HER-3 targeting alters the dimerization pattern of ErbB protein family members in breast carcinomas
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Michalis V. Karamouzis1, Georgia Dalagiorgou1, Urania Georgopoulou2, Afroditi Nonni3, Michalis Kontos4, Athanasios G. Papavassiliou1
1Molecular Oncology Unit, Department of Biological Chemistry, Medical School, National and Kapodistrian University of Athens, 11527 Athens, Greece
2Laboratory of Molecular Virology, Hellenic Pasteur Institute, 11521 Athens, Greece
3First Department of Pathology, Medical School, National and Kapodistrian University of Athens, 11527 Athens, Greece
4Department of Propaedeutic Surgery, Medical School, National and Kapodistrian University of Athens, ‘Laikon’ General Hospital, 11527 Athens, Greece
Athanasios G. Papavassiliou, e-mail: firstname.lastname@example.org
Keywords: HER-3, ErbB, dimerization pattern, proximity ligation assay, breast cancer
Received: September 13, 2015 Accepted: December 22, 2015 Published: December 26, 2015
Breast carcinogenesis is a multi-step process in which membrane receptor tyrosine kinases are crucial participants. Lots of research has been done on epidermal growth factor receptor (EGFR) and HER-2 with important clinical results. However, breast cancer patients present intrinsic or acquired resistance to available HER-2-directed therapies, mainly due to HER-3. Using new techniques, such as proximity ligation assay, herein we evaluate the dimerization pattern of HER-3 and the importance of context-dependent dimer formation between HER-3 and other HER protein family members. Additionally, we show that the efficacy of novel HER-3 targeting agents can be better predicted in certain breast cancer patient sub-groups based on the dimerization pattern of HER protein family members. Moreover, this model was also evaluated and reproduced in human paraffin-embedded breast cancer tissues.
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