Loading…

Cloning and Cellular Distribution of a Group II Phospholipase A2Expressed in the Heart

Phospholipase A2has been considered to play a role in physiological membrane turnover in cardiac tissue and in the degradation of membrane lipids under pathophysiological conditions, such as ischemia and reperfusion. We report the cloning of a cDNA encoding a member of the Ca2+-dependent, low molecu...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular and cellular cardiology 1997-08, Vol.29 (8), p.2095-2106
Main Authors: De Windt, Leon J., Willemsen, Peter H.M., Pöpping, Stephanie, Van der Vusse, Ger J., Reneman, Robert S., Van Bilsen, Marc
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c1334-5543439627ae91e59553bdd93e1462f043060b546c4d9554a44a8a455bc5e0f33
cites
container_end_page 2106
container_issue 8
container_start_page 2095
container_title Journal of molecular and cellular cardiology
container_volume 29
creator De Windt, Leon J.
Willemsen, Peter H.M.
Pöpping, Stephanie
Van der Vusse, Ger J.
Reneman, Robert S.
Van Bilsen, Marc
description Phospholipase A2has been considered to play a role in physiological membrane turnover in cardiac tissue and in the degradation of membrane lipids under pathophysiological conditions, such as ischemia and reperfusion. We report the cloning of a cDNA encoding a member of the Ca2+-dependent, low molecular mass phospholipase A2(PLA2) present in rat heart. The cDNA predicts a mature protein of 146 amino acid residues including a 21 amino acid sequence at the N-terminal end, which has the features characteristic of eukaryotic secretory signal peptides. The deduced amino acid sequence constitutes an enzyme of the group II class of PLA2s, and resembles PLA2s from other mammalian sources. A Northern blot analysis performed to determine the tissue distribution showed that rat ileum contains the largest amount of the PLA2transcript among the tissues examined, a weaker signal was present in heart, spleen and soleus muscle, and no signal could be detected in EDL muscle, stomach, liver, kidney, brain and lung. Northern blot analysis and reverse transcriptase–polymerase chain reaction (RT–PCR) techniques indicate the presence of this enzyme in neonatal and adult rat cardiomyocytes and in a cultured rat cardiac fibroblast-like cell line, but not in rat cardiac-derived endothelial cell lines. Transcription levels of rat heart group II PLA2in isolated neonatal rat cardiomyocytes were found to increase after stimulating the cells with tumor necrosis factor-α(TNF-α) or theα1-adrenergic agonist phenylephrine.
doi_str_mv 10.1006/jmcc.1997.0444
format article
fullrecord <record><control><sourceid>elsevier_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1006_jmcc_1997_0444</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022282897904442</els_id><sourcerecordid>S0022282897904442</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1334-5543439627ae91e59553bdd93e1462f043060b546c4d9554a44a8a455bc5e0f33</originalsourceid><addsrcrecordid>eNp1kD1PwzAURS0EEqWwMvsPJPjjOY3HKpS2EhIMwGo5zgt1lcaRnSL49zQqK9Mdrs7V1SHknrOcM1Y87A_O5VzrRc4A4ILMONMqK1UJl2TGmBCZKEV5TW5S2jPGNEg5Ix9VF3rff1LbN7TCrjt2NtJHn8bo6-PoQ09DSy1dx3Ac6HZLX3chDbvQ-cEmpEux-h4ipoQN9T0dd0g3aON4S65a2yW8-8s5eX9avVWb7Pllva2Wz5njUkKmFEiQuhALi5qj0krJumm0RA6FaBlIVrBaQeGgOXVgAWxpQanaKWStlHOSn3ddDClFbM0Q_cHGH8OZmayYyYqZrJjJygkozwCeXn15jCY5j73Dxkd0o2mC_w_9BVIrZ4k</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Cloning and Cellular Distribution of a Group II Phospholipase A2Expressed in the Heart</title><source>ScienceDirect Freedom Collection</source><creator>De Windt, Leon J. ; Willemsen, Peter H.M. ; Pöpping, Stephanie ; Van der Vusse, Ger J. ; Reneman, Robert S. ; Van Bilsen, Marc</creator><creatorcontrib>De Windt, Leon J. ; Willemsen, Peter H.M. ; Pöpping, Stephanie ; Van der Vusse, Ger J. ; Reneman, Robert S. ; Van Bilsen, Marc</creatorcontrib><description>Phospholipase A2has been considered to play a role in physiological membrane turnover in cardiac tissue and in the degradation of membrane lipids under pathophysiological conditions, such as ischemia and reperfusion. We report the cloning of a cDNA encoding a member of the Ca2+-dependent, low molecular mass phospholipase A2(PLA2) present in rat heart. The cDNA predicts a mature protein of 146 amino acid residues including a 21 amino acid sequence at the N-terminal end, which has the features characteristic of eukaryotic secretory signal peptides. The deduced amino acid sequence constitutes an enzyme of the group II class of PLA2s, and resembles PLA2s from other mammalian sources. A Northern blot analysis performed to determine the tissue distribution showed that rat ileum contains the largest amount of the PLA2transcript among the tissues examined, a weaker signal was present in heart, spleen and soleus muscle, and no signal could be detected in EDL muscle, stomach, liver, kidney, brain and lung. Northern blot analysis and reverse transcriptase–polymerase chain reaction (RT–PCR) techniques indicate the presence of this enzyme in neonatal and adult rat cardiomyocytes and in a cultured rat cardiac fibroblast-like cell line, but not in rat cardiac-derived endothelial cell lines. Transcription levels of rat heart group II PLA2in isolated neonatal rat cardiomyocytes were found to increase after stimulating the cells with tumor necrosis factor-α(TNF-α) or theα1-adrenergic agonist phenylephrine.</description><identifier>ISSN: 0022-2828</identifier><identifier>EISSN: 1095-8584</identifier><identifier>DOI: 10.1006/jmcc.1997.0444</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Cloning ; Group II phospholipase A2 ; Ischemia/reperfusion ; Phenylephrine ; Phospholipids ; TNF-α</subject><ispartof>Journal of molecular and cellular cardiology, 1997-08, Vol.29 (8), p.2095-2106</ispartof><rights>1997 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1334-5543439627ae91e59553bdd93e1462f043060b546c4d9554a44a8a455bc5e0f33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>De Windt, Leon J.</creatorcontrib><creatorcontrib>Willemsen, Peter H.M.</creatorcontrib><creatorcontrib>Pöpping, Stephanie</creatorcontrib><creatorcontrib>Van der Vusse, Ger J.</creatorcontrib><creatorcontrib>Reneman, Robert S.</creatorcontrib><creatorcontrib>Van Bilsen, Marc</creatorcontrib><title>Cloning and Cellular Distribution of a Group II Phospholipase A2Expressed in the Heart</title><title>Journal of molecular and cellular cardiology</title><description>Phospholipase A2has been considered to play a role in physiological membrane turnover in cardiac tissue and in the degradation of membrane lipids under pathophysiological conditions, such as ischemia and reperfusion. We report the cloning of a cDNA encoding a member of the Ca2+-dependent, low molecular mass phospholipase A2(PLA2) present in rat heart. The cDNA predicts a mature protein of 146 amino acid residues including a 21 amino acid sequence at the N-terminal end, which has the features characteristic of eukaryotic secretory signal peptides. The deduced amino acid sequence constitutes an enzyme of the group II class of PLA2s, and resembles PLA2s from other mammalian sources. A Northern blot analysis performed to determine the tissue distribution showed that rat ileum contains the largest amount of the PLA2transcript among the tissues examined, a weaker signal was present in heart, spleen and soleus muscle, and no signal could be detected in EDL muscle, stomach, liver, kidney, brain and lung. Northern blot analysis and reverse transcriptase–polymerase chain reaction (RT–PCR) techniques indicate the presence of this enzyme in neonatal and adult rat cardiomyocytes and in a cultured rat cardiac fibroblast-like cell line, but not in rat cardiac-derived endothelial cell lines. Transcription levels of rat heart group II PLA2in isolated neonatal rat cardiomyocytes were found to increase after stimulating the cells with tumor necrosis factor-α(TNF-α) or theα1-adrenergic agonist phenylephrine.</description><subject>Cloning</subject><subject>Group II phospholipase A2</subject><subject>Ischemia/reperfusion</subject><subject>Phenylephrine</subject><subject>Phospholipids</subject><subject>TNF-α</subject><issn>0022-2828</issn><issn>1095-8584</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNp1kD1PwzAURS0EEqWwMvsPJPjjOY3HKpS2EhIMwGo5zgt1lcaRnSL49zQqK9Mdrs7V1SHknrOcM1Y87A_O5VzrRc4A4ILMONMqK1UJl2TGmBCZKEV5TW5S2jPGNEg5Ix9VF3rff1LbN7TCrjt2NtJHn8bo6-PoQ09DSy1dx3Ac6HZLX3chDbvQ-cEmpEux-h4ipoQN9T0dd0g3aON4S65a2yW8-8s5eX9avVWb7Pllva2Wz5njUkKmFEiQuhALi5qj0krJumm0RA6FaBlIVrBaQeGgOXVgAWxpQanaKWStlHOSn3ddDClFbM0Q_cHGH8OZmayYyYqZrJjJygkozwCeXn15jCY5j73Dxkd0o2mC_w_9BVIrZ4k</recordid><startdate>199708</startdate><enddate>199708</enddate><creator>De Windt, Leon J.</creator><creator>Willemsen, Peter H.M.</creator><creator>Pöpping, Stephanie</creator><creator>Van der Vusse, Ger J.</creator><creator>Reneman, Robert S.</creator><creator>Van Bilsen, Marc</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>199708</creationdate><title>Cloning and Cellular Distribution of a Group II Phospholipase A2Expressed in the Heart</title><author>De Windt, Leon J. ; Willemsen, Peter H.M. ; Pöpping, Stephanie ; Van der Vusse, Ger J. ; Reneman, Robert S. ; Van Bilsen, Marc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1334-5543439627ae91e59553bdd93e1462f043060b546c4d9554a44a8a455bc5e0f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Cloning</topic><topic>Group II phospholipase A2</topic><topic>Ischemia/reperfusion</topic><topic>Phenylephrine</topic><topic>Phospholipids</topic><topic>TNF-α</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Windt, Leon J.</creatorcontrib><creatorcontrib>Willemsen, Peter H.M.</creatorcontrib><creatorcontrib>Pöpping, Stephanie</creatorcontrib><creatorcontrib>Van der Vusse, Ger J.</creatorcontrib><creatorcontrib>Reneman, Robert S.</creatorcontrib><creatorcontrib>Van Bilsen, Marc</creatorcontrib><collection>CrossRef</collection><jtitle>Journal of molecular and cellular cardiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Windt, Leon J.</au><au>Willemsen, Peter H.M.</au><au>Pöpping, Stephanie</au><au>Van der Vusse, Ger J.</au><au>Reneman, Robert S.</au><au>Van Bilsen, Marc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Cellular Distribution of a Group II Phospholipase A2Expressed in the Heart</atitle><jtitle>Journal of molecular and cellular cardiology</jtitle><date>1997-08</date><risdate>1997</risdate><volume>29</volume><issue>8</issue><spage>2095</spage><epage>2106</epage><pages>2095-2106</pages><issn>0022-2828</issn><eissn>1095-8584</eissn><abstract>Phospholipase A2has been considered to play a role in physiological membrane turnover in cardiac tissue and in the degradation of membrane lipids under pathophysiological conditions, such as ischemia and reperfusion. We report the cloning of a cDNA encoding a member of the Ca2+-dependent, low molecular mass phospholipase A2(PLA2) present in rat heart. The cDNA predicts a mature protein of 146 amino acid residues including a 21 amino acid sequence at the N-terminal end, which has the features characteristic of eukaryotic secretory signal peptides. The deduced amino acid sequence constitutes an enzyme of the group II class of PLA2s, and resembles PLA2s from other mammalian sources. A Northern blot analysis performed to determine the tissue distribution showed that rat ileum contains the largest amount of the PLA2transcript among the tissues examined, a weaker signal was present in heart, spleen and soleus muscle, and no signal could be detected in EDL muscle, stomach, liver, kidney, brain and lung. Northern blot analysis and reverse transcriptase–polymerase chain reaction (RT–PCR) techniques indicate the presence of this enzyme in neonatal and adult rat cardiomyocytes and in a cultured rat cardiac fibroblast-like cell line, but not in rat cardiac-derived endothelial cell lines. Transcription levels of rat heart group II PLA2in isolated neonatal rat cardiomyocytes were found to increase after stimulating the cells with tumor necrosis factor-α(TNF-α) or theα1-adrenergic agonist phenylephrine.</abstract><pub>Elsevier Ltd</pub><doi>10.1006/jmcc.1997.0444</doi><tpages>12</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0022-2828
ispartof Journal of molecular and cellular cardiology, 1997-08, Vol.29 (8), p.2095-2106
issn 0022-2828
1095-8584
language eng
recordid cdi_crossref_primary_10_1006_jmcc_1997_0444
source ScienceDirect Freedom Collection
subjects Cloning
Group II phospholipase A2
Ischemia/reperfusion
Phenylephrine
Phospholipids
TNF-α
title Cloning and Cellular Distribution of a Group II Phospholipase A2Expressed in the Heart
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T11%3A54%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-elsevier_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cloning%20and%20Cellular%20Distribution%20of%20a%20Group%20II%20Phospholipase%20A2Expressed%20in%20the%20Heart&rft.jtitle=Journal%20of%20molecular%20and%20cellular%20cardiology&rft.au=De%20Windt,%20Leon%20J.&rft.date=1997-08&rft.volume=29&rft.issue=8&rft.spage=2095&rft.epage=2106&rft.pages=2095-2106&rft.issn=0022-2828&rft.eissn=1095-8584&rft_id=info:doi/10.1006/jmcc.1997.0444&rft_dat=%3Celsevier_cross%3ES0022282897904442%3C/elsevier_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c1334-5543439627ae91e59553bdd93e1462f043060b546c4d9554a44a8a455bc5e0f33%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true