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Proteomic Analysis of Gliosomes from Mouse Brain: Identification and Investigation of Glial Membrane Proteins

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Department of Molecular & Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, 1081 HV Amsterdam, The Netherlands
Department of Pharmacy, Pharmacology and Toxicology Unit and Center of Excellence for Biomedical Research, University of Genoa, 16148 Genoa, Italy
§ INSERM U862, Neurocentre Magendie, 33077 Bordeaux, France
Université de Bordeaux, 33077 Bordeaux, France
*E-mail: [email protected]; Phone: +31 20 5987120; Fax: +31 20 5989281.
Cite this: J. Proteome Res. 2014, 13, 12, 5918–5927
Publication Date (Web):October 13, 2014
Copyright © 2014 American Chemical Society

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    Astrocytes are being increasingly recognized as crucial contributors to neuronal function at synapses, axons, and somas. Reliable methods that can provide insight into astrocyte proteins at the neuron–astrocyte functional interface are highly desirable. Here, we conducted a mass spectrometry analysis of Percoll gradient-isolated gliosomes, a viable preparation of glial subcellular particles often used to study mechanisms of astrocytic transmitter uptake and release and their regulation. Gliosomes were compared with synaptosomes, a preparation containing the neurotransmitter release machinery, and, accordingly, synaptosomes were enriched for proteins involved in synaptic vesicle-mediated transport. Interestingly, gliosome preparations were found to be enriched for different classes of known astrocyte proteins, such as VAMP3 (involved in astrocyte exocytosis), Ezrin (perisynaptic astrocyte cytoskeletal protein), and Basigin (astrocyte membrane glycoprotein), as well as for G-protein-mediated signaling proteins. Mass spectrometry data are available via ProteomeXchange with the identifier PXD001375. Together, these data provide the first detailed description of the gliosome proteome and show that gliosomes can be a useful preparation to study glial membrane proteins and associated processes.

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    Figure 1: Validation of mass spectrometry measurements of homogenate samples. Bar graph depicts log2 enrichment + SEM of indicated proteins as compared to homogenate measured on the same set of samples (n = 3–5) by mass spectrometry and immunoblot. Corresponding immunoblots can be found in Figure 2. * FDR p ≤ 10% for mass spectrometry measurements and p ≤ 0.05 for immunoblots as determined by a one-tailed paired Student’s t test. Table 1: Mass spectrometry data indicating the identified proteins, numbers of peptides, post-translational modifications, and measured intensities per sample. Table 2: Over-represented biological process terms in gliosomes versus homogenate with gene names. Table 3: Over-represented biological process terms in synaptosomes versus homogenate with gene names. Table 4: Over-represented biological process terms in synaptosomes versus gliosomes with gene names. Table 5: Over-represented molecular function terms in gliosomes versus homogenate with gene names. Table 6: Over-represented molecular function terms in synaptosomes versus homogenate with gene names. Table 7: Over-represented molecular function terms in gliosomes versus synaptosomes with gene names. Table 8: Over-represented molecular function terms in synaptosomes versus gliosomes with gene names. Table 9: Over-represented cellular component terms in gliosomes versus homogenate with gene names. Table 10: Over-represented cellular component terms in synaptosomes versus homogenate with gene names. Table 11: Over-represented cellular component terms in gliosomes versus synaptosomes with gene names. Table 12: Over-represented cellular component terms in synaptosomes versus gliosomes with gene names. This material is available free of charge via the Internet at The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (54) via the PRIDE partner repository with the dataset identifier PDX001375.

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