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 |
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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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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).</description><identifier>ISSN: 1615-9853</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.201500040</identifier><identifier>PMID: 25914152</identifier><language>eng</language><publisher>Germany: Blackwell Publishing Ltd</publisher><subject>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</subject><ispartof>Proteomics (Weinheim), 2015-09, Vol.15 (17), p.2934-2944</ispartof><rights>2015 WILEY‐VCH Verlag GmbH & Co. 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M.</creatorcontrib><title>Unravelling the proteome of degenerative human mitral valves</title><title>Proteomics (Weinheim)</title><addtitle>Proteomics</addtitle><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).</description><subject>Annotations</subject><subject>Biglycan - metabolism</subject><subject>Biomarkers - blood</subject><subject>Catheters</subject><subject>Cell biology</subject><subject>Chondroitin Sulfate Proteoglycans - metabolism</subject><subject>Databases, Protein</subject><subject>Decorin</subject><subject>Degenerative diseases</subject><subject>Extracellular matrix</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>Humans</subject><subject>Keratan Sulfate - metabolism</subject><subject>Lumican</subject><subject>Mitral valve</subject><subject>Mitral Valve - metabolism</subject><subject>Mitral Valve - physiopathology</subject><subject>Mitral Valve Insufficiency - metabolism</subject><subject>Mitral Valve Insufficiency - physiopathology</subject><subject>Mitral Valve Prolapse - metabolism</subject><subject>Mitral Valve Prolapse - physiopathology</subject><subject>Molecular modelling</subject><subject>Molecular Sequence Annotation</subject><subject>Pathogenesis</subject><subject>Proteins</subject><subject>Proteome - analysis</subject><subject>Proteome profiling</subject><subject>Proteomes</subject><subject>Regurgitation</subject><subject>Rheumatic heart disease</subject><subject>SWATH-MS</subject><subject>Tandem Mass Spectrometry</subject><subject>Ultrasonic imaging</subject><subject>Versican</subject><subject>Versicans - metabolism</subject><subject>Vinculin</subject><subject>Vinculin - metabolism</subject><subject>Western blotting</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1P3DAQxa2qVflorz1WkXrhkmXGju1Y6qVa0QUJCkKgSr1YTjKB0HwsdrKF_x6vFvbQQ-lh5Dn83tMbP8Y-IcwQgB8uu6accUAJABm8YbuoUKYmV_h2u0uxw_ZCuANAnRv9nu1waTBDyXfZ1-veuxW1bdPfJOMtJUs_jDR0lAx1UtEN9eTd2KwouZ061yddM3rXJivXrih8YO9q1wb6-Pzus-vvR1fz4_T0fHEy_3aallLkIs2UpgLRQQFZnee1KEvBKTPSQaWMI3AFyEwoU-oiBuR14bBytVQ1L0yuK7HPDja-Mdz9RGG0XRPKGNr1NEzBoka9_gDI_wMFoxG5hIh--Qu9Gybfx0OsACPWo8y_qOiVG2UM8kjNNlTphxA81Xbpm875R4tg10XZdVF2W1QUfH62nYqOqi3-0kwE5Ab407T0-IqdvTg7mSMHLqIu3eiaMNLDVuf8b6u00NL-_LGwvxaX2RnOr-xCPAH4mKtB</recordid><startdate>201509</startdate><enddate>201509</enddate><creator>Tan, Hwee Tong</creator><creator>Lim, Teck Kwang</creator><creator>Richards, Arthur Mark</creator><creator>Kofidis, Theodoros</creator><creator>Teoh, Kristine Leok-Kheng</creator><creator>Ling, Lieng H.</creator><creator>Chung, Maxey C. 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M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unravelling the proteome of degenerative human mitral valves</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2015-09</date><risdate>2015</risdate><volume>15</volume><issue>17</issue><spage>2934</spage><epage>2944</epage><pages>2934-2944</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><abstract>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).</abstract><cop>Germany</cop><pub>Blackwell Publishing Ltd</pub><pmid>25914152</pmid><doi>10.1002/pmic.201500040</doi><tpages>11</tpages></addata></record> |
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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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