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Article Open Access

17AAG‑induced internalisation of HER2‑specific Affibody molecules

  • Authors:
    • Lovisa Göstring
    • Sture Lindegren
    • Lars Gedda
  • View Affiliations / Copyright

    Affiliations: Department of Immunology, Genetics and Pathology, Uppsala University, SE‑75185 Uppsala, Sweden, Department of Radiation Physics, Sahlgrenska Academy, University of Gothenburg, SE-41345 Gothenburg, Sweden
    Copyright: © Göstring et al. This is an open access article distributed under the terms of Creative Commons Attribution License.
  • Pages: 2574-2580
    |
    Published online on: August 10, 2016
       https://doi.org/10.3892/ol.2016.4990
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Abstract

The geldanamycin derivative 17-allylamino-​17-demethoxygeldanamycin (17-AAG) is known to induce internalisation and degradation of the otherwise internalisation‑resistant human epidermal growth factor receptor 2 (HER2) receptor. In the present study, 17‑AAG was used to increase internalisation of the HER2‑specific Affibody molecule ABY‑025. The cellular redistribution of halogen‑labelled 211At‑ABY‑025 and radiometal‑labelled 111In‑ABY‑025 following treatment with 17‑AAG was studied. 17‑AAG treatment of SKOV‑3 human ovarian carcinoma and SKBR‑3 human breast carcinoma cells to some extent shifted the localisation of 111In‑ABY‑025 from the cell surface to intracellular compartments in the two cell lines. ABY‑025 labelled with the high‑linear energy transfer α emitter 211At was also internalised to a higher degree; however, due to its physiological properties, this nuclide was excreted faster. The results indicate that 17‑AAG may be used to facilitate cell‑specific intracellular localisation of a suitable cytotoxic or radioactive agent coupled to ABY‑025 in HER2‑overexpressing cells.
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Copy and paste a formatted citation
Spandidos Publications style
Göstring L, Lindegren S and Gedda L: 17AAG‑induced internalisation of HER2‑specific Affibody molecules. Oncol Lett 12: 2574-2580, 2016.
APA
Göstring, L., Lindegren, S., & Gedda, L. (2016). 17AAG‑induced internalisation of HER2‑specific Affibody molecules. Oncology Letters, 12, 2574-2580. https://doi.org/10.3892/ol.2016.4990
MLA
Göstring, L., Lindegren, S., Gedda, L."17AAG‑induced internalisation of HER2‑specific Affibody molecules". Oncology Letters 12.4 (2016): 2574-2580.
Chicago
Göstring, L., Lindegren, S., Gedda, L."17AAG‑induced internalisation of HER2‑specific Affibody molecules". Oncology Letters 12, no. 4 (2016): 2574-2580. https://doi.org/10.3892/ol.2016.4990
Copy and paste a formatted citation
x
Spandidos Publications style
Göstring L, Lindegren S and Gedda L: 17AAG‑induced internalisation of HER2‑specific Affibody molecules. Oncol Lett 12: 2574-2580, 2016.
APA
Göstring, L., Lindegren, S., & Gedda, L. (2016). 17AAG‑induced internalisation of HER2‑specific Affibody molecules. Oncology Letters, 12, 2574-2580. https://doi.org/10.3892/ol.2016.4990
MLA
Göstring, L., Lindegren, S., Gedda, L."17AAG‑induced internalisation of HER2‑specific Affibody molecules". Oncology Letters 12.4 (2016): 2574-2580.
Chicago
Göstring, L., Lindegren, S., Gedda, L."17AAG‑induced internalisation of HER2‑specific Affibody molecules". Oncology Letters 12, no. 4 (2016): 2574-2580. https://doi.org/10.3892/ol.2016.4990
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