Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors
Identifieur interne : 001F95 ( Istex/Corpus ); précédent : 001F94; suivant : 001F96Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors
Auteurs : M. Mokotoff ; D. P. Swanson ; S. S. Jonnalagadda ; M. W. Epperly ; M. L. BrownSource :
- The Journal of Peptide Research [ 1397-002X ] ; 1997-06.
English descriptors
- KwdEn :
- Animal model, Basement membranes, Biodistribution, Brain blood heart lung liver spleen stomach, Carcinoma, Cell attachment, Cell biol, Cleavage, Corresponding monomer, Dimer, Dtpa, Dtpa dianhydride, Female mice, Functional site, General procedure, Hplc, Hplc purification, Kaiser ninhydrin test, Kidney ovary skin muscle bone, Kleinman, Laminin, Laminin peptide fragments, Laminin receptor, Linear gradient, Malignant, Malignant cells, Malignant tumors, Mammary tumor model, Mbha resin, Melanoma cells, Mokotoff, Negative control, Other organs, Peptide, Pharmaceutical sciences, Polymeric form, Potential detection, Radiolabeled, Radiolabeled dimer, Radiolabeled peptides, Receptor, Room temperature, Selective removal, Specific activity, Steroid receptor, Tissue distribution, Tumor localization, Yigsr peptides.
- Teeft :
- Animal model, Basement membranes, Biodistribution, Brain blood heart lung liver spleen stomach, Carcinoma, Cell attachment, Cell biol, Cleavage, Corresponding monomer, Dimer, Dtpa, Dtpa dianhydride, Female mice, Functional site, General procedure, Hplc, Hplc purification, Kaiser ninhydrin test, Kidney ovary skin muscle bone, Kleinman, Laminin, Laminin peptide fragments, Laminin receptor, Linear gradient, Malignant, Malignant cells, Malignant tumors, Mammary tumor model, Mbha resin, Melanoma cells, Mokotoff, Negative control, Other organs, Peptide, Pharmaceutical sciences, Polymeric form, Potential detection, Radiolabeled, Radiolabeled dimer, Radiolabeled peptides, Receptor, Room temperature, Selective removal, Specific activity, Steroid receptor, Tissue distribution, Tumor localization, Yigsr peptides.
Abstract
The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.
Url:
DOI: 10.1111/j.1399-3011.1997.tb01158.x
Links to Exploration step
ISTEX:89199FC0B0E87F193856CC8C3C9D62B5F7F99997Le document en format XML
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Brown</name><affiliation><mods:affiliation>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Peptide Research</title><title level="j" type="alt">JOURNAL OF PEPTIDE RESEARCH</title><idno type="ISSN">1397-002X</idno><idno type="eISSN">1399-3011</idno><imprint><biblScope unit="vol">49</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="510">510</biblScope><biblScope unit="page" to="516">516</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-06">1997-06</date></imprint><idno type="ISSN">1397-002X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1397-002X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animal model</term><term>Basement membranes</term><term>Biodistribution</term><term>Brain blood heart lung liver spleen stomach</term><term>Carcinoma</term><term>Cell attachment</term><term>Cell biol</term><term>Cleavage</term><term>Corresponding monomer</term><term>Dimer</term><term>Dtpa</term><term>Dtpa dianhydride</term><term>Female mice</term><term>Functional site</term><term>General procedure</term><term>Hplc</term><term>Hplc purification</term><term>Kaiser ninhydrin test</term><term>Kidney ovary skin muscle bone</term><term>Kleinman</term><term>Laminin</term><term>Laminin peptide fragments</term><term>Laminin receptor</term><term>Linear gradient</term><term>Malignant</term><term>Malignant cells</term><term>Malignant tumors</term><term>Mammary tumor model</term><term>Mbha resin</term><term>Melanoma cells</term><term>Mokotoff</term><term>Negative control</term><term>Other organs</term><term>Peptide</term><term>Pharmaceutical sciences</term><term>Polymeric form</term><term>Potential detection</term><term>Radiolabeled</term><term>Radiolabeled dimer</term><term>Radiolabeled peptides</term><term>Receptor</term><term>Room temperature</term><term>Selective removal</term><term>Specific activity</term><term>Steroid receptor</term><term>Tissue distribution</term><term>Tumor localization</term><term>Yigsr peptides</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Animal model</term><term>Basement membranes</term><term>Biodistribution</term><term>Brain blood heart lung liver spleen stomach</term><term>Carcinoma</term><term>Cell attachment</term><term>Cell biol</term><term>Cleavage</term><term>Corresponding monomer</term><term>Dimer</term><term>Dtpa</term><term>Dtpa dianhydride</term><term>Female mice</term><term>Functional site</term><term>General procedure</term><term>Hplc</term><term>Hplc purification</term><term>Kaiser ninhydrin test</term><term>Kidney ovary skin muscle bone</term><term>Kleinman</term><term>Laminin</term><term>Laminin peptide fragments</term><term>Laminin receptor</term><term>Linear gradient</term><term>Malignant</term><term>Malignant cells</term><term>Malignant tumors</term><term>Mammary tumor model</term><term>Mbha resin</term><term>Melanoma cells</term><term>Mokotoff</term><term>Negative control</term><term>Other organs</term><term>Peptide</term><term>Pharmaceutical sciences</term><term>Polymeric form</term><term>Potential detection</term><term>Radiolabeled</term><term>Radiolabeled dimer</term><term>Radiolabeled peptides</term><term>Receptor</term><term>Room temperature</term><term>Selective removal</term><term>Specific activity</term><term>Steroid receptor</term><term>Tissue distribution</term><term>Tumor localization</term><term>Yigsr peptides</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>peptide</json:string><json:string>receptor</json:string><json:string>laminin</json:string><json:string>dtpa</json:string><json:string>radiolabeled</json:string><json:string>kleinman</json:string><json:string>hplc</json:string><json:string>mokotoff</json:string><json:string>malignant</json:string><json:string>dimer</json:string><json:string>biodistribution</json:string><json:string>laminin peptide fragments</json:string><json:string>laminin receptor</json:string><json:string>room temperature</json:string><json:string>tissue distribution</json:string><json:string>malignant tumors</json:string><json:string>specific activity</json:string><json:string>carcinoma</json:string><json:string>negative control</json:string><json:string>dtpa dianhydride</json:string><json:string>radiolabeled peptides</json:string><json:string>tumor localization</json:string><json:string>female mice</json:string><json:string>kidney ovary skin muscle bone</json:string><json:string>mbha resin</json:string><json:string>linear gradient</json:string><json:string>animal model</json:string><json:string>other organs</json:string><json:string>pharmaceutical sciences</json:string><json:string>general procedure</json:string><json:string>basement membranes</json:string><json:string>kaiser ninhydrin test</json:string><json:string>selective removal</json:string><json:string>cell attachment</json:string><json:string>malignant cells</json:string><json:string>hplc purification</json:string><json:string>cell biol</json:string><json:string>steroid receptor</json:string><json:string>melanoma cells</json:string><json:string>yigsr peptides</json:string><json:string>polymeric form</json:string><json:string>mammary tumor model</json:string><json:string>brain blood heart lung liver spleen stomach</json:string><json:string>functional site</json:string><json:string>radiolabeled dimer</json:string><json:string>corresponding monomer</json:string><json:string>potential detection</json:string><json:string>cleavage</json:string></teeft></keywords><author><json:item><name>M. MOKOTOFF</name><affiliations><json:string>Departments ofPharmaceutical Sciences University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</json:string></affiliations></json:item><json:item><name>D.P. SWANSON</name><affiliations><json:string>Pharmacy and Therapeutics, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</json:string><json:string>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</json:string></affiliations></json:item><json:item><name>S.S. JONNALAGADDA</name><affiliations><json:string>Departments ofPharmaceutical Sciences University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</json:string></affiliations></json:item><json:item><name>M.W. EPPERLY</name><affiliations><json:string>Radiation Oncology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA</json:string></affiliations></json:item><json:item><name>M.L. BROWN</name><affiliations><json:string>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>indium‐111</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>laminin peptide fragments</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>imaging</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>chelation of indium‐111</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DTPA peptides</value></json:item></subject><articleId><json:string>CBDD510</json:string></articleId><arkIstex>ark:/67375/WNG-GKN7J915-T</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</abstract><qualityIndicators><score>7.504</score><pdfWordCount>4148</pdfWordCount><pdfCharCount>26724</pdfCharCount><pdfVersion>1.4</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>586.8 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>113</abstractWordCount><abstractCharCount>840</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors</title><genre><json:string>article</json:string></genre><host><title>The Journal of Peptide Research</title><language><json:string>unknown</json:string></language><doi><json:string>10.1111/(ISSN)1399-3011</json:string></doi><issn><json:string>1397-002X</json:string></issn><eissn><json:string>1399-3011</json:string></eissn><publisherId><json:string>CBDD</json:string></publisherId><volume>49</volume><issue>6</issue><pages><first>510</first><last>516</last><total>7</total></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1997</json:string><json:string>70s</json:string></date><geogName></geogName><orgName><json:string>Department of Pharmaceutical Sciences, Schc</json:string><json:string>B Diagnostics</json:string><json:string>University of Pittsburgh</json:string><json:string>Department of Radiology, School of Med</json:string><json:string>University of Pittsburgh Medical Center</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Mono</json:string><json:string>M. Mokotoff</json:string><json:string>Massia</json:string><json:string>Bernard Fisher</json:string></persName><placeName><json:string>Pittsburgh</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>M. Mokotoff et al.</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/WNG-GKN7J915-T</json:string></ark><categories><wos></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biophysics</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Endocrinology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string><json:string>4 - radiotherapie. traitement instrumental. physiotherapie. reeducation. readaptation, orthophonie, crenotherapie. traitement dietetique et traitements divers (generalites)</json:string></inist></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1111/j.1399-3011.1997.tb01158.x</json:string></doi><id>89199FC0B0E87F193856CC8C3C9D62B5F7F99997</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/89199FC0B0E87F193856CC8C3C9D62B5F7F99997/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/89199FC0B0E87F193856CC8C3C9D62B5F7F99997/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/89199FC0B0E87F193856CC8C3C9D62B5F7F99997/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant 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key="US"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">D.P.</forename><surname>SWANSON</surname></persName><affiliation>Pharmacy and Therapeutics, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania, USA and<address><country key="US"></country></address></affiliation><affiliation>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and<address><country key="US"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">S.S.</forename><surname>JONNALAGADDA</surname></persName><affiliation>Departments ofPharmaceutical Sciences University of Pittsburgh, Pittsburgh, Pennsylvania, USA and<address><country key="US"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">M.W.</forename><surname>EPPERLY</surname></persName><affiliation>Radiation Oncology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">M.L.</forename><surname>BROWN</surname></persName><affiliation>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and<address><country key="US"></country></address></affiliation></author><idno type="istex">89199FC0B0E87F193856CC8C3C9D62B5F7F99997</idno><idno type="ark">ark:/67375/WNG-GKN7J915-T</idno><idno type="DOI">10.1111/j.1399-3011.1997.tb01158.x</idno><idno type="unit">CBDD510</idno><idno type="toTypesetVersion">file:CBDD.CBDD510.pdf</idno></analytic><monogr><title level="j" type="main">The Journal of Peptide Research</title><title level="j" type="alt">JOURNAL OF PEPTIDE RESEARCH</title><idno type="pISSN">1397-002X</idno><idno type="eISSN">1399-3011</idno><idno type="book-DOI">10.1111/(ISSN)1399-3011</idno><idno type="book-part-DOI">10.1111/jpp.1997.49.issue-6</idno><idno type="product">CBDD</idno><idno type="publisherDivision">ST</idno><imprint><biblScope unit="vol">49</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="510">510</biblScope><biblScope unit="page" to="516">516</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-06"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><p>The laminin peptide fragments GYIGSR‐NH<hi rend="superscript">2</hi> and CDPGYIGSR‐NH<hi rend="superscript">2</hi> are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH<hi rend="superscript">2</hi> (1), DTPA‐(GYIGSR‐NH<hi rend="superscript">2</hi>)<hi rend="superscript">2</hi> (2), DTPA‐CDPGYIGSR‐NH<hi rend="superscript">2</hi> (3), DTPA‐(CDPGYIGSR‐NH<hi rend="superscript">2</hi>)<hi rend="superscript">2</hi> (4), and negative control DTPA‐GAGAGA‐NH<hi rend="superscript">2</hi> (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with <hi rend="superscript">111</hi>ln and their tissue distribution evaluated in mice bearing C3H tumors. <hi rend="superscript">111</hi>In‐3 and <hi rend="superscript">111</hi>In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">indium‐111</term><term xml:id="k2">laminin peptide fragments</term><term xml:id="k3">imaging</term><term xml:id="k4">chelation of indium‐111</term><term xml:id="k5">DTPA peptides</term></keywords><keywords rend="tocHeading1"><term>Article</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/89199FC0B0E87F193856CC8C3C9D62B5F7F99997/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" 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level="unit" type="article" position="0051000" status="forIssue"><doi origin="wiley">10.1111/j.1399-3011.1997.tb01158.x</doi><idGroup><id type="unit" value="CBDD510"></id></idGroup><countGroup><count type="pageTotal" number="7"></count></countGroup><titleGroup><title type="tocHeading1">Article</title></titleGroup><eventGroup><event type="firstOnline" date="2009-01-12"></event><event type="publishedOnlineFinalForm" date="2009-01-12"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-04"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-04"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="510">510</numbering><numbering type="pageLast" number="516">516</numbering></numberingGroup><linkGroup><link type="toTypesetVersion" href="file:CBDD.CBDD510.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 30 August, revised 1 November 1996, accepted for publication 18 January 1997</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="41"></count><count type="linksCrossRef" number="6"></count></countGroup><titleGroup><title type="main">Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>M.</givenNames><familyName>MOKOTOFF</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a2 #a3"><personName><givenNames>D.P.</givenNames><familyName>SWANSON</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a1"><personName><givenNames>S.S.</givenNames><familyName>JONNALAGADDA</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a4"><personName><givenNames>M.W.</givenNames><familyName>EPPERLY</familyName></personName></creator><creator creatorRole="author" xml:id="cr5" affiliationRef="#a3"><personName><givenNames>M.L.</givenNames><familyName>BROWN</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="US"><unparsedAffiliation>Departments ofPharmaceutical Sciences University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="US"><unparsedAffiliation>Pharmacy and Therapeutics, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</unparsedAffiliation></affiliation><affiliation xml:id="a3" countryCode="US"><unparsedAffiliation>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</unparsedAffiliation></affiliation><affiliation xml:id="a4" countryCode="US"><unparsedAffiliation>Radiation Oncology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">indium‐111</keyword><keyword xml:id="k2">laminin peptide fragments</keyword><keyword xml:id="k3">imaging</keyword><keyword xml:id="k4">chelation of indium‐111</keyword><keyword xml:id="k5">DTPA peptides</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>The laminin peptide fragments GYIGSR‐NH<sup>2</sup> and CDPGYIGSR‐NH<sup>2</sup> are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH<sup>2</sup> (1), DTPA‐(GYIGSR‐NH<sup>2</sup>)<sup>2</sup> (2), DTPA‐CDPGYIGSR‐NH<sup>2</sup> (3), DTPA‐(CDPGYIGSR‐NH<sup>2</sup>)<sup>2</sup> (4), and negative control DTPA‐GAGAGA‐NH<sup>2</sup> (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with <sup>111</sup>ln and their tissue distribution evaluated in mice bearing C3H tumors. <sup>111</sup>In‐3 and <sup>111</sup>In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors</title></titleInfo><name type="personal"><namePart type="given">M.</namePart><namePart type="family">MOKOTOFF</namePart><affiliation>Departments ofPharmaceutical Sciences University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">D.P.</namePart><namePart type="family">SWANSON</namePart><affiliation>Pharmacy and Therapeutics, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</affiliation><affiliation>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.S.</namePart><namePart type="family">JONNALAGADDA</namePart><affiliation>Departments ofPharmaceutical Sciences University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.W.</namePart><namePart type="family">EPPERLY</namePart><affiliation>Radiation Oncology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.L.</namePart><namePart type="family">BROWN</namePart><affiliation>Departments of Radiology University of Pittsburgh, Pittsburgh, Pennsylvania, USA and</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1997-06</dateIssued><edition>Received 30 August, revised 1 November 1996, accepted for publication 18 January 1997</edition><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="references">41</extent><extent unit="linksCrossRef">6</extent></physicalDescription><abstract lang="en">The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</abstract><subject lang="en"><genre>keywords</genre><topic>indium‐111</topic><topic>laminin peptide fragments</topic><topic>imaging</topic><topic>chelation of indium‐111</topic><topic>DTPA peptides</topic></subject><relatedItem type="host"><titleInfo><title>The Journal of Peptide Research</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">1397-002X</identifier><identifier type="eISSN">1399-3011</identifier><identifier type="DOI">10.1111/(ISSN)1399-3011</identifier><identifier type="PublisherID">CBDD</identifier><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>49</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>510</start><end>516</end><total>7</total></extent></part></relatedItem><identifier type="istex">89199FC0B0E87F193856CC8C3C9D62B5F7F99997</identifier><identifier type="ark">ark:/67375/WNG-GKN7J915-T</identifier><identifier type="DOI">10.1111/j.1399-3011.1997.tb01158.x</identifier><identifier type="ArticleID">CBDD510</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/89199FC0B0E87F193856CC8C3C9D62B5F7F99997/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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