a tyrosine kinase overexpressed in nearly 20% to 25% of invasive breast cancers. Trastuzumab is a humanized monoclonal antibody that targets HER2. The majority of patients with metastatic breast cancer initially respond to trastuzumab, however, within 1 year of treatment disease progresses. Several molecular mechanisms have been described as contributing to the development of trastuzumab resistance. They could be grouped as impaired access of trastuzumab to HER2, upregulation of HER2 downstream signaling pathways, signaling of alternative pathways, and impaired immune antitumor mechanisms. However, since many of them have overlapping effects, it would be of great clinical impact to identify the principal signaling pathways involved in drug resistance. Significant efforts are being applied to find other therapeutic modalities besides trastuzumab treatment to be used alone or in combination with current modalities.
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spelling doaj-art-5df84d1599804d1ab40c36069f7aac392025-08-20T03:34:45ZengWileyInternational Journal of Breast Cancer2090-31892011-01-01201110.4061/2011/352182352182Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast CancerGabriel L. Fiszman0María A. Jasnis1Immunobiology Department, Institute of Oncology A. H. Roffo, University of Buenos Aires, Avenida San Martín 5481, CP1417 DTB Buenos Aires, ArgentinaImmunobiology Department, Institute of Oncology A. H. Roffo, University of Buenos Aires, Avenida San Martín 5481, CP1417 DTB Buenos Aires, ArgentinaThe epidermal growth factor receptor 2 (HER2) is a tyrosine kinase overexpressed in nearly 20% to 25% of invasive breast cancers. Trastuzumab is a humanized monoclonal antibody that targets HER2. The majority of patients with metastatic breast cancer initially respond to trastuzumab, however, within 1 year of treatment disease progresses. Several molecular mechanisms have been described as contributing to the development of trastuzumab resistance. They could be grouped as impaired access of trastuzumab to HER2, upregulation of HER2 downstream signaling pathways, signaling of alternative pathways, and impaired immune antitumor mechanisms. However, since many of them have overlapping effects, it would be of great clinical impact to identify the principal signaling pathways involved in drug resistance. Significant efforts are being applied to find other therapeutic modalities besides trastuzumab treatment to be used alone or in combination with current modalities.http://dx.doi.org/10.4061/2011/352182
spellingShingle Gabriel L. Fiszman
María A. Jasnis
Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
International Journal of Breast Cancer
title Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
title_full Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
title_fullStr Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
title_full_unstemmed Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
title_short Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
title_sort molecular mechanisms of trastuzumab resistance in her2 overexpressing breast cancer
url http://dx.doi.org/10.4061/2011/352182
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