Source:http://linkedlifedata.com/resource/pubmed/id/12644568
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2003-4-2
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| pubmed:abstractText |
Specific molecular markers for various normal and pathogenic cell states and cell types provide knowledge of basic biological systems and have a direct application in targeted therapy. We describe a proteomic method based on the combination of new and improved phage display antibody technologies and mass spectrometry that allows identification of cell type-specific protein markers. The most important features of the method are (i) reduction of experimental noise originating from background binding of phage particles and (ii) isolation of affinity binders after a single round of selection, which assures a high diversity of binders. The method demonstrates, for the first time, the ability to detect, identify, and analyze both secreted and membrane-associated extracellular proteins as well as a variety of different cellular structures including proteins and carbohydrates. The optimized phage display method was applied to analysis of human skin keratinocytes resulting in the isolation of a panel of antibodies. Fourteen of these antibodies were further characterized, half of which predominantly recognized keratinocytes in a screen of a range of different cell types. Three cognate keratinocyte antigens were subsequently identified by mass spectrometry as laminin-5, plectin, and fibronectin. The combination of phage display technology with mass spectrometry methods for protein identification is a general and promising approach for proteomic analysis of cell surface complexity.
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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/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Genetic Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Intermediate Filament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/PLEC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Plectin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
1535-9476
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
2
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
61-9
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| pubmed:dateRevised |
2011-10-27
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| pubmed:meshHeading |
pubmed-meshheading:12644568-Antibodies, Monoclonal,
pubmed-meshheading:12644568-Breast,
pubmed-meshheading:12644568-Cell Line,
pubmed-meshheading:12644568-Cell Line, Tumor,
pubmed-meshheading:12644568-Cells, Cultured,
pubmed-meshheading:12644568-Coliphages,
pubmed-meshheading:12644568-Epitopes,
pubmed-meshheading:12644568-Escherichia coli,
pubmed-meshheading:12644568-Genetic Markers,
pubmed-meshheading:12644568-HeLa Cells,
pubmed-meshheading:12644568-Humans,
pubmed-meshheading:12644568-Intermediate Filament Proteins,
pubmed-meshheading:12644568-Keratinocytes,
pubmed-meshheading:12644568-Laminin,
pubmed-meshheading:12644568-Mass Spectrometry,
pubmed-meshheading:12644568-Peptide Library,
pubmed-meshheading:12644568-Plectin,
pubmed-meshheading:12644568-Sensitivity and Specificity,
pubmed-meshheading:12644568-Skin Physiological Phenomena,
pubmed-meshheading:12644568-Spectrometry, Mass, Matrix-Assisted Laser...
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| pubmed:year |
2003
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| pubmed:articleTitle |
Identification of keratinocyte-specific markers using phage display and mass spectrometry.
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| pubmed:affiliation |
Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus, Denmark.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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