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Title: Deep proteomic profiling of human carotid atherosclerotic plaques using multidimensional LC-MS/MS
Authors: Sze, Siu Kwan
Hao, Piliang
Ren, Yan
Pasterkamp, Gerard
Moll, Frans L.
de Kleijn, Dominique P. V.
Keywords: DRNTU::Science::Biological sciences::Human anatomy and physiology
Issue Date: 2014
Source: Hao, P., Ren, Y., Pasterkamp, G., Moll, F. L., de Kleijn, D. P. V., & Sze, S. K. (2014). Deep proteomic profiling of human carotid atherosclerotic plaques using multidimensional LC-MS/MS. PROTEOMICS - clinical applications, 8(7-8), 631-635.
Series/Report no.: PROTEOMICS - clinical applications
Abstract: Purpose: To increase the proteome coverage of human atherosclerotic plaques and identify low-abundance proteins that may have important functions during the development and progression of atherosclerosis. Experimental design: Thirty-eight human carotid atherosclerotic plaques were pooled into two samples and analyzed in triplicate using offline multidimensional LC-MS/MS. The collected fractions of trypsin-digested peptides from Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) were analyzed by LC-MS/MS on a Q Exactive (Thermo Fisher, MA, USA). Results: A total of 4702 proteins were identified from atherosclerotic plaques at a false discovery rate (FDR) of 1%, of which 3846 were identified with at least 2 unique peptides. Many pathways related to the development and progression of atherosclerosis were identified, such as atherosclerosis signaling, toll receptor signaling pathway and inhibition of matrix metalloproteases. Many low-abundance proteins with important functions in atherosclerosis that were previously unidentifiable using mass spectrometry based proteomics methods, such as TGF-β, interleukins and other growth factors, were identified confidently from plaques. Conclusions and clinical relevance: This study has substantially increased the coverage of the atherosclerotic plaque proteome which represents a leap forward in understanding of plaque composition, development and progression. The identification of many low-abundance proteins may also facilitate biomarker discovery.
ISSN: 1862-8346
DOI: 10.1002/prca.201400007
Rights: © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Fulltext Permission: none
Fulltext Availability: No Fulltext
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