rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
2
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pubmed:dateCreated |
2008-11-14
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pubmed:abstractText |
HER2-specific affibody molecules in different formats have previously been shown to be useful tumor targeting agents for radionuclide-based imaging and therapy applications, but their biological effect on tumor cells is not well known. In this study, two dimeric ((Z(HER2:4))(2) and (Z(HER2:342))(2)) and one monomeric (Z(HER2:342)) HER2-specific affibody molecules are investigated with respect to biological activity. Both (Z(HER2:4))(2) and (Z(HER2:342))(2) were found to decrease the growth rate of SKBR-3 cells to the same extent as the antibody trastuzumab. When the substances were removed, the cells treated with the dimeric affibody molecules continued to be growth suppressed while the cells treated with trastuzumab immediately resumed normal proliferation. The effects of Z(HER2:342) were minor on both proliferation and cell signaling. The dimeric (Z(HER2:4))(2) and (Z(HER2:342))(2) both reduced growth of SKBR-3 cells and may prove therapeutically useful either by themselves or as carriers of radionuclides or other cytotoxic agents.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal, Humanized,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, erbB-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Z(HER2.4)2 affibody,
http://linkedlifedata.com/resource/pubmed/chemical/trastuzumab
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
1090-2104
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
12
|
pubmed:volume |
377
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
489-94
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:18930032-Antibodies, Monoclonal,
pubmed-meshheading:18930032-Antibodies, Monoclonal, Humanized,
pubmed-meshheading:18930032-Biosensing Techniques,
pubmed-meshheading:18930032-Breast Neoplasms,
pubmed-meshheading:18930032-Cell Line,
pubmed-meshheading:18930032-Cell Line, Tumor,
pubmed-meshheading:18930032-Cell Proliferation,
pubmed-meshheading:18930032-Dimerization,
pubmed-meshheading:18930032-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:18930032-Humans,
pubmed-meshheading:18930032-Phosphorylation,
pubmed-meshheading:18930032-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:18930032-Receptor, erbB-2,
pubmed-meshheading:18930032-Recombinant Fusion Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Dimeric HER2-specific affibody molecules inhibit proliferation of the SKBR-3 breast cancer cell line.
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pubmed:affiliation |
Department of Oncology, Radiology and Clinical Immunology, Division of Biomedical Radiation Sciences, Rudbeck Laboratory, Uppsala University, SE-751 85 Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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