Attenuation of Parasite cAMP Levels in T. cruzi‐Host Cell Membrane Interactions In Vitro
Identifieur interne : 001861 ( Istex/Corpus ); précédent : 001860; suivant : 001862Attenuation of Parasite cAMP Levels in T. cruzi‐Host Cell Membrane Interactions In Vitro
Auteurs : Betsy F. Von Kreuter ; Beth L. Walton ; Charles A. Santos UchSource :
- Journal of Eukaryotic Microbiology [ 1066-5234 ] ; 1995-01.
English descriptors
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Abstract
Previous investigations have shown that the adhesion of T. cruzi plasma membrane vesicles (PMV) to monolayers of host cell myoblasts and to immobilized heart muscle sarcolemma membranes (PAM) on polyaerylamide beads is mediated by the interaction of T. cruzi attachment sites with the muscarinic cholinergic and β‐adrenergic receptors of the host cell membrane. It has also been shown that this interaction is blunted by the specific antagonists of the mammalian receptors atropine and propranol, respectively. In the studies reported here, PAM also rapidly attached to swimming T. cruzi trypomastigotes in a complex, concentration‐dependent fashion and binding isotherms showed that the equilibrium between free and bound PAM is rapidly reached within 2 minutes of incubation in physiologically balanced salt solutions. In this time frame, trypomastigote cAMP levels are significantly reduced from steady state values within 30 seconds of the addition of PAM in a buffer system containing a diesterase inhibitor. Maximal attenuation of cAMP levels was measured between 1 and 2 minutes of the addition of PAM to T. cruzi trypomastigotes. The degree of cAMP level attenuation was reduced by blocking PAM attachment with either atropine or propranol. On the basis of these results we propose that a likely pathway for the negative parasite signal generated upon adhesion of host muscle cell membranes to the surface of the flagellates is from the parasite's surface attachment sites directly to a Pertussis toxin sensitive inhibitory protein Gi, thereby blunting adenyl cyclase activity and cAMP formation.
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DOI: 10.1111/j.1550-7408.1995.tb01535.x
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It has also been shown that this interaction is blunted by the specific antagonists of the mammalian receptors atropine and propranol, respectively. In the studies reported here, PAM also rapidly attached to swimming T. cruzi trypomastigotes in a complex, concentration‐dependent fashion and binding isotherms showed that the equilibrium between free and bound PAM is rapidly reached within 2 minutes of incubation in physiologically balanced salt solutions. In this time frame, trypomastigote cAMP levels are significantly reduced from steady state values within 30 seconds of the addition of PAM in a buffer system containing a diesterase inhibitor. Maximal attenuation of cAMP levels was measured between 1 and 2 minutes of the addition of PAM to T. cruzi trypomastigotes. The degree of cAMP level attenuation was reduced by blocking PAM attachment with either atropine or propranol. On the basis of these results we propose that a likely pathway for the negative parasite signal generated upon adhesion of host muscle cell membranes to the surface of the flagellates is from the parasite's surface attachment sites directly to a Pertussis toxin sensitive inhibitory protein Gi, thereby blunting adenyl cyclase activity and cAMP formation.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>BETSY F. VON KREUTER</name><affiliations><json:string>Department of Pathology, Cornell University Medical College, 1300 York Avenue, New York, New York 10021</json:string></affiliations></json:item><json:item><name>BETH L. WALTON</name><affiliations><json:string>Department of Pathology, Cornell University Medical College, 1300 York Avenue, New York, New York 10021</json:string></affiliations></json:item><json:item><name>CHARLES A. 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It has also been shown that this interaction is blunted by the specific antagonists of the mammalian receptors atropine and propranol, respectively. In the studies reported here, PAM also rapidly attached to swimming T. cruzi trypomastigotes in a complex, concentration‐dependent fashion and binding isotherms showed that the equilibrium between free and bound PAM is rapidly reached within 2 minutes of incubation in physiologically balanced salt solutions. In this time frame, trypomastigote cAMP levels are significantly reduced from steady state values within 30 seconds of the addition of PAM in a buffer system containing a diesterase inhibitor. Maximal attenuation of cAMP levels was measured between 1 and 2 minutes of the addition of PAM to T. cruzi trypomastigotes. The degree of cAMP level attenuation was reduced by blocking PAM attachment with either atropine or propranol. 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It has also been shown that this interaction is blunted by the specific antagonists of the mammalian receptors atropine and propranol, respectively. In the studies reported here, PAM also rapidly attached to swimming T. cruzi trypomastigotes in a complex, concentration‐dependent fashion and binding isotherms showed that the equilibrium between free and bound PAM is rapidly reached within 2 minutes of incubation in physiologically balanced salt solutions. In this time frame, trypomastigote cAMP levels are significantly reduced from steady state values within 30 seconds of the addition of PAM in a buffer system containing a diesterase inhibitor. Maximal attenuation of cAMP levels was measured between 1 and 2 minutes of the addition of PAM to T. cruzi trypomastigotes. The degree of cAMP level attenuation was reduced by blocking PAM attachment with either atropine or propranol. On the basis of these results we propose that a likely pathway for the negative parasite signal generated upon adhesion of host muscle cell membranes to the surface of the flagellates is from the parasite's surface attachment sites directly to a Pertussis toxin sensitive inhibitory protein Gi, thereby blunting adenyl cyclase activity and cAMP formation.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Chagas</term></item><item><term>heart cell</term></item><item><term>protein G</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/BDCC28441E254C6FF38C811A88ADCECDCBBF7B1F/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1550-7408</doi><issn type="print">1066-5234</issn><issn type="electronic">1550-7408</issn><idGroup><id type="product" value="JEU"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="JOURNAL OF EUKARYOTIC MICROBIOLOGY">Journal of Eukaryotic Microbiology</title></titleGroup></publicationMeta><publicationMeta level="part" position="01001"><doi origin="wiley">10.1111/jeu.1995.42.issue-1</doi><numberingGroup><numbering type="journalVolume" number="42">42</numbering><numbering type="journalIssue" number="1">1</numbering></numberingGroup><coverDate startDate="1995-01">January 1995</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0002000" status="forIssue"><doi origin="wiley">10.1111/j.1550-7408.1995.tb01535.x</doi><idGroup><id type="unit" value="JEU20"></id></idGroup><countGroup><count type="pageTotal" number="7"></count></countGroup><eventGroup><event type="firstOnline" date="2007-05-01"></event><event type="publishedOnlineFinalForm" date="2007-05-01"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.6 mode:FullText source:HeaderRef result:HeaderRef" date="2010-04-20"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-30"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-30"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="20">20</numbering><numbering type="pageLast" number="26">26</numbering></numberingGroup><correspondenceTo>To whom correspondence should be addressed.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JEU.JEU20.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 1‐12‐94, 3‐28‐94, 7‐13‐94; accepted 8‐8‐94</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="21"></count><count type="linksCrossRef" number="4"></count></countGroup><titleGroup><title type="main">Attenuation of Parasite cAMP Levels in <i>T. cruzi</i>‐Host Cell Membrane Interactions In Vitro</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>BETSY F.</givenNames><familyNamePrefix>VON</familyNamePrefix><familyName>KREUTER</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>BETH L.</givenNames><familyName>WALTON</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a1" corresponding="yes"><personName><givenNames>CHARLES A.</givenNames><familyName>SANTOS‐BUCH</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="US"><unparsedAffiliation>Department of Pathology, Cornell University Medical College, 1300 York Avenue, New York, New York 10021</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">Chagas</keyword><keyword xml:id="k2">heart cell</keyword><keyword xml:id="k3">protein G</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">ABSTRACT</title><p>Previous investigations have shown that the adhesion of <i>T. cruzi</i> plasma membrane vesicles (PMV) to monolayers of host cell myoblasts and to immobilized heart muscle sarcolemma membranes (PAM) on polyaerylamide beads is mediated by the interaction of <i>T. cruzi</i> attachment sites with the muscarinic cholinergic and β‐adrenergic receptors of the host cell membrane. It has also been shown that this interaction is blunted by the specific antagonists of the mammalian receptors atropine and propranol, respectively. In the studies reported here, PAM also rapidly attached to swimming <i>T. cruzi</i> trypomastigotes in a complex, concentration‐dependent fashion and binding isotherms showed that the equilibrium between free and bound PAM is rapidly reached within 2 minutes of incubation in physiologically balanced salt solutions. In this time frame, trypomastigote cAMP levels are significantly reduced from steady state values within 30 seconds of the addition of PAM in a buffer system containing a diesterase inhibitor. Maximal attenuation of cAMP levels was measured between 1 and 2 minutes of the addition of PAM to <i>T. cruzi</i> trypomastigotes. The degree of cAMP level attenuation was reduced by blocking PAM attachment with either atropine or propranol. On the basis of these results we propose that a likely pathway for the negative parasite signal generated upon adhesion of host muscle cell membranes to the surface of the flagellates is from the parasite's surface attachment sites directly to a Pertussis toxin sensitive inhibitory protein G<sub>i</sub>, thereby blunting adenyl cyclase activity and cAMP formation.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Attenuation of Parasite cAMP Levels in T. cruzi‐Host Cell Membrane Interactions In Vitro</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Attenuation of Parasite cAMP Levels in</title></titleInfo><name type="personal"><namePart type="given">BETSY F.</namePart><namePart type="family">VON KREUTER</namePart><affiliation>Department of Pathology, Cornell University Medical College, 1300 York Avenue, New York, New York 10021</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">BETH L.</namePart><namePart type="family">WALTON</namePart><affiliation>Department of Pathology, Cornell University Medical College, 1300 York Avenue, New York, New York 10021</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">CHARLES A.</namePart><namePart type="family">SANTOS‐BUCH</namePart><affiliation>Department of Pathology, Cornell University Medical College, 1300 York Avenue, New York, New York 10021</affiliation><description>Correspondence: To whom correspondence should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1995-01</dateIssued><edition>Received 1‐12‐94, 3‐28‐94, 7‐13‐94; accepted 8‐8‐94</edition><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="references">21</extent></physicalDescription><abstract lang="en">Previous investigations have shown that the adhesion of T. cruzi plasma membrane vesicles (PMV) to monolayers of host cell myoblasts and to immobilized heart muscle sarcolemma membranes (PAM) on polyaerylamide beads is mediated by the interaction of T. cruzi attachment sites with the muscarinic cholinergic and β‐adrenergic receptors of the host cell membrane. It has also been shown that this interaction is blunted by the specific antagonists of the mammalian receptors atropine and propranol, respectively. In the studies reported here, PAM also rapidly attached to swimming T. cruzi trypomastigotes in a complex, concentration‐dependent fashion and binding isotherms showed that the equilibrium between free and bound PAM is rapidly reached within 2 minutes of incubation in physiologically balanced salt solutions. In this time frame, trypomastigote cAMP levels are significantly reduced from steady state values within 30 seconds of the addition of PAM in a buffer system containing a diesterase inhibitor. Maximal attenuation of cAMP levels was measured between 1 and 2 minutes of the addition of PAM to T. cruzi trypomastigotes. The degree of cAMP level attenuation was reduced by blocking PAM attachment with either atropine or propranol. On the basis of these results we propose that a likely pathway for the negative parasite signal generated upon adhesion of host muscle cell membranes to the surface of the flagellates is from the parasite's surface attachment sites directly to a Pertussis toxin sensitive inhibitory protein Gi, thereby blunting adenyl cyclase activity and cAMP formation.</abstract><subject lang="en"><genre>Keywords</genre><topic>Chagas</topic><topic>heart cell</topic><topic>protein G</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Eukaryotic Microbiology</title></titleInfo><genre type="Journal">journal</genre><identifier type="ISSN">1066-5234</identifier><identifier type="eISSN">1550-7408</identifier><identifier type="DOI">10.1111/(ISSN)1550-7408</identifier><identifier type="PublisherID">JEU</identifier><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>42</number></detail><detail type="issue"><caption>no.</caption><number>1</number></detail><extent unit="pages"><start>20</start><end>26</end><total>7</total></extent></part></relatedItem><identifier type="istex">BDCC28441E254C6FF38C811A88ADCECDCBBF7B1F</identifier><identifier type="DOI">10.1111/j.1550-7408.1995.tb01535.x</identifier><identifier type="ArticleID">JEU20</identifier><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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