Unravelling the proteome of degenerative human mitral valves

Degenerative mitral valve disease (DMVD), which includes the syndromes of mitral valve prolapse (MVP) and flail leaflet, is a common valvular condition which can be complicated by mitral regurgitation and adverse cardiovascular outcomes. Although several genetic and other studies of MVP in dog model...

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Veröffentlicht in:Proteomics (Weinheim) 2015-09, Vol.15 (17), p.2934-2944
Hauptverfasser: Tan, Hwee Tong, Lim, Teck Kwang, Richards, Arthur Mark, Kofidis, Theodoros, Teoh, Kristine Leok-Kheng, Ling, Lieng H., Chung, Maxey C. M.
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container_end_page 2944
container_issue 17
container_start_page 2934
container_title Proteomics (Weinheim)
container_volume 15
creator Tan, Hwee Tong
Lim, Teck Kwang
Richards, Arthur Mark
Kofidis, Theodoros
Teoh, Kristine Leok-Kheng
Ling, Lieng H.
Chung, Maxey C. M.
description Degenerative mitral valve disease (DMVD), which includes the syndromes of mitral valve prolapse (MVP) and flail leaflet, is a common valvular condition which can be complicated by mitral regurgitation and adverse cardiovascular outcomes. Although several genetic and other studies of MVP in dog models have provided some information regarding the underlying disease mechanisms, the proteins and molecular events mediating human MVP pathogenesis have not been unraveled. In this study, we report the first large‐scale proteome profiling of mitral valve tissue resected from patients with MVP. A total of 1134 proteins were identified, some of which were validated using SWATH‐MS and western blotting. GO annotation of these proteins confirmed the validity of this proteome database in various cardiovascular processes. Among the list of proteins, we found several structural and extracellular matrix proteins, such as asporin, biglycan, decorin, lumican, mimecan, prolargin, versican, and vinculin, that have putative roles in the pathophysiology of MVP. These proteins could also be involved in the cardiac remodeling associated with mitral regurgitation. All MS data have been deposited in the ProteomeXchange with identifier PXD000774 (http://proteomecentral.proteomexchange.org/dataset/PXD000774).
doi_str_mv 10.1002/pmic.201500040
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Among the list of proteins, we found several structural and extracellular matrix proteins, such as asporin, biglycan, decorin, lumican, mimecan, prolargin, versican, and vinculin, that have putative roles in the pathophysiology of MVP. These proteins could also be involved in the cardiac remodeling associated with mitral regurgitation. 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subjects Annotations
Biglycan - metabolism
Biomarkers - blood
Catheters
Cell biology
Chondroitin Sulfate Proteoglycans - metabolism
Databases, Protein
Decorin
Degenerative diseases
Extracellular matrix
Extracellular Matrix Proteins - metabolism
Humans
Keratan Sulfate - metabolism
Lumican
Mitral valve
Mitral Valve - metabolism
Mitral Valve - physiopathology
Mitral Valve Insufficiency - metabolism
Mitral Valve Insufficiency - physiopathology
Mitral Valve Prolapse - metabolism
Mitral Valve Prolapse - physiopathology
Molecular modelling
Molecular Sequence Annotation
Pathogenesis
Proteins
Proteome - analysis
Proteome profiling
Proteomes
Regurgitation
Rheumatic heart disease
SWATH-MS
Tandem Mass Spectrometry
Ultrasonic imaging
Versican
Versicans - metabolism
Vinculin
Vinculin - metabolism
Western blotting
title Unravelling the proteome of degenerative human mitral valves
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