Profiling Protein Tyrosine Phosphorylation: A Quantitative 45-Plex Peptide-Based Immunoassay
| Autor: | James R. Graham, Amy B. Hall, Cheryl Murphy, Christine Rauh-Adelmann, Timothy K. Nadler, Lucy G. Yen, Neal F. Gordon, Jeffrey A. Radding |
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| Rok vydání: | 2008 |
| Předmět: |
Proteomics
macromolecular substances Protein tyrosine phosphatase Biology SH2 domain Models Biological Biochemistry Antibodies Receptor tyrosine kinase Cell Line Analytical Chemistry Epitopes Jurkat Cells chemistry.chemical_compound Cell Line Tumor Humans Protein phosphorylation Phosphorylation Immunoassay Tyrosine phosphorylation U937 Cells Reference Standards Cell biology chemistry biology.protein Tyrosine Molecular Medicine Signal transduction Peptides Platelet-derived growth factor receptor Signal Transduction Biotechnology |
| Zdroj: | SLAS Discovery. 13:626-637 |
| ISSN: | 2472-5552 |
| DOI: | 10.1177/1087057108319978 |
| Popis: | Cellular homeostasis and responses to stimuli are mediated by complex signaling network events dominated by changes in protein phosphorylation states. Understanding information flow in the network is essential for correlating signaling changes to cell physiology. Tyrosine phosphorylation constitutes only a small portion of all protein phosphorylation, but its importance is manifested by the significant role it plays in diseases such as cancer. A peptide-based immunoassay microarray, designed to provide site specificity, quantification, broad coverage, and accessibility, is described that profiles 45 tyrosine phosphorylation sites across 34 proteins. Epidermal growth factor–stimulated A431 cells in the absence and presence of kinase inhibitors analyzed by microarrays showed biologically validated tyrosine phosphorylation changes and unanticipated activation of other targets. The approach is scalable for increasing the breadth of content as well as for interrogating other types of protein posttranslational modifications. (Journal of Biomolecular Screening 2008:626-637) |
| Databáze: | OpenAIRE |
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