Peroxidasin-like protein: a novel peroxidase homologue in the human heart
Peroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the ex...
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| Veröffentlicht in: | Cardiovascular research 2014-03, Vol.101 (3), p.393-399 |
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| container_title | Cardiovascular research |
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| creator | Péterfi, Zalán Tóth, Zsuzsanna E Kovács, Hajnal A Lázár, Eniko Sum, Adrienn Donkó, Agnes Sirokmány, Gábor Shah, Ajay M Geiszt, Miklós |
| description | Peroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the expression and function of peroxidasin-like protein (PXDNL), a previously unknown peroxidase homologue.
We cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.
PXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function. |
| doi_str_mv | 10.1093/cvr/cvt256 |
| format | Article |
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We cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.
PXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function.</description><identifier>EISSN: 1755-3245</identifier><identifier>DOI: 10.1093/cvr/cvt256</identifier><identifier>PMID: 24253521</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Cells, Cultured ; Extracellular Matrix - metabolism ; Extracellular Matrix Proteins - pharmacology ; Gene Expression Regulation ; Heart - drug effects ; Heart Failure - metabolism ; Humans ; In Situ Hybridization - methods ; Oxidation-Reduction - drug effects ; Peroxidase - pharmacology ; Peroxidasin ; RNA, Messenger - metabolism</subject><ispartof>Cardiovascular research, 2014-03, Vol.101 (3), p.393-399</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24253521$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Péterfi, Zalán</creatorcontrib><creatorcontrib>Tóth, Zsuzsanna E</creatorcontrib><creatorcontrib>Kovács, Hajnal A</creatorcontrib><creatorcontrib>Lázár, Eniko</creatorcontrib><creatorcontrib>Sum, Adrienn</creatorcontrib><creatorcontrib>Donkó, Agnes</creatorcontrib><creatorcontrib>Sirokmány, Gábor</creatorcontrib><creatorcontrib>Shah, Ajay M</creatorcontrib><creatorcontrib>Geiszt, Miklós</creatorcontrib><title>Peroxidasin-like protein: a novel peroxidase homologue in the human heart</title><title>Cardiovascular research</title><addtitle>Cardiovasc Res</addtitle><description>Peroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the expression and function of peroxidasin-like protein (PXDNL), a previously unknown peroxidase homologue.
We cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.
PXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function.</description><subject>Animals</subject><subject>Cells, Cultured</subject><subject>Extracellular Matrix - metabolism</subject><subject>Extracellular Matrix Proteins - pharmacology</subject><subject>Gene Expression Regulation</subject><subject>Heart - drug effects</subject><subject>Heart Failure - metabolism</subject><subject>Humans</subject><subject>In Situ Hybridization - methods</subject><subject>Oxidation-Reduction - drug effects</subject><subject>Peroxidase - pharmacology</subject><subject>Peroxidasin</subject><subject>RNA, Messenger - metabolism</subject><issn>1755-3245</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1j01LxDAYhIMg7rp68QdIjl6q-WxSb7K4urCgBz2XJH1ro2lTm3bRf2_B3cMwMDwMMwhdUXJLScHv3H6YNTKZn6AlVVJmnAm5QOcpfRJCpFTiDC2YYJJLRpdo-wpD_PGVSb7Lgv8C3A9xBN_dY4O7uIeA-yMBuIltDPFjAuw7PDZzMLWmww2YYbxAp7UJCS4PvkLvm8e39XO2e3narh92WU8FHTMtau2E5k4YoaQtKk2KeY6G3Li8okwosJRYqwupnNYAwAknyglba0sqyVfo5r93Hvo9QRrL1icHIZgO4pRKKgnJdcF4PqPXB3SyLVRlP_jWDL_l8T7_A5SnWjU</recordid><startdate>20140301</startdate><enddate>20140301</enddate><creator>Péterfi, Zalán</creator><creator>Tóth, Zsuzsanna E</creator><creator>Kovács, Hajnal A</creator><creator>Lázár, Eniko</creator><creator>Sum, Adrienn</creator><creator>Donkó, Agnes</creator><creator>Sirokmány, Gábor</creator><creator>Shah, Ajay M</creator><creator>Geiszt, Miklós</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20140301</creationdate><title>Peroxidasin-like protein: a novel peroxidase homologue in the human heart</title><author>Péterfi, Zalán ; Tóth, Zsuzsanna E ; Kovács, Hajnal A ; Lázár, Eniko ; Sum, Adrienn ; Donkó, Agnes ; Sirokmány, Gábor ; Shah, Ajay M ; Geiszt, Miklós</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p141t-84f8c483c4a475b9d8092428e6ac6d1247eb10bb8957c88eee30307c4bf8b0d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Cells, Cultured</topic><topic>Extracellular Matrix - metabolism</topic><topic>Extracellular Matrix Proteins - pharmacology</topic><topic>Gene Expression Regulation</topic><topic>Heart - drug effects</topic><topic>Heart Failure - metabolism</topic><topic>Humans</topic><topic>In Situ Hybridization - methods</topic><topic>Oxidation-Reduction - drug effects</topic><topic>Peroxidase - pharmacology</topic><topic>Peroxidasin</topic><topic>RNA, Messenger - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Péterfi, Zalán</creatorcontrib><creatorcontrib>Tóth, Zsuzsanna E</creatorcontrib><creatorcontrib>Kovács, Hajnal A</creatorcontrib><creatorcontrib>Lázár, Eniko</creatorcontrib><creatorcontrib>Sum, Adrienn</creatorcontrib><creatorcontrib>Donkó, Agnes</creatorcontrib><creatorcontrib>Sirokmány, Gábor</creatorcontrib><creatorcontrib>Shah, Ajay M</creatorcontrib><creatorcontrib>Geiszt, Miklós</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Cardiovascular research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Péterfi, Zalán</au><au>Tóth, Zsuzsanna E</au><au>Kovács, Hajnal A</au><au>Lázár, Eniko</au><au>Sum, Adrienn</au><au>Donkó, Agnes</au><au>Sirokmány, Gábor</au><au>Shah, Ajay M</au><au>Geiszt, Miklós</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peroxidasin-like protein: a novel peroxidase homologue in the human heart</atitle><jtitle>Cardiovascular research</jtitle><addtitle>Cardiovasc Res</addtitle><date>2014-03-01</date><risdate>2014</risdate><volume>101</volume><issue>3</issue><spage>393</spage><epage>399</epage><pages>393-399</pages><eissn>1755-3245</eissn><abstract>Peroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the expression and function of peroxidasin-like protein (PXDNL), a previously unknown peroxidase homologue.
We cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.
PXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function.</abstract><cop>England</cop><pmid>24253521</pmid><doi>10.1093/cvr/cvt256</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 1755-3245 |
| ispartof | Cardiovascular research, 2014-03, Vol.101 (3), p.393-399 |
| issn | 1755-3245 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Cells, Cultured Extracellular Matrix - metabolism Extracellular Matrix Proteins - pharmacology Gene Expression Regulation Heart - drug effects Heart Failure - metabolism Humans In Situ Hybridization - methods Oxidation-Reduction - drug effects Peroxidase - pharmacology Peroxidasin RNA, Messenger - metabolism |
| title | Peroxidasin-like protein: a novel peroxidase homologue in the human heart |
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