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Molecular & Cellular Proteomics 8:2500-2514, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proteomic Analysis of Microtubule-associated Proteins during Macrophage Activation^*,

Prerna C. Patel, Katherine H. Fisher^,¶, Eric C. C. Yang^||, Charlotte M. Deane^,¶ and Rene E. Harrison^,**

From the Department of Biological Sciences, University of Toronto Scarborough, 1265 Military Trail, Toronto, Ontario M1C 1A4, Canada,
Department of Statistics, University of Oxford, Oxford OX1 3TG, United Kingdom,
¶Oxford Doctoral Training Centre, University of Oxford, Oxford OX1 3QD, United Kingdom, and
||Proteomics Core Facility, Sunnybrook Research Institute, Sunnybrook Health Sciences Centre and University of Toronto, Toronto, Ontario M4N 3M5, Canada

Classical activation of macrophages induces a wide range of signaling and vesicle trafficking events to produce a more aggressive cellular phenotype. The microtubule (MT) cytoskeleton is crucial for the regulation of immune responses. In the current study, we used a large scale proteomics approach to analyze the change in protein composition of the MT-associated protein (MAP) network by macrophage stimulation with the inflammatory cytokine interferon- and the endotoxin lipopolysaccharide. Overall the analysis identified 409 proteins that bound directly or indirectly to MTs. Of these, 52 were up-regulated 2-fold or greater and 42 were down-regulated 2-fold or greater after interferon-/lipopolysaccharide stimulation. Bioinformatics analysis based on publicly available binary protein interaction data produced a putative interaction network of MAPs in activated macrophages. We confirmed the up-regulation of several MAPs by immunoblotting and immunofluorescence analysis. More detailed analysis of one up-regulated protein revealed a role for HSP90β in stabilization of the MT cytoskeleton during macrophage activation.

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