Short Communication

Oncogene (2007) 26, 7163–7169; doi:10.1038/sj.onc.1210528; published online 21 May 2007

ERBB2 phosphorylation and trastuzumab sensitivity of breast cancer cell lines

C Ginestier1,5, J Adélaïde1,5, A Gonçalvès2,3,5, L Repellini1, F Sircoulomb1, A Letessier1, P Finetti1, J Geneix1, E Charafe-Jauffret1,3,4, F Bertucci1,2,3, J Jacquemier1,4, P Viens2,3 and D Birnbaum1

  1. 1UMR599 Inserm, Institut Paoli-Calmettes, Centre de Recherche en Cancérologie de Marseille, Département d'Oncologie Moléculaire, Marseille, France
  2. 2UMR599 Inserm, Institut Paoli-Calmettes, Centre de Recherche en Cancérologie de Marseille, Département d'Oncologie Médicale, Marseille, France
  3. 3Faculté de Médecine, Université de la Méditerranée, Marseille, France
  4. 4Département de BioPathologie, Institut Paoli-Calmettes, Marseille, France

Correspondence: Dr D Birnbaum, UMR599 Inserm, 27 Bd. Leï Roure, 13009 Marseille, France. E-mail: birnbaum@marseille.inserm.fr

5These authors contributed equally to this work.

Received 6 January 2006; Revised 22 February 2007; Accepted 11 April 2007; Published online 21 May 2007.

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Abstract

Breast cancers that overexpress the ERBB2 tyrosine kinase receptor may be treated with the recombinant humanized monoclonal anti-ERBB2 antibody trastuzumab (herceptin). However, resistance to this targeted therapy is frequent. We have determined the response of 18 breast tumor cell lines to trastuzumab and compared it with the ERBB2 phosphorylation status using antibodies directed against tyrosine residue 1248. We show that sensitivity to trastuzumab is frequently associated with the expression of a phosphorylated ERBB2 protein.

Keywords:

herceptin, trastuzumab, ERBB2, breast cancer, phosphorylation, tyrosine kinase

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