Tumour-specific MHC-class-II-restricted responses after in vitro sensitization to synthetic peptides corresponding to gp100 and Annexin II eluted from melanoma cells.
Identifieur interne : 002B38 ( Ncbi/Merge ); précédent : 002B37; suivant : 002B39Tumour-specific MHC-class-II-restricted responses after in vitro sensitization to synthetic peptides corresponding to gp100 and Annexin II eluted from melanoma cells.
Auteurs : K. Li [Allemagne] ; M. Adibzadeh ; T. Halder ; H. Kalbacher ; S. Heinzel ; C. Müller ; J. Zeuthen ; G. PawelecSource :
- Cancer immunology, immunotherapy : CII [ 0340-7004 ] ; 1998.
Descripteurs français
- KwdFr :
- Animaux, Annexine A2 (immunologie), Anticorps antitumoraux (immunologie), Antigène gp100 du mélanome, Antigènes d'histocompatibilité de classe II (pharmacologie), Cellules CHO (métabolisme), Cellules cancéreuses en culture, Cricetinae, Fragments peptidiques (biosynthèse), Glycoprotéines membranaires (immunologie), Humains, Immunisation, Mélanome expérimental (anatomopathologie), Mélanome expérimental (immunologie), Protéines tumorales (immunologie), Spécificité des anticorps.
- MESH :
- anatomopathologie : Mélanome expérimental.
- biosynthèse : Fragments peptidiques.
- immunologie : Annexine A2, Anticorps antitumoraux, Glycoprotéines membranaires, Mélanome expérimental, Protéines tumorales.
- métabolisme : Cellules CHO.
- pharmacologie : Antigènes d'histocompatibilité de classe II.
- Animaux, Antigène gp100 du mélanome, Cellules cancéreuses en culture, Cricetinae, Humains, Immunisation, Spécificité des anticorps.
English descriptors
- KwdEn :
- Animals, Annexin A2 (immunology), Antibodies, Neoplasm (immunology), Antibody Specificity, CHO Cells (metabolism), Cricetinae, Histocompatibility Antigens Class II (pharmacology), Humans, Immunization, Melanoma, Experimental (immunology), Melanoma, Experimental (pathology), Membrane Glycoproteins (immunology), Neoplasm Proteins (immunology), Peptide Fragments (biosynthesis), Tumor Cells, Cultured, gp100 Melanoma Antigen.
- MESH :
- chemical , biosynthesis : Peptide Fragments.
- chemical , immunology : Annexin A2, Antibodies, Neoplasm, Membrane Glycoproteins, Neoplasm Proteins.
- immunology : Melanoma, Experimental.
- metabolism : CHO Cells.
- pathology : Melanoma, Experimental.
- chemical , pharmacology : Histocompatibility Antigens Class II.
- Animals, Antibody Specificity, Cricetinae, Humans, Immunization, Tumor Cells, Cultured, gp100 Melanoma Antigen.
Abstract
In a search for potentially tumour-specific MHC-class-II-restricted antigens, the immunogenicity of endogenous peptides that had been eluted from HLA-DR molecules of the human melanoma cell line FM3 (HLA-DRB1*02x, DRB1*0401) was tested in vitro. Two 16-mers representing gp100 positions 44-59, and annexin II positions 208-223 bound well to isolated DRB1*0401 molecules and are discussed here. HLA-DR-matched normal donors' T cells were cultured with peptide-pulsed artificial antigen-presenting cells (CHO cells cotransfected with genes for HLA-DRB1*0401 and CD80 and coexpressing high levels of both human molecules). Specific sensitization was achieved against both peptides, as measured in assays of autocrine proliferation and interleukin-2 secretion. Moreover, responses to native autologous melanoma cells but not to autologous B cells were also observed. In view of the expression of fas by the activated T cells and of fas ligand by the melanoma cells, blockade of potential fas/ fas-ligand interactions was undertaken using monoclonal antibodies (mAb). The antagonistic fas-specific mAb M3, but not the fas agonist M33, caused a markedly enhanced T cell response to FM3 cells. These results demonstrate that synthetic peptide antigens are able to sensitize T cells in vitro for effective MHC-class-II-restricted recognition of melanoma cells.
DOI: 10.1007/s002620050501
PubMed: 9755876
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Adibzadeh</name></author><author><name sortKey="Halder, T" sort="Halder, T" uniqKey="Halder T" first="T" last="Halder">T. Halder</name></author><author><name sortKey="Kalbacher, H" sort="Kalbacher, H" uniqKey="Kalbacher H" first="H" last="Kalbacher">H. Kalbacher</name></author><author><name sortKey="Heinzel, S" sort="Heinzel, S" uniqKey="Heinzel S" first="S" last="Heinzel">S. Heinzel</name></author><author><name sortKey="Muller, C" sort="Muller, C" uniqKey="Muller C" first="C" last="Müller">C. Müller</name></author><author><name sortKey="Zeuthen, J" sort="Zeuthen, J" uniqKey="Zeuthen J" first="J" last="Zeuthen">J. Zeuthen</name></author><author><name sortKey="Pawelec, G" sort="Pawelec, G" uniqKey="Pawelec G" first="G" last="Pawelec">G. 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Li</name><affiliation wicri:level="1"><nlm:affiliation>Second Department of Internal Medicine, University of Tübingen Medical School, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Second Department of Internal Medicine, University of Tübingen Medical School</wicri:regionArea><wicri:noRegion>University of Tübingen Medical School</wicri:noRegion><wicri:noRegion>University of Tübingen Medical School</wicri:noRegion><wicri:noRegion>University of Tübingen Medical School</wicri:noRegion></affiliation></author><author><name sortKey="Adibzadeh, M" sort="Adibzadeh, M" uniqKey="Adibzadeh M" first="M" last="Adibzadeh">M. Adibzadeh</name></author><author><name sortKey="Halder, T" sort="Halder, T" uniqKey="Halder T" first="T" last="Halder">T. Halder</name></author><author><name sortKey="Kalbacher, H" sort="Kalbacher, H" uniqKey="Kalbacher H" first="H" last="Kalbacher">H. Kalbacher</name></author><author><name sortKey="Heinzel, S" sort="Heinzel, S" uniqKey="Heinzel S" first="S" last="Heinzel">S. Heinzel</name></author><author><name sortKey="Muller, C" sort="Muller, C" uniqKey="Muller C" first="C" last="Müller">C. Müller</name></author><author><name sortKey="Zeuthen, J" sort="Zeuthen, J" uniqKey="Zeuthen J" first="J" last="Zeuthen">J. Zeuthen</name></author><author><name sortKey="Pawelec, G" sort="Pawelec, G" uniqKey="Pawelec G" first="G" last="Pawelec">G. Pawelec</name></author></analytic><series><title level="j">Cancer immunology, immunotherapy : CII</title><idno type="ISSN">0340-7004</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Annexin A2 (immunology)</term><term>Antibodies, Neoplasm (immunology)</term><term>Antibody Specificity</term><term>CHO Cells (metabolism)</term><term>Cricetinae</term><term>Histocompatibility Antigens Class II (pharmacology)</term><term>Humans</term><term>Immunization</term><term>Melanoma, Experimental (immunology)</term><term>Melanoma, Experimental (pathology)</term><term>Membrane Glycoproteins (immunology)</term><term>Neoplasm Proteins (immunology)</term><term>Peptide Fragments (biosynthesis)</term><term>Tumor Cells, Cultured</term><term>gp100 Melanoma Antigen</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Annexine A2 (immunologie)</term><term>Anticorps antitumoraux (immunologie)</term><term>Antigène gp100 du mélanome</term><term>Antigènes d'histocompatibilité de classe II (pharmacologie)</term><term>Cellules CHO (métabolisme)</term><term>Cellules cancéreuses en culture</term><term>Cricetinae</term><term>Fragments peptidiques (biosynthèse)</term><term>Glycoprotéines membranaires (immunologie)</term><term>Humains</term><term>Immunisation</term><term>Mélanome expérimental (anatomopathologie)</term><term>Mélanome expérimental (immunologie)</term><term>Protéines tumorales (immunologie)</term><term>Spécificité des anticorps</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Annexin A2</term><term>Antibodies, Neoplasm</term><term>Membrane Glycoproteins</term><term>Neoplasm Proteins</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Mélanome expérimental</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Fragments peptidiques</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Annexine A2</term><term>Anticorps antitumoraux</term><term>Glycoprotéines membranaires</term><term>Mélanome expérimental</term><term>Protéines tumorales</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Melanoma, Experimental</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>CHO Cells</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules CHO</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Melanoma, Experimental</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antigènes d'histocompatibilité de classe II</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Histocompatibility Antigens Class II</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Antibody Specificity</term><term>Cricetinae</term><term>Humans</term><term>Immunization</term><term>Tumor Cells, Cultured</term><term>gp100 Melanoma Antigen</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antigène gp100 du mélanome</term><term>Cellules cancéreuses en culture</term><term>Cricetinae</term><term>Humains</term><term>Immunisation</term><term>Spécificité des anticorps</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In a search for potentially tumour-specific MHC-class-II-restricted antigens, the immunogenicity of endogenous peptides that had been eluted from HLA-DR molecules of the human melanoma cell line FM3 (HLA-DRB1*02x, DRB1*0401) was tested in vitro. Two 16-mers representing gp100 positions 44-59, and annexin II positions 208-223 bound well to isolated DRB1*0401 molecules and are discussed here. HLA-DR-matched normal donors' T cells were cultured with peptide-pulsed artificial antigen-presenting cells (CHO cells cotransfected with genes for HLA-DRB1*0401 and CD80 and coexpressing high levels of both human molecules). Specific sensitization was achieved against both peptides, as measured in assays of autocrine proliferation and interleukin-2 secretion. Moreover, responses to native autologous melanoma cells but not to autologous B cells were also observed. In view of the expression of fas by the activated T cells and of fas ligand by the melanoma cells, blockade of potential fas/ fas-ligand interactions was undertaken using monoclonal antibodies (mAb). The antagonistic fas-specific mAb M3, but not the fas agonist M33, caused a markedly enhanced T cell response to FM3 cells. These results demonstrate that synthetic peptide antigens are able to sensitize T cells in vitro for effective MHC-class-II-restricted recognition of melanoma cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9755876</PMID><DateCompleted><Year>1998</Year><Month>10</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>09</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0340-7004</ISSN><JournalIssue CitedMedium="Print"><Volume>47</Volume><Issue>1</Issue><PubDate><Year>1998</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Cancer immunology, immunotherapy : CII</Title><ISOAbbreviation>Cancer Immunol. Immunother.</ISOAbbreviation></Journal><ArticleTitle>Tumour-specific MHC-class-II-restricted responses after in vitro sensitization to synthetic peptides corresponding to gp100 and Annexin II eluted from melanoma cells.</ArticleTitle><Pagination><MedlinePgn>32-8</MedlinePgn></Pagination><Abstract><AbstractText>In a search for potentially tumour-specific MHC-class-II-restricted antigens, the immunogenicity of endogenous peptides that had been eluted from HLA-DR molecules of the human melanoma cell line FM3 (HLA-DRB1*02x, DRB1*0401) was tested in vitro. Two 16-mers representing gp100 positions 44-59, and annexin II positions 208-223 bound well to isolated DRB1*0401 molecules and are discussed here. HLA-DR-matched normal donors' T cells were cultured with peptide-pulsed artificial antigen-presenting cells (CHO cells cotransfected with genes for HLA-DRB1*0401 and CD80 and coexpressing high levels of both human molecules). Specific sensitization was achieved against both peptides, as measured in assays of autocrine proliferation and interleukin-2 secretion. Moreover, responses to native autologous melanoma cells but not to autologous B cells were also observed. In view of the expression of fas by the activated T cells and of fas ligand by the melanoma cells, blockade of potential fas/ fas-ligand interactions was undertaken using monoclonal antibodies (mAb). The antagonistic fas-specific mAb M3, but not the fas agonist M33, caused a markedly enhanced T cell response to FM3 cells. These results demonstrate that synthetic peptide antigens are able to sensitize T cells in vitro for effective MHC-class-II-restricted recognition of melanoma cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Second Department of Internal Medicine, University of Tübingen Medical School, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Adibzadeh</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Halder</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Kalbacher</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Heinzel</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Zeuthen</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Pawelec</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Cancer Immunol Immunother</MedlineTA><NlmUniqueID>8605732</NlmUniqueID><ISSNLinking>0340-7004</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017306">Annexin A2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000912">Antibodies, Neoplasm</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000949">Histocompatibility Antigens Class II</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009363">Neoplasm Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C548637">PMEL protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D058951">gp100 Melanoma Antigen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017306" MajorTopicYN="N">Annexin A2</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000912" MajorTopicYN="N">Antibodies, Neoplasm</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000918" MajorTopicYN="N">Antibody Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016466" MajorTopicYN="N">CHO Cells</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006224" MajorTopicYN="N">Cricetinae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000949" MajorTopicYN="N">Histocompatibility Antigens Class II</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007114" MajorTopicYN="N">Immunization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008546" MajorTopicYN="N">Melanoma, Experimental</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009363" MajorTopicYN="N">Neoplasm Proteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014407" MajorTopicYN="N">Tumor Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058951" MajorTopicYN="N">gp100 Melanoma Antigen</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>10</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>10</Month><Day>2</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>10</Month><Day>2</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9755876</ArticleId><ArticleId IdType="doi">10.1007/s002620050501</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Adibzadeh, M" sort="Adibzadeh, M" uniqKey="Adibzadeh M" first="M" last="Adibzadeh">M. Adibzadeh</name><name sortKey="Halder, T" sort="Halder, T" uniqKey="Halder T" first="T" last="Halder">T. Halder</name><name sortKey="Heinzel, S" sort="Heinzel, S" uniqKey="Heinzel S" first="S" last="Heinzel">S. Heinzel</name><name sortKey="Kalbacher, H" sort="Kalbacher, H" uniqKey="Kalbacher H" first="H" last="Kalbacher">H. Kalbacher</name><name sortKey="Muller, C" sort="Muller, C" uniqKey="Muller C" first="C" last="Müller">C. Müller</name><name sortKey="Pawelec, G" sort="Pawelec, G" uniqKey="Pawelec G" first="G" last="Pawelec">G. Pawelec</name><name sortKey="Zeuthen, J" sort="Zeuthen, J" uniqKey="Zeuthen J" first="J" last="Zeuthen">J. Zeuthen</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Li, K" sort="Li, K" uniqKey="Li K" first="K" last="Li">K. Li</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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