Dimerization of soluble major histocompatibility complex-peptide complexes is sufficient for activation of T cell hybridoma and induction of unresponsiveness
Major histocompatibility complex (MHC) class I molecules are cell-surface proteins that present peptides to CD8+ T cells. These peptides are mostly derived from endogenously synthesized protein. Recombinant, soluble MHC class I molecules were produced, purified, and loaded homogeneously with synthet...
Gespeichert in:
| Veröffentlicht in: | The Journal of experimental medicine 1995-08, Vol.182 (2), p.439-447 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 447 |
|---|---|
| container_issue | 2 |
| container_start_page | 439 |
| container_title | The Journal of experimental medicine |
| container_volume | 182 |
| creator | Abastado, J P Lone, Y C Casrouge, A Boulot, G Kourilsky, P |
| description | Major histocompatibility complex (MHC) class I molecules are cell-surface proteins that present peptides to CD8+ T cells. These peptides are mostly derived from endogenously synthesized protein. Recombinant, soluble MHC class I molecules were produced, purified, and loaded homogeneously with synthetic peptide. These MHC-peptide complexes were used to activate a T cell hybridoma. While monomers of MHC-peptide bound to the T cell, they showed no stimulatory activity. Dimers fully triggered the T cell hybridoma to secrete interleukin 2. This response was followed by a state in which the T cell was refractory to restimulation as a result of defective signal transduction through the T cell receptor. |
| doi_str_mv | 10.1084/jem.182.2.439 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2192121</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77430055</sourcerecordid><originalsourceid>FETCH-LOGICAL-c413t-d0896aaba252196914fb0c480ce446f0bbd8f0863b092abee35f494a17007fdf3</originalsourceid><addsrcrecordid>eNqFkU2LFDEQhoMo67h69Cjk5K3Hykd_XQRZP2HBy3oOSbriZOhO2qR7cPwv_lcz7OygJ0-hqCdvqvIQ8pLBlkEn3-xx2rKOb_lWiv4R2bBaQtXXontMNgCcVwygfUqe5bwHYFLWzRW5ahve1yA35Pd7P2Hyv_TiY6DR0RzH1YxIJ72Pie58XqKN01z6xo9-OdJTNeLPasZ58QM-1JipzzSvznnrMSzUlevaLv5wib6jFseR7o4m-SFOmuowUB-G1T4Qa0iY5xiyP2DAnJ-TJ06PGV-cz2vy7eOHu5vP1e3XT19u3t1WVjKxVAN0faO10bzmrG96Jp0BKzuwKGXjwJihc9A1wkDPtUEUtZO91KwtX-MGJ67J2_vceTUTDrbMn_So5uQnnY4qaq_-7QS_U9_jQZXnOOOsBLw-B6T4Y8W8qMnn07Y6YFyzalspAOr6vyBrOiEZ8AJW96BNMeeE7jINA3USr4p4VcQrror4wr_6e4ULfTYt_gCn8a_r</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16834102</pqid></control><display><type>article</type><title>Dimerization of soluble major histocompatibility complex-peptide complexes is sufficient for activation of T cell hybridoma and induction of unresponsiveness</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Abastado, J P ; Lone, Y C ; Casrouge, A ; Boulot, G ; Kourilsky, P</creator><creatorcontrib>Abastado, J P ; Lone, Y C ; Casrouge, A ; Boulot, G ; Kourilsky, P</creatorcontrib><description>Major histocompatibility complex (MHC) class I molecules are cell-surface proteins that present peptides to CD8+ T cells. These peptides are mostly derived from endogenously synthesized protein. Recombinant, soluble MHC class I molecules were produced, purified, and loaded homogeneously with synthetic peptide. These MHC-peptide complexes were used to activate a T cell hybridoma. While monomers of MHC-peptide bound to the T cell, they showed no stimulatory activity. Dimers fully triggered the T cell hybridoma to secrete interleukin 2. This response was followed by a state in which the T cell was refractory to restimulation as a result of defective signal transduction through the T cell receptor.</description><identifier>ISSN: 0022-1007</identifier><identifier>EISSN: 1540-9538</identifier><identifier>DOI: 10.1084/jem.182.2.439</identifier><identifier>PMID: 7629504</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Amino Acid Sequence ; Animals ; H-2 Antigens - chemistry ; H-2 Antigens - immunology ; Hybridomas ; In Vitro Techniques ; Lymphocyte Activation ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Peptides - immunology ; Protein Binding ; Receptors, Antigen, T-Cell - physiology ; Signal Transduction ; Solubility ; Structure-Activity Relationship ; T-Lymphocytes, Cytotoxic - immunology ; Time Factors</subject><ispartof>The Journal of experimental medicine, 1995-08, Vol.182 (2), p.439-447</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-d0896aaba252196914fb0c480ce446f0bbd8f0863b092abee35f494a17007fdf3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7629504$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abastado, J P</creatorcontrib><creatorcontrib>Lone, Y C</creatorcontrib><creatorcontrib>Casrouge, A</creatorcontrib><creatorcontrib>Boulot, G</creatorcontrib><creatorcontrib>Kourilsky, P</creatorcontrib><title>Dimerization of soluble major histocompatibility complex-peptide complexes is sufficient for activation of T cell hybridoma and induction of unresponsiveness</title><title>The Journal of experimental medicine</title><addtitle>J Exp Med</addtitle><description>Major histocompatibility complex (MHC) class I molecules are cell-surface proteins that present peptides to CD8+ T cells. These peptides are mostly derived from endogenously synthesized protein. Recombinant, soluble MHC class I molecules were produced, purified, and loaded homogeneously with synthetic peptide. These MHC-peptide complexes were used to activate a T cell hybridoma. While monomers of MHC-peptide bound to the T cell, they showed no stimulatory activity. Dimers fully triggered the T cell hybridoma to secrete interleukin 2. This response was followed by a state in which the T cell was refractory to restimulation as a result of defective signal transduction through the T cell receptor.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>H-2 Antigens - chemistry</subject><subject>H-2 Antigens - immunology</subject><subject>Hybridomas</subject><subject>In Vitro Techniques</subject><subject>Lymphocyte Activation</subject><subject>Macromolecular Substances</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Peptides - immunology</subject><subject>Protein Binding</subject><subject>Receptors, Antigen, T-Cell - physiology</subject><subject>Signal Transduction</subject><subject>Solubility</subject><subject>Structure-Activity Relationship</subject><subject>T-Lymphocytes, Cytotoxic - immunology</subject><subject>Time Factors</subject><issn>0022-1007</issn><issn>1540-9538</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2LFDEQhoMo67h69Cjk5K3Hykd_XQRZP2HBy3oOSbriZOhO2qR7cPwv_lcz7OygJ0-hqCdvqvIQ8pLBlkEn3-xx2rKOb_lWiv4R2bBaQtXXontMNgCcVwygfUqe5bwHYFLWzRW5ahve1yA35Pd7P2Hyv_TiY6DR0RzH1YxIJ72Pie58XqKN01z6xo9-OdJTNeLPasZ58QM-1JipzzSvznnrMSzUlevaLv5wib6jFseR7o4m-SFOmuowUB-G1T4Qa0iY5xiyP2DAnJ-TJ06PGV-cz2vy7eOHu5vP1e3XT19u3t1WVjKxVAN0faO10bzmrG96Jp0BKzuwKGXjwJihc9A1wkDPtUEUtZO91KwtX-MGJ67J2_vceTUTDrbMn_So5uQnnY4qaq_-7QS_U9_jQZXnOOOsBLw-B6T4Y8W8qMnn07Y6YFyzalspAOr6vyBrOiEZ8AJW96BNMeeE7jINA3USr4p4VcQrror4wr_6e4ULfTYt_gCn8a_r</recordid><startdate>19950801</startdate><enddate>19950801</enddate><creator>Abastado, J P</creator><creator>Lone, Y C</creator><creator>Casrouge, A</creator><creator>Boulot, G</creator><creator>Kourilsky, P</creator><general>The Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T5</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950801</creationdate><title>Dimerization of soluble major histocompatibility complex-peptide complexes is sufficient for activation of T cell hybridoma and induction of unresponsiveness</title><author>Abastado, J P ; Lone, Y C ; Casrouge, A ; Boulot, G ; Kourilsky, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-d0896aaba252196914fb0c480ce446f0bbd8f0863b092abee35f494a17007fdf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>H-2 Antigens - chemistry</topic><topic>H-2 Antigens - immunology</topic><topic>Hybridomas</topic><topic>In Vitro Techniques</topic><topic>Lymphocyte Activation</topic><topic>Macromolecular Substances</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Peptides - immunology</topic><topic>Protein Binding</topic><topic>Receptors, Antigen, T-Cell - physiology</topic><topic>Signal Transduction</topic><topic>Solubility</topic><topic>Structure-Activity Relationship</topic><topic>T-Lymphocytes, Cytotoxic - immunology</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Abastado, J P</creatorcontrib><creatorcontrib>Lone, Y C</creatorcontrib><creatorcontrib>Casrouge, A</creatorcontrib><creatorcontrib>Boulot, G</creatorcontrib><creatorcontrib>Kourilsky, P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of experimental medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abastado, J P</au><au>Lone, Y C</au><au>Casrouge, A</au><au>Boulot, G</au><au>Kourilsky, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dimerization of soluble major histocompatibility complex-peptide complexes is sufficient for activation of T cell hybridoma and induction of unresponsiveness</atitle><jtitle>The Journal of experimental medicine</jtitle><addtitle>J Exp Med</addtitle><date>1995-08-01</date><risdate>1995</risdate><volume>182</volume><issue>2</issue><spage>439</spage><epage>447</epage><pages>439-447</pages><issn>0022-1007</issn><eissn>1540-9538</eissn><abstract>Major histocompatibility complex (MHC) class I molecules are cell-surface proteins that present peptides to CD8+ T cells. These peptides are mostly derived from endogenously synthesized protein. Recombinant, soluble MHC class I molecules were produced, purified, and loaded homogeneously with synthetic peptide. These MHC-peptide complexes were used to activate a T cell hybridoma. While monomers of MHC-peptide bound to the T cell, they showed no stimulatory activity. Dimers fully triggered the T cell hybridoma to secrete interleukin 2. This response was followed by a state in which the T cell was refractory to restimulation as a result of defective signal transduction through the T cell receptor.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>7629504</pmid><doi>10.1084/jem.182.2.439</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-1007 |
| ispartof | The Journal of experimental medicine, 1995-08, Vol.182 (2), p.439-447 |
| issn | 0022-1007 1540-9538 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2192121 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence Animals H-2 Antigens - chemistry H-2 Antigens - immunology Hybridomas In Vitro Techniques Lymphocyte Activation Macromolecular Substances Mice Molecular Sequence Data Peptides - immunology Protein Binding Receptors, Antigen, T-Cell - physiology Signal Transduction Solubility Structure-Activity Relationship T-Lymphocytes, Cytotoxic - immunology Time Factors |
| title | Dimerization of soluble major histocompatibility complex-peptide complexes is sufficient for activation of T cell hybridoma and induction of unresponsiveness |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T14%3A44%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Dimerization%20of%20soluble%20major%20histocompatibility%20complex-peptide%20complexes%20is%20sufficient%20for%20activation%20of%20T%20cell%20hybridoma%20and%20induction%20of%20unresponsiveness&rft.jtitle=The%20Journal%20of%20experimental%20medicine&rft.au=Abastado,%20J%20P&rft.date=1995-08-01&rft.volume=182&rft.issue=2&rft.spage=439&rft.epage=447&rft.pages=439-447&rft.issn=0022-1007&rft.eissn=1540-9538&rft_id=info:doi/10.1084/jem.182.2.439&rft_dat=%3Cproquest_pubme%3E77430055%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16834102&rft_id=info:pmid/7629504&rfr_iscdi=true |