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  Compartment-resolved Proteomic Analysis of Mouse Aorta during Atherosclerotic Plaque Formation Reveals Osteoclast-specific Protein Expression

Wierer, M., Prestel, M., Schiller, H. B., Yan, G., Schaab, C., Azghandi, S., et al. (2018). Compartment-resolved Proteomic Analysis of Mouse Aorta during Atherosclerotic Plaque Formation Reveals Osteoclast-specific Protein Expression. Molecular and Cellular Proteomics, 17(2), 321-334. doi:10.1074/mcp.RA117.000315.

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Mol Cell Proteomics-2018-Wierer-321-34.pdf (Publisher version), 3MB
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Mol Cell Proteomics-2018-Wierer-321-34.pdf
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The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository with the data set identifier PXD006752 (https://www.ebi.ac.uk/pride/archive/projects/PXD006752).
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Author's Choice—Final version free via Creative Commons CC-BY license.

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 Creators:
Wierer, Michael1, Author              
Prestel, Matthias2, Author
Schiller, Herbert B.1, Author              
Yan, Guangyao2, Author
Schaab, Christoph1, Author              
Azghandi, Sepiede2, Author
Werner, Julia2, Author
Kessler, Thorsten2, Author
Malik, Rainer2, Author
Murgia, Marta1, Author              
Aherrahrou, Zouhair2, Author
Schunkert, Heribert2, Author
Dichgans, Martin2, Author
Mann, Matthias1, Author              
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              

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Free keywords: SMOOTH-MUSCLE-CELLS; GLOMERULAR EXTRACELLULAR-MATRIX; CORONARY-ARTERY-DISEASE; VASCULAR CALCIFICATION; DEFICIENT MICE; GENE INACTIVATION; IMMUNE-SYSTEM; INFLAMMATION; STROKE; IDENTIFICATIONBiochemistry & Molecular Biology;
 Abstract: Atherosclerosis leads to vascular lesions that involve major rearrangements of the vascular proteome, especially of the extracellular matrix (ECM). Using single aortas from ApoE knock out mice, we quantified formation of plaques by single-run, high-resolution mass spectrometry (MS)-based proteomics. To probe localization on a proteome-wide scale we employed quantitative detergent solubility profiling. This compartment- and time-resolved resource of atherogenesis comprised 5117 proteins, 182 of which changed their expression status in response to vessel maturation and atherosclerotic plaque development. In the insoluble ECM proteome, 65 proteins significantly changed, including relevant collagens, matrix metalloproteinases and macrophage derived proteins. Among novel factors in atherosclerosis, we identified matrilin-2, the collagen IV crosslinking enzyme peroxidasin as well as the poorly characterized MAM-domain containing 2 (Mamdc2) protein as being up-regulated in the ECM during atherogenesis. Intriguingly, three subunits of the osteoclast specific V-ATPase complex were strongly increased in mature plaques with an enrichment in macrophages thus implying an active de-mineralization function.

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Language(s): eng - English
 Dates: 2018-02
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000424091400009
DOI: 10.1074/mcp.RA117.000315
 Degree: -

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Project name : This work was supported by the German Federal Ministry of Education and Research (BMBF) within the framework of the e:Med research and funding concept (e:AtheroSysMed, 01ZX1313A-2014, 01ZX1313F-2014 and 01ZX1313G-2014), the Deutsche Forschungsgemeinschaft (CRC 1123 [B3] and Munich Cluster for Systems Neurology [SyNergy]), and the FP7/2007–2103 European Union project CVgenes@target (grant agreement No Health-F2-2013-601456).
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Title: Molecular and Cellular Proteomics
Source Genre: Journal
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Publ. Info: Bethesda, MD : American Society for Biochemistry and Molecular Biology
Pages: - Volume / Issue: 17 (2) Sequence Number: - Start / End Page: 321 - 334 Identifier: ISSN: 1535-9476
CoNE: https://pure.mpg.de/cone/journals/resource/111035577487002