A novel approach for the identification of unique tumor vasculature binding peptides using an E. coli peptide display library.
Identifieur interne : 002569 ( PubMed/Curation ); précédent : 002568; suivant : 002570A novel approach for the identification of unique tumor vasculature binding peptides using an E. coli peptide display library.
Auteurs : C K Brown [États-Unis] ; R A Modzelewski ; C S Johnson ; M K WongSource :
- Annals of surgical oncology [ 1068-9265 ] ; 2000.
Descripteurs français
- KwdFr :
- Animaux, Banque de peptides, Carcinome épidermoïde, Cellules 3T3, Cellules cancéreuses en culture, Endothélium (métabolisme), Escherichia coli, Liaison aux protéines, Motifs d'acides aminés, Néovascularisation pathologique (anatomopathologie), Néovascularisation pathologique (métabolisme), Souris, Souris de lignée C3H, Tumeurs (), Tumeurs (anatomopathologie), Tumeurs (métabolisme).
- MESH :
- anatomopathologie : Néovascularisation pathologique, Tumeurs.
- métabolisme : Endothélium, Néovascularisation pathologique, Tumeurs.
- Animaux, Banque de peptides, Carcinome épidermoïde, Cellules 3T3, Cellules cancéreuses en culture, Escherichia coli, Liaison aux protéines, Motifs d'acides aminés, Souris, Souris de lignée C3H, Tumeurs.
English descriptors
- KwdEn :
- 3T3 Cells, Amino Acid Motifs, Animals, Carcinoma, Squamous Cell, Endothelium (metabolism), Escherichia coli, Mice, Mice, Inbred C3H, Neoplasms (blood supply), Neoplasms (metabolism), Neoplasms (pathology), Neovascularization, Pathologic (metabolism), Neovascularization, Pathologic (pathology), Peptide Library, Protein Binding, Tumor Cells, Cultured.
- MESH :
- chemical : Peptide Library.
- blood supply : Neoplasms.
- metabolism : Endothelium, Neoplasms, Neovascularization, Pathologic.
- pathology : Neoplasms, Neovascularization, Pathologic.
- 3T3 Cells, Amino Acid Motifs, Animals, Carcinoma, Squamous Cell, Escherichia coli, Mice, Mice, Inbred C3H, Protein Binding, Tumor Cells, Cultured.
Abstract
Tumor neovascularization is necessary for continued tumor growth and metastasis. During the process of endothelial cell (EC) recruitment and tumor infiltration, specific molecular markers unique for this interaction are expressed on the EC surface. Targeting these molecular markers would, in effect, allow for specific tumor targeting. Tripeptide sequence motifs have previously been reported that will bind to angiogenic tumor ECs. These sequences were identified from in vivo phage peptide display libraries. The purpose of this study was to use a more simplified bacterial peptide display library in an in vitro system to seek out peptide motifs with unique binding to tumor microvasculature.
DOI: 10.1007/s10434-000-0743-0
PubMed: 11129422
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pubmed:11129422Le document en format XML
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<author><name sortKey="Brown, C K" sort="Brown, C K" uniqKey="Brown C" first="C K" last="Brown">C K Brown</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Surgery, University of Chicago, Illinois, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Surgery, University of Chicago, Illinois</wicri:regionArea>
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<author><name sortKey="Modzelewski, R A" sort="Modzelewski, R A" uniqKey="Modzelewski R" first="R A" last="Modzelewski">R A Modzelewski</name>
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<author><name sortKey="Johnson, C S" sort="Johnson, C S" uniqKey="Johnson C" first="C S" last="Johnson">C S Johnson</name>
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<author><name sortKey="Wong, M K" sort="Wong, M K" uniqKey="Wong M" first="M K" last="Wong">M K Wong</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">A novel approach for the identification of unique tumor vasculature binding peptides using an E. coli peptide display library.</title>
<author><name sortKey="Brown, C K" sort="Brown, C K" uniqKey="Brown C" first="C K" last="Brown">C K Brown</name>
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<author><name sortKey="Johnson, C S" sort="Johnson, C S" uniqKey="Johnson C" first="C S" last="Johnson">C S Johnson</name>
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<author><name sortKey="Wong, M K" sort="Wong, M K" uniqKey="Wong M" first="M K" last="Wong">M K Wong</name>
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<series><title level="j">Annals of surgical oncology</title>
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<imprint><date when="2000" type="published">2000</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3T3 Cells</term>
<term>Amino Acid Motifs</term>
<term>Animals</term>
<term>Carcinoma, Squamous Cell</term>
<term>Endothelium (metabolism)</term>
<term>Escherichia coli</term>
<term>Mice</term>
<term>Mice, Inbred C3H</term>
<term>Neoplasms (blood supply)</term>
<term>Neoplasms (metabolism)</term>
<term>Neoplasms (pathology)</term>
<term>Neovascularization, Pathologic (metabolism)</term>
<term>Neovascularization, Pathologic (pathology)</term>
<term>Peptide Library</term>
<term>Protein Binding</term>
<term>Tumor Cells, Cultured</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Banque de peptides</term>
<term>Carcinome épidermoïde</term>
<term>Cellules 3T3</term>
<term>Cellules cancéreuses en culture</term>
<term>Endothélium (métabolisme)</term>
<term>Escherichia coli</term>
<term>Liaison aux protéines</term>
<term>Motifs d'acides aminés</term>
<term>Néovascularisation pathologique (anatomopathologie)</term>
<term>Néovascularisation pathologique (métabolisme)</term>
<term>Souris</term>
<term>Souris de lignée C3H</term>
<term>Tumeurs ()</term>
<term>Tumeurs (anatomopathologie)</term>
<term>Tumeurs (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Peptide Library</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Néovascularisation pathologique</term>
<term>Tumeurs</term>
</keywords>
<keywords scheme="MESH" qualifier="blood supply" xml:lang="en"><term>Neoplasms</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endothelium</term>
<term>Neoplasms</term>
<term>Neovascularization, Pathologic</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endothélium</term>
<term>Néovascularisation pathologique</term>
<term>Tumeurs</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neoplasms</term>
<term>Neovascularization, Pathologic</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>3T3 Cells</term>
<term>Amino Acid Motifs</term>
<term>Animals</term>
<term>Carcinoma, Squamous Cell</term>
<term>Escherichia coli</term>
<term>Mice</term>
<term>Mice, Inbred C3H</term>
<term>Protein Binding</term>
<term>Tumor Cells, Cultured</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Banque de peptides</term>
<term>Carcinome épidermoïde</term>
<term>Cellules 3T3</term>
<term>Cellules cancéreuses en culture</term>
<term>Escherichia coli</term>
<term>Liaison aux protéines</term>
<term>Motifs d'acides aminés</term>
<term>Souris</term>
<term>Souris de lignée C3H</term>
<term>Tumeurs</term>
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<front><div type="abstract" xml:lang="en">Tumor neovascularization is necessary for continued tumor growth and metastasis. During the process of endothelial cell (EC) recruitment and tumor infiltration, specific molecular markers unique for this interaction are expressed on the EC surface. Targeting these molecular markers would, in effect, allow for specific tumor targeting. Tripeptide sequence motifs have previously been reported that will bind to angiogenic tumor ECs. These sequences were identified from in vivo phage peptide display libraries. The purpose of this study was to use a more simplified bacterial peptide display library in an in vitro system to seek out peptide motifs with unique binding to tumor microvasculature.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11129422</PMID>
<DateCompleted><Year>2001</Year>
<Month>02</Month>
<Day>08</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>09</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">1068-9265</ISSN>
<JournalIssue CitedMedium="Print"><Volume>7</Volume>
<Issue>10</Issue>
<PubDate><Year>2000</Year>
<Month>Dec</Month>
</PubDate>
</JournalIssue>
<Title>Annals of surgical oncology</Title>
<ISOAbbreviation>Ann. Surg. Oncol.</ISOAbbreviation>
</Journal>
<ArticleTitle>A novel approach for the identification of unique tumor vasculature binding peptides using an E. coli peptide display library.</ArticleTitle>
<Pagination><MedlinePgn>743-9</MedlinePgn>
</Pagination>
<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Tumor neovascularization is necessary for continued tumor growth and metastasis. During the process of endothelial cell (EC) recruitment and tumor infiltration, specific molecular markers unique for this interaction are expressed on the EC surface. Targeting these molecular markers would, in effect, allow for specific tumor targeting. Tripeptide sequence motifs have previously been reported that will bind to angiogenic tumor ECs. These sequences were identified from in vivo phage peptide display libraries. The purpose of this study was to use a more simplified bacterial peptide display library in an in vitro system to seek out peptide motifs with unique binding to tumor microvasculature.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">FliTrx is a bacterial peptide display library containing the entire repertoire of possible random dodecapeptides expressed on the flagella tip of E. coli. Two EC populations were used for the screening process, Matrigel invading cells (MAGIC) and tumor-derived endothelial cells (TDEC). MAGIC are obtained from ECs that infiltrate a subcutaneous fibroblast growth factor-containing Matrigel deposit, and TDEC are ECs selectively obtained from tumor vasculature. FliTrx cells were incubated with MAGIC at 4 degrees C to remove any potential clones displaying peptides that will bind to nonspecific EC surface targets. The non-binding cells were then incubated with TDEC, allowing for clones displaying potential binding peptides to bind tumor specific targets on TDECs. The bacterial population was then expanded and this "panning" process was carried out a total of five times. Peptide insert sequences from 100 bacterial colonies were analyzed for potential repetitive peptide motifs.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">Recurring peptide sequences were detected that were 3-mers (13 sequences) and 4-mers (4 sequences). Of the 3-mers, four repeated 3 times, whereas none of the 4-mers repeated more than twice. All of the repeated sequences were basic in charge, and arginine was the most commonly seen amino acid. A tripeptide basic-basic-nonpolar amino acid arrangement was the most prevalent charge sequence in all repetitive motifs (17 repeat sequences). Two test peptides showed TDEC binding specificity, and both conformed to the basic-basic-nonpolar motif.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">We report peptide sequences derived from panning an in vitro system designed to detect tumor-EC specific markers. These putative motifs may serve as molecular determinants for a novel therapeutic modality aimed at specifically targeting tumors through tumor angiogenic vessels.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Brown</LastName>
<ForeName>C K</ForeName>
<Initials>CK</Initials>
<AffiliationInfo><Affiliation>Department of Surgery, University of Chicago, Illinois, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Modzelewski</LastName>
<ForeName>R A</ForeName>
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<Author ValidYN="Y"><LastName>Johnson</LastName>
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<Initials>CS</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wong</LastName>
<ForeName>M K</ForeName>
<Initials>MK</Initials>
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<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
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<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Ann Surg Oncol</MedlineTA>
<NlmUniqueID>9420840</NlmUniqueID>
<ISSNLinking>1068-9265</ISSNLinking>
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<NameOfSubstance UI="D019151">Peptide Library</NameOfSubstance>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D016475" MajorTopicYN="N">3T3 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
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<MeshHeading><DescriptorName UI="D002294" MajorTopicYN="N">Carcinoma, Squamous Cell</DescriptorName>
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<MeshHeading><DescriptorName UI="D008809" MajorTopicYN="N">Mice, Inbred C3H</DescriptorName>
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<MeshHeading><DescriptorName UI="D009369" MajorTopicYN="N">Neoplasms</DescriptorName>
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<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
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<MeshHeading><DescriptorName UI="D009389" MajorTopicYN="Y">Neovascularization, Pathologic</DescriptorName>
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<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019151" MajorTopicYN="Y">Peptide Library</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="Y">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014407" MajorTopicYN="N">Tumor Cells, Cultured</DescriptorName>
</MeshHeading>
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