Protein Kinase Activity Profiling of Postmortem Human Brain Tissue

J.J.M. Hoozemans, R. Hilhorst, R. Ruitenbeek, J.M. Rozemuller, S.M. van der Vies

Research output: Contribution to JournalArticleAcademicpeer-review


Background: Identification of signal transduction pathways that are critically involved in Alzheimer's disease (AD) is essential for the development of disease-specific biomarkers and drug therapy. Objective: This study is aimed at identifying protein kinases and signaling pathways that are activated in AD pathology. Methods: Microarray-based kinome profiling was employed for the detection of protein kinase activity in postmortem brain tissue derived from AD and age-matched nondemented control cases. Global serine/threonine kinase activity profiles are identified applying a peptide array system consisting of 140 peptides derived from known kinase substrate sequences covalently attached to porous chips, through which a protein solution is constantly pumped up and down. Peptide phosphorylation is determined by measuring the association of a mixture of fluorescently labeled antibodies, raised against phosphoserine- or phosphothreonine-containing peptides. Results: Protein lysates from freshly frozen postmortem brain tissue from nondemented controls and pathologically confirmed AD cases show ATP-dependent phosphorylation of peptides. In AD and control cases, peptides that are differentially phosphorylated are identified. Conclusion: Protein kinase activity profiling can be used to reveal novel kinases and new signaling pathways involved in AD pathology. Copyright © 2012 S. Karger AG, Basel.
Original languageEnglish
Pages (from-to)46-48
JournalNeurodegenerative Diseases
Issue number1-4
Early online date16 Feb 2012
Publication statusPublished - 2012


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