Quantification of HER expression and dimerization in patients' tumor samples using time-resolved Förster resonance energy transfer

• Published in: PloS one Vol. 7; no. 7; p. e37065
• Main Authors: Ho-Pun-Cheung, Alexandre, Bazin, Hervé, Gaborit, Nadège, Larbouret, Christel, Garnero, Patrick, Assenat, Eric, Castan, Florence, Bascoul-Mollevi, Caroline, Ramos, Jeanne, Ychou, Marc, Pèlegrin, André, Mathis, Gérard, Lopez-Crapez, Evelyne
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 19.07.2012; Public Library of Science (PLoS)
• Subjects: Activation; Animals; Bioassays; Biological assays; Biology; Breast cancer; Breast Neoplasms - metabolism; Cancer therapies; Cell Line, Tumor; Copy number; Dimerization; Energy consumption; Energy transfer; Epidermal growth factor; Epidermal growth factor receptors; ErbB-2 protein; FDA approval; Female; Fluorescence resonance energy transfer; Fluorescence Resonance Energy Transfer - methods; Humans; Immunoglobulins; In Vitro Techniques; Kinases; Laboratories; Ligands; Medical prognosis; Medicine; Metastasis; Mice; mRNA; Oncology; Patients; Protein expression; Protein Multimerization; Proteins; Receptor mechanisms; Receptor, Epidermal Growth Factor - metabolism; Receptor, ErbB-2 - chemistry; Receptor, ErbB-2 - metabolism; Receptors; Resonance; Rodents; Tumors; Tyrosine; Xenografts; France

Following the development of targeted therapies against EGFR and HER2, two members of the human epidermal receptor (HER) family of receptor tyrosine kinases, much interest has been focused on their expression in tumors. However, knowing the expression levels of individual receptors may not be suffic...