A bead-based western for high-throughput cellular signal transduction analyses

Fridolin Treindl, Benjamin Ruprecht, Yvonne Beiter, Silke Schultz, Anette Döttinger, Annette Staebler, Thomas O. Joos, Simon Kling, Oliver Poetz, Tanja Fehm, Hans Neubauer, Bernhard Kuster and Markus F. Templin ()
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Fridolin Treindl: NMI Natural and Medical Sciences Institute at the University of Tübingen
Benjamin Ruprecht: Chair for Proteomics and Bioanalytics, Center of Life and Food Sciences Weihenstephan, Technische Universität München
Yvonne Beiter: NMI Natural and Medical Sciences Institute at the University of Tübingen
Silke Schultz: Medical Faculty and University Hospital of the Heinrich-Heine University Duesseldorf
Anette Döttinger: NMI Natural and Medical Sciences Institute at the University of Tübingen
Annette Staebler: University Hospital Tübingen
Thomas O. Joos: NMI Natural and Medical Sciences Institute at the University of Tübingen
Simon Kling: NMI Natural and Medical Sciences Institute at the University of Tübingen
Oliver Poetz: NMI Natural and Medical Sciences Institute at the University of Tübingen
Tanja Fehm: Medical Faculty and University Hospital of the Heinrich-Heine University Duesseldorf
Hans Neubauer: Medical Faculty and University Hospital of the Heinrich-Heine University Duesseldorf
Bernhard Kuster: Chair for Proteomics and Bioanalytics, Center of Life and Food Sciences Weihenstephan, Technische Universität München
Markus F. Templin: NMI Natural and Medical Sciences Institute at the University of Tübingen

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract Dissecting cellular signalling requires the analysis of large number of proteins. The DigiWest approach we describe here transfers the western blot to a bead-based microarray platform. By combining gel-based protein separation with immobilization on microspheres, hundreds of replicas of the initial blot are created, thus enabling the comprehensive analysis of limited material, such as cells collected by laser capture microdissection, and extending traditional western blotting to reach proteomic scales. The combination of molecular weight resolution, sensitivity and signal linearity on an automated platform enables the rapid quantification of hundreds of specific proteins and protein modifications in complex samples. This high-throughput western blot approach allowed us to identify and characterize alterations in cellular signal transduction that occur during the development of resistance to the kinase inhibitor Lapatinib, revealing major changes in the activation state of Ephrin-mediated signalling and a central role for p53-controlled processes.

Date: 2016
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DOI: 10.1038/ncomms12852

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