Abstract
Design and evaluation of new high-affinity protein compounds that can selectively and efficiently destroy human cancer cells are a priority research area in biomedicine. In this study we report on the ability of the recombinant phototoxic protein DARPin-miniSOG to interact with breast adenacarcinoma human cells overexpressing the extracellular domain of human epidermal growth factor receptor 2 (HER2). It was found that the targeted phototoxin DARPin-miniSOG specifically binds to the HER2 with following internalization and slow recycling back to the cell membrane. An insight into the role of DARPin-miniSOG in HER2 internalization could contribute to the treatment of HER2-positive cancer using this phototoxic protein.
| Original language | English |
|---|---|
| Pages (from-to) | 126-132 |
| Number of pages | 7 |
| Journal | Acta Naturae |
| Volume | 7 |
| Issue number | 3 |
| Publication status | Published - 2015 |
| Externally published | Yes |
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Keywords
- DARPin
- HER2
- Internalization
- Recycling
- Scaffold proteins
- Targeted phototoxic protein
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Medicine
- Molecular Biology
Cite this
Internalization and Recycling of the HER2 Receptor on Human Breast Adenocarcinoma Cells Treated with Targeted Phototoxic Protein DARPinminiSOG. / Shilova, O. N.; Proshkina, G. M.; Lebedenko, E. N.; Deyev, S. M.
In: Acta Naturae, Vol. 7, No. 3, 2015, p. 126-132.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Internalization and Recycling of the HER2 Receptor on Human Breast Adenocarcinoma Cells Treated with Targeted Phototoxic Protein DARPinminiSOG
AU - Shilova, O. N.
AU - Proshkina, G. M.
AU - Lebedenko, E. N.
AU - Deyev, S. M.
PY - 2015
Y1 - 2015
N2 - Design and evaluation of new high-affinity protein compounds that can selectively and efficiently destroy human cancer cells are a priority research area in biomedicine. In this study we report on the ability of the recombinant phototoxic protein DARPin-miniSOG to interact with breast adenacarcinoma human cells overexpressing the extracellular domain of human epidermal growth factor receptor 2 (HER2). It was found that the targeted phototoxin DARPin-miniSOG specifically binds to the HER2 with following internalization and slow recycling back to the cell membrane. An insight into the role of DARPin-miniSOG in HER2 internalization could contribute to the treatment of HER2-positive cancer using this phototoxic protein.
AB - Design and evaluation of new high-affinity protein compounds that can selectively and efficiently destroy human cancer cells are a priority research area in biomedicine. In this study we report on the ability of the recombinant phototoxic protein DARPin-miniSOG to interact with breast adenacarcinoma human cells overexpressing the extracellular domain of human epidermal growth factor receptor 2 (HER2). It was found that the targeted phototoxin DARPin-miniSOG specifically binds to the HER2 with following internalization and slow recycling back to the cell membrane. An insight into the role of DARPin-miniSOG in HER2 internalization could contribute to the treatment of HER2-positive cancer using this phototoxic protein.
KW - DARPin
KW - HER2
KW - Internalization
KW - Recycling
KW - Scaffold proteins
KW - Targeted phototoxic protein
UR - http://www.scopus.com/inward/record.url?scp=84944627461&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84944627461&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:84944627461
VL - 7
SP - 126
EP - 132
JO - Acta Naturae
JF - Acta Naturae
SN - 2075-8251
IS - 3
ER -