Imaging brain tumors by targeting peptide radiopharmaceuticals through the blood-brain barrier.
Identifieur interne : 003C43 ( Main/Exploration ); précédent : 003C42; suivant : 003C44Imaging brain tumors by targeting peptide radiopharmaceuticals through the blood-brain barrier.
Auteurs : RBID : pubmed:10626807English descriptors
- KwdEn :
- Animals, Biotinylation, Blood-Brain Barrier, Brain Neoplasms (radionuclide imaging), Epidermal Growth Factor (metabolism), Humans, Indium Radioisotopes (diagnostic use), Indium Radioisotopes (metabolism), Mice, Mice, Nude, Neoplasm Transplantation, Pentetic Acid (chemistry), Peptides (metabolism), Radiopharmaceuticals (diagnostic use), Radiopharmaceuticals (metabolism), Receptor, Epidermal Growth Factor (genetics), Receptor, Epidermal Growth Factor (metabolism), Tumor Cells, Cultured.
- MESH :
- chemical , chemistry : Pentetic Acid.
- chemical , diagnostic use : Indium Radioisotopes, Radiopharmaceuticals.
- chemical , genetics : Receptor, Epidermal Growth Factor.
- chemical , metabolism : Epidermal Growth Factor, Indium Radioisotopes, Peptides, Radiopharmaceuticals, Receptor, Epidermal Growth Factor.
- radionuclide imaging : Brain Neoplasms.
- Animals, Biotinylation, Blood-Brain Barrier, Humans, Mice, Mice, Nude, Neoplasm Transplantation, Tumor Cells, Cultured.
Abstract
Present day imaging of brain tumors requires a disrupted blood-brain barrier (BBB). However, the BBB is intact in the early stages of brain tumor growth, when diagnosis is most critical. Relative to normal brain, brain tumor cells frequently overexpress peptide receptors, such as the receptor for epidermal growth factor (EGF). Peptide radiopharmaceuticals such as radiolabeled EGF could be used to image early brain tumors, should these radiopharmaceuticals be made transportable through the BBB. The present studies describe a bifunctional molecule that contains both biologically active human EGF radiolabeled with 111In and an anti-transferrin receptor monoclonal antibody that undergoes transcytosis through the BBB via the endogenous transferrin transport system. The two domains of the bifunctional conjugate are separated by a Mr 3400 polyethyleneglycol linker, which releases steric hindrance and allows the conjugate to bind to both the EGF receptor, to image the brain tumor, and to the transferrin receptor, to enable transport through the BBB. Successful imaging of experimental brain tumors with this system is demonstrated in nude rats bearing cerebral implants of human U87 glioma.
PubMed: 10626807
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Imaging brain tumors by targeting peptide radiopharmaceuticals through the blood-brain barrier.</title><author><name sortKey="Kurihara, A" uniqKey="Kurihara A">A Kurihara</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medicine, University of California at Los Angeles School of Medicine, 90095, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, University of California at Los Angeles School of Medicine, 90095</wicri:regionArea></affiliation></author><author><name sortKey="Pardridge, W M" uniqKey="Pardridge W">W M Pardridge</name></author></titleStmt><publicationStmt><date when="1999">1999</date><idno type="RBID">pubmed:10626807</idno><idno type="pmid">10626807</idno><idno type="wicri:Area/Main/Corpus">003D59</idno><idno type="wicri:Area/Main/Curation">003D59</idno><idno type="wicri:Area/Main/Exploration">003C43</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Biotinylation</term><term>Blood-Brain Barrier</term><term>Brain Neoplasms (radionuclide imaging)</term><term>Epidermal Growth Factor (metabolism)</term><term>Humans</term><term>Indium Radioisotopes (diagnostic use)</term><term>Indium Radioisotopes (metabolism)</term><term>Mice</term><term>Mice, Nude</term><term>Neoplasm Transplantation</term><term>Pentetic Acid (chemistry)</term><term>Peptides (metabolism)</term><term>Radiopharmaceuticals (diagnostic use)</term><term>Radiopharmaceuticals (metabolism)</term><term>Receptor, Epidermal Growth Factor (genetics)</term><term>Receptor, Epidermal Growth Factor (metabolism)</term><term>Tumor Cells, Cultured</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Pentetic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="diagnostic use" xml:lang="en"><term>Indium Radioisotopes</term><term>Radiopharmaceuticals</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Receptor, Epidermal Growth Factor</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Epidermal Growth Factor</term><term>Indium Radioisotopes</term><term>Peptides</term><term>Radiopharmaceuticals</term><term>Receptor, Epidermal Growth Factor</term></keywords><keywords scheme="MESH" qualifier="radionuclide imaging" xml:lang="en"><term>Brain Neoplasms</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biotinylation</term><term>Blood-Brain Barrier</term><term>Humans</term><term>Mice</term><term>Mice, Nude</term><term>Neoplasm Transplantation</term><term>Tumor Cells, Cultured</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Present day imaging of brain tumors requires a disrupted blood-brain barrier (BBB). However, the BBB is intact in the early stages of brain tumor growth, when diagnosis is most critical. Relative to normal brain, brain tumor cells frequently overexpress peptide receptors, such as the receptor for epidermal growth factor (EGF). Peptide radiopharmaceuticals such as radiolabeled EGF could be used to image early brain tumors, should these radiopharmaceuticals be made transportable through the BBB. The present studies describe a bifunctional molecule that contains both biologically active human EGF radiolabeled with 111In and an anti-transferrin receptor monoclonal antibody that undergoes transcytosis through the BBB via the endogenous transferrin transport system. The two domains of the bifunctional conjugate are separated by a Mr 3400 polyethyleneglycol linker, which releases steric hindrance and allows the conjugate to bind to both the EGF receptor, to image the brain tumor, and to the transferrin receptor, to enable transport through the BBB. Successful imaging of experimental brain tumors with this system is demonstrated in nude rats bearing cerebral implants of human U87 glioma.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">10626807</PMID><DateCreated><Year>2000</Year><Month>01</Month><Day>24</Day></DateCreated><DateCompleted><Year>2000</Year><Month>01</Month><Day>24</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0008-5472</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>24</Issue><PubDate><Year>1999</Year><Month>Dec</Month><Day>15</Day></PubDate></JournalIssue><Title>Cancer research</Title><ISOAbbreviation>Cancer Res.</ISOAbbreviation></Journal><ArticleTitle>Imaging brain tumors by targeting peptide radiopharmaceuticals through the blood-brain barrier.</ArticleTitle><Pagination><MedlinePgn>6159-63</MedlinePgn></Pagination><Abstract><AbstractText>Present day imaging of brain tumors requires a disrupted blood-brain barrier (BBB). However, the BBB is intact in the early stages of brain tumor growth, when diagnosis is most critical. Relative to normal brain, brain tumor cells frequently overexpress peptide receptors, such as the receptor for epidermal growth factor (EGF). Peptide radiopharmaceuticals such as radiolabeled EGF could be used to image early brain tumors, should these radiopharmaceuticals be made transportable through the BBB. The present studies describe a bifunctional molecule that contains both biologically active human EGF radiolabeled with 111In and an anti-transferrin receptor monoclonal antibody that undergoes transcytosis through the BBB via the endogenous transferrin transport system. The two domains of the bifunctional conjugate are separated by a Mr 3400 polyethyleneglycol linker, which releases steric hindrance and allows the conjugate to bind to both the EGF receptor, to image the brain tumor, and to the transferrin receptor, to enable transport through the BBB. Successful imaging of experimental brain tumors with this system is demonstrated in nude rats bearing cerebral implants of human U87 glioma.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kurihara</LastName><ForeName>A</ForeName><Initials>A</Initials><Affiliation>Department of Medicine, University of California at Los Angeles School of Medicine, 90095, USA.</Affiliation></Author><Author ValidYN="Y"><LastName>Pardridge</LastName><ForeName>W M</ForeName><Initials>WM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType><PublicationType>Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>UNITED STATES</Country><MedlineTA>Cancer Res</MedlineTA><NlmUniqueID>2984705R</NlmUniqueID><ISSNLinking>0008-5472</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Indium Radioisotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Radiopharmaceuticals</NameOfSubstance></Chemical><Chemical><RegistryNumber>62229-50-9</RegistryNumber><NameOfSubstance>Epidermal Growth Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>7A314HQM0I</RegistryNumber><NameOfSubstance>Pentetic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.1</RegistryNumber><NameOfSubstance>Receptor, Epidermal Growth Factor</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Biotinylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="Y">Blood-Brain Barrier</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Brain Neoplasms</DescriptorName><QualifierName MajorTopicYN="Y">radionuclide imaging</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Epidermal Growth Factor</DescriptorName><QualifierName MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Indium Radioisotopes</DescriptorName><QualifierName MajorTopicYN="N">diagnostic use</QualifierName><QualifierName MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Mice, Nude</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Neoplasm Transplantation</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Pentetic Acid</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Peptides</DescriptorName><QualifierName MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Radiopharmaceuticals</DescriptorName><QualifierName MajorTopicYN="N">diagnostic use</QualifierName><QualifierName MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Receptor, Epidermal Growth Factor</DescriptorName><QualifierName MajorTopicYN="N">genetics</QualifierName><QualifierName MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Tumor Cells, Cultured</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>1</Month><Day>8</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>1</Month><Day>8</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>1</Month><Day>8</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10626807</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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