Identification of proteins associated with ligand-activated estrogen receptor α in human breast cancer cell nuclei by tandem affinity purification and nano LC-MS/MS
| Autor: | Angela Bamundo, Giovanni Nassa, Roberta Tarallo, E. Nola, Ornella Paris, Marc Baumann, Tuula A. Nyman, Angelo Facchiano, Alessandro Weisz, Concetta Ambrosino |
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| Přispěvatelé: | Tarallo, R, Bamundo, A, Nassa, G, Nola, Ernesto, Paris, O, Ambrosino, C, Facchiano, A, Baumann, M, Nyman, Ta, Weisz, A. |
| Rok vydání: | 2010 |
| Předmět: |
Functional proteomic
medicine.medical_specialty Carcinogenesis Clinical Biochemistry Estrogen receptor Breast Neoplasms Biology Biochemistry Interactome Chromatography Affinity 03 medical and health sciences 0302 clinical medicine Tandem Mass Spectrometry Internal medicine Cell Line Tumor Breast Cancer medicine Humans Nuclear protein Molecular Biology Estrogen receptor beta Oncogene 030304 developmental biology Tandem affinity purification 0303 health sciences Estrogen Receptor alpha Genomics Ligand (biochemistry) Cell biology Endocrinology Nuclear receptor Gene expression 030220 oncology & carcinogenesis Cancer cell Female Chromatography Liquid |
| Zdroj: | Proteomics. 11(1) |
| ISSN: | 1615-9861 |
| Popis: | Estrogen receptor α (ER-α) is a key mediator of estrogen actions in breast cancer (BC) cells. Understanding the effects of ligand-activated ER-α in target cells requires identification of the molecular partners acting in concert with this nuclear receptor to transduce the hormonal signal. We applied tandem affinity purification (TAP), glycerol gradient centrifugation and MS analysis to isolate and identify proteins interacting with ligand-activated ER-α in MCF-7 cell nuclei. This led to the identification of 264 ER-associated proteins, whose functions highlight the hinge role of ER-α in the coordination of multiple hormone-regulated nuclear processes in BC cells. |
| Databáze: | OpenAIRE |
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