Compartment-resolved Proteomic Analysis of Mouse Aorta during Atherosclerotic Plaque Formation Reveals Osteoclast-specific Protein Expression
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Compartment-resolved Proteomic Analysis of Mouse Aorta during Atherosclerotic Plaque Formation Reveals Osteoclast-specific Protein Expression. / Wierer, Michael; Prestel, Matthias; Schiller, Herbert; Yan, Guangyao; Schaab, Christoph; Azghandi, Sepiede; Werner, Julia; Kessler, Thorsten; Malik, Rainer; Murgia, Marta; Aherrahrou, Zouhair; Schunkert, Heribert; Dichgans, Martin; Mann, Matthias.
In: Molecular and Cellular Proteomics, 02.2018.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Compartment-resolved Proteomic Analysis of Mouse Aorta during Atherosclerotic Plaque Formation Reveals Osteoclast-specific Protein Expression
AU - Wierer, Michael
AU - Prestel, Matthias
AU - Schiller, Herbert
AU - Yan, Guangyao
AU - Schaab, Christoph
AU - Azghandi, Sepiede
AU - Werner, Julia
AU - Kessler, Thorsten
AU - Malik, Rainer
AU - Murgia, Marta
AU - Aherrahrou, Zouhair
AU - Schunkert, Heribert
AU - Dichgans, Martin
AU - Mann, Matthias
N1 - Copyright © 2017, The American Society for Biochemistry and Molecular Biology.
PY - 2018/2
Y1 - 2018/2
N2 - 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 5,117 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 upregulated in the ECM in the course of 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.
AB - 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 5,117 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 upregulated in the ECM in the course of 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.
KW - Journal Article
U2 - 10.1074/mcp.RA117.000315
DO - 10.1074/mcp.RA117.000315
M3 - Journal article
C2 - 29208753
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
SN - 1535-9476
ER -
ID: 186869030