A secreted form of the human interleukin 2 receptor encoded by an "anchor minus" cDNA
The DNA sequence encoding all of the putative intracytoplasmic domain and most of the trans-membrane domain of the human IL 2 receptor was deleted from a full length receptor cDNA. After expression in mouse L cells, the resultant "anchor minus" cDNA was found to direct the synthesis of a s...
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| Veröffentlicht in: | The Journal of immunology (1950) 1986-06, Vol.136 (11), p.4099-4105 |
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| container_issue | 11 |
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| container_title | The Journal of immunology (1950) |
| container_volume | 136 |
| creator | Treiger, BF Leonard, WJ Svetlik, P Rubin, LA Nelson, DL Greene, WC |
| description | The DNA sequence encoding all of the putative intracytoplasmic domain and most of the trans-membrane domain of the human IL 2 receptor was deleted from a full length receptor cDNA. After expression in mouse L cells, the resultant "anchor minus" cDNA was found to direct the synthesis of a secreted rather than membrane-associated form of the IL 2 receptor. The secreted receptor protein (44,000 to 46,000 Mr) retained the capacity to bind both IL 2 and the monoclonal anti-Tac antibody, as evidenced by retention on IL 2 and anti-Tac affinity columns, inhibition of [3H]-anti-Tac binding to HUT 102B2 cells, and partial inhibition of IL 2-induced CTLL proliferation. Removal of these domains from the IL 2 receptor did not alter the posttranslational processing or rate of export of the truncated receptor protein. These data confirm the proposed membrane orientation of the IL 2 receptor (NH2 terminus out, COOH terminus in) and underscore the anchoring function of this carboxy terminal receptor segment. The availability of such anchor minus receptor cDNA constructs may facilitate purification of large quantities of receptor protein for further analysis of receptor structure, valency, and localization of the IL 2 binding site(s). |
| doi_str_mv | 10.4049/jimmunol.136.11.4099 |
| format | Article |
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After expression in mouse L cells, the resultant "anchor minus" cDNA was found to direct the synthesis of a secreted rather than membrane-associated form of the IL 2 receptor. The secreted receptor protein (44,000 to 46,000 Mr) retained the capacity to bind both IL 2 and the monoclonal anti-Tac antibody, as evidenced by retention on IL 2 and anti-Tac affinity columns, inhibition of [3H]-anti-Tac binding to HUT 102B2 cells, and partial inhibition of IL 2-induced CTLL proliferation. Removal of these domains from the IL 2 receptor did not alter the posttranslational processing or rate of export of the truncated receptor protein. These data confirm the proposed membrane orientation of the IL 2 receptor (NH2 terminus out, COOH terminus in) and underscore the anchoring function of this carboxy terminal receptor segment. The availability of such anchor minus receptor cDNA constructs may facilitate purification of large quantities of receptor protein for further analysis of receptor structure, valency, and localization of the IL 2 binding site(s).</description><identifier>ISSN: 0022-1767</identifier><identifier>EISSN: 1550-6606</identifier><identifier>DOI: 10.4049/jimmunol.136.11.4099</identifier><identifier>PMID: 3084654</identifier><identifier>CODEN: JOIMA3</identifier><language>eng</language><publisher>Bethesda, MD: Am Assoc Immnol</publisher><subject>Amino Acid Sequence ; Analysis of the immune response. Humoral and cellular immunity ; Animals ; Base Sequence ; Biological and medical sciences ; Carbohydrate Conformation ; Chromatography, Affinity ; DNA - metabolism ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Immunobiology ; Interleukin-2 - genetics ; Interleukin-2 - metabolism ; L Cells (Cell Line) - metabolism ; Lymphokines, interleukins ( function, expression) ; Membrane Proteins - genetics ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Mice ; Neuraminidase ; Precipitin Tests ; Protein Processing, Post-Translational ; Receptors, Immunologic - genetics ; Receptors, Immunologic - isolation & purification ; Receptors, Immunologic - metabolism ; Receptors, Interleukin-2 ; Regulatory factors and their cellular receptors</subject><ispartof>The Journal of immunology (1950), 1986-06, Vol.136 (11), p.4099-4105</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-aa7b85d316f5b67601447bb63a60c158166af0641757c15aff26bc7e97e42a5c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8704294$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3084654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Treiger, BF</creatorcontrib><creatorcontrib>Leonard, WJ</creatorcontrib><creatorcontrib>Svetlik, P</creatorcontrib><creatorcontrib>Rubin, LA</creatorcontrib><creatorcontrib>Nelson, DL</creatorcontrib><creatorcontrib>Greene, WC</creatorcontrib><title>A secreted form of the human interleukin 2 receptor encoded by an "anchor minus" cDNA</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>The DNA sequence encoding all of the putative intracytoplasmic domain and most of the trans-membrane domain of the human IL 2 receptor was deleted from a full length receptor cDNA. After expression in mouse L cells, the resultant "anchor minus" cDNA was found to direct the synthesis of a secreted rather than membrane-associated form of the IL 2 receptor. The secreted receptor protein (44,000 to 46,000 Mr) retained the capacity to bind both IL 2 and the monoclonal anti-Tac antibody, as evidenced by retention on IL 2 and anti-Tac affinity columns, inhibition of [3H]-anti-Tac binding to HUT 102B2 cells, and partial inhibition of IL 2-induced CTLL proliferation. Removal of these domains from the IL 2 receptor did not alter the posttranslational processing or rate of export of the truncated receptor protein. These data confirm the proposed membrane orientation of the IL 2 receptor (NH2 terminus out, COOH terminus in) and underscore the anchoring function of this carboxy terminal receptor segment. The availability of such anchor minus receptor cDNA constructs may facilitate purification of large quantities of receptor protein for further analysis of receptor structure, valency, and localization of the IL 2 binding site(s).</description><subject>Amino Acid Sequence</subject><subject>Analysis of the immune response. Humoral and cellular immunity</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Conformation</subject><subject>Chromatography, Affinity</subject><subject>DNA - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Immunobiology</subject><subject>Interleukin-2 - genetics</subject><subject>Interleukin-2 - metabolism</subject><subject>L Cells (Cell Line) - metabolism</subject><subject>Lymphokines, interleukins ( function, expression)</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Neuraminidase</subject><subject>Precipitin Tests</subject><subject>Protein Processing, Post-Translational</subject><subject>Receptors, Immunologic - genetics</subject><subject>Receptors, Immunologic - isolation & purification</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, Interleukin-2</subject><subject>Regulatory factors and their cellular receptors</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkMFu1DAQhi0EKtvCG4BkVQhxyTJOnHFyXBVKkSp6ac-W4x0TlzhZ7ESrvj1e7VL1ZHnm-_-RPsY-CFhLkO3XRx_CMk7DWlS4FiIP2_YVW4m6hgIR8DVbAZRlIRSqt-w8pUcAQCjlGTuroJFYyxV72PBENtJMW-6mGPjk-NwT75dgRu7HmeJAyx8_8pJHsrSbp8hptNM2B7onnqFLM9o-T4Mfl3TJ7bdfm3fsjTNDoven94I9XH-_v7opbu9-_Lza3BZWKpwLY1TX1NtKoKs7VAhCStV1WBkEK-pGIBoHKIWqVf4b50rsrKJWkSxNbasL9vnYu4vT34XSrINPlobBjDQtSStsABulMiiPoI1TSpGc3kUfTHzSAvTBpv5vU2ebWgh9sJljH0_9Sxdo-xw66cv7T6e9SdYMLmYVPj1jjQJZtgfsyxHr_e9-7yPpFMww5FKh9_v9y4v_AKWPi64</recordid><startdate>19860601</startdate><enddate>19860601</enddate><creator>Treiger, BF</creator><creator>Leonard, WJ</creator><creator>Svetlik, P</creator><creator>Rubin, LA</creator><creator>Nelson, DL</creator><creator>Greene, WC</creator><general>Am Assoc Immnol</general><general>American Association of Immunologists</general><scope>IQODW</scope><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>7X8</scope></search><sort><creationdate>19860601</creationdate><title>A secreted form of the human interleukin 2 receptor encoded by an "anchor minus" cDNA</title><author>Treiger, BF ; Leonard, WJ ; Svetlik, P ; Rubin, LA ; Nelson, DL ; Greene, WC</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-aa7b85d316f5b67601447bb63a60c158166af0641757c15aff26bc7e97e42a5c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino Acid Sequence</topic><topic>Analysis of the immune response. Humoral and cellular immunity</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Conformation</topic><topic>Chromatography, Affinity</topic><topic>DNA - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Immunobiology</topic><topic>Interleukin-2 - genetics</topic><topic>Interleukin-2 - metabolism</topic><topic>L Cells (Cell Line) - metabolism</topic><topic>Lymphokines, interleukins ( function, expression)</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Neuraminidase</topic><topic>Precipitin Tests</topic><topic>Protein Processing, Post-Translational</topic><topic>Receptors, Immunologic - genetics</topic><topic>Receptors, Immunologic - isolation & purification</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, Interleukin-2</topic><topic>Regulatory factors and their cellular receptors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Treiger, BF</creatorcontrib><creatorcontrib>Leonard, WJ</creatorcontrib><creatorcontrib>Svetlik, P</creatorcontrib><creatorcontrib>Rubin, LA</creatorcontrib><creatorcontrib>Nelson, DL</creatorcontrib><creatorcontrib>Greene, WC</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of immunology (1950)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Treiger, BF</au><au>Leonard, WJ</au><au>Svetlik, P</au><au>Rubin, LA</au><au>Nelson, DL</au><au>Greene, WC</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A secreted form of the human interleukin 2 receptor encoded by an "anchor minus" cDNA</atitle><jtitle>The Journal of immunology (1950)</jtitle><addtitle>J Immunol</addtitle><date>1986-06-01</date><risdate>1986</risdate><volume>136</volume><issue>11</issue><spage>4099</spage><epage>4105</epage><pages>4099-4105</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><coden>JOIMA3</coden><abstract>The DNA sequence encoding all of the putative intracytoplasmic domain and most of the trans-membrane domain of the human IL 2 receptor was deleted from a full length receptor cDNA. After expression in mouse L cells, the resultant "anchor minus" cDNA was found to direct the synthesis of a secreted rather than membrane-associated form of the IL 2 receptor. The secreted receptor protein (44,000 to 46,000 Mr) retained the capacity to bind both IL 2 and the monoclonal anti-Tac antibody, as evidenced by retention on IL 2 and anti-Tac affinity columns, inhibition of [3H]-anti-Tac binding to HUT 102B2 cells, and partial inhibition of IL 2-induced CTLL proliferation. Removal of these domains from the IL 2 receptor did not alter the posttranslational processing or rate of export of the truncated receptor protein. These data confirm the proposed membrane orientation of the IL 2 receptor (NH2 terminus out, COOH terminus in) and underscore the anchoring function of this carboxy terminal receptor segment. The availability of such anchor minus receptor cDNA constructs may facilitate purification of large quantities of receptor protein for further analysis of receptor structure, valency, and localization of the IL 2 binding site(s).</abstract><cop>Bethesda, MD</cop><pub>Am Assoc Immnol</pub><pmid>3084654</pmid><doi>10.4049/jimmunol.136.11.4099</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0022-1767 |
| ispartof | The Journal of immunology (1950), 1986-06, Vol.136 (11), p.4099-4105 |
| issn | 0022-1767 1550-6606 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76806877 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analysis of the immune response. Humoral and cellular immunity Animals Base Sequence Biological and medical sciences Carbohydrate Conformation Chromatography, Affinity DNA - metabolism Fundamental and applied biological sciences. Psychology Fundamental immunology Immunobiology Interleukin-2 - genetics Interleukin-2 - metabolism L Cells (Cell Line) - metabolism Lymphokines, interleukins ( function, expression) Membrane Proteins - genetics Membrane Proteins - isolation & purification Membrane Proteins - metabolism Mice Neuraminidase Precipitin Tests Protein Processing, Post-Translational Receptors, Immunologic - genetics Receptors, Immunologic - isolation & purification Receptors, Immunologic - metabolism Receptors, Interleukin-2 Regulatory factors and their cellular receptors |
| title | A secreted form of the human interleukin 2 receptor encoded by an "anchor minus" cDNA |
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