Murine interferon-β Receptor-Mediated Endocytosis and Nuclear Membrane Binding
Radioiodinated mouse interferon-β (125I-MuIFN-β ) bound with high affinity (Kd= 9.8 × 10-10M) to plasma membrane of L929murine fibroblasts (4-6 × 103receptor sites per cell). The binding was saturable and inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess mouse IFN-γ (MuIFN-γ ). M...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1985-05, Vol.82 (10), p.3281-3285 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Kushnaryov, Vladimir M. MacDonald, Hector S. Sedmak, J. James Grossberg, Sidney E. |
| description | Radioiodinated mouse interferon-β (125I-MuIFN-β ) bound with high affinity (Kd= 9.8 × 10-10M) to plasma membrane of L929murine fibroblasts (4-6 × 103receptor sites per cell). The binding was saturable and inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess mouse IFN-γ (MuIFN-γ ). MuIFN-β bound at 4 degrees C was very rapidly internalized upon warming of the cells to 37 degrees C (t1/2= 1.5 min). Indirect immunoferritin labeling indicated that MuIFN-β was initially located in coated pits and subsequently internalized by receptor-mediated endocytosis. Isolated L929cell nuclei bound125I-MuIFN-β with a 7-fold higher affinity (Kd= 1.4 × 10-10M) and higher receptor density (about 104per nucleus) than that for the plasma membrane. Binding to the nuclear membrane was inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess MuIFN-γ . Trypsin treatment of nuclei decreased IFN binding by 80%, suggesting that the putative nuclear receptors are protein. Specific binding of MuIFN-β to nuclei was also shown by fluorescence and electron microscopy. We propose that the very rapid internalization of MuIFN-β by receptor-mediated endocytosis is important in the cellular processing of IFN and that its high-affinity binding to the nuclear membrane suggests the nucleus as an intracellular site of IFN action. |
| doi_str_mv | 10.1073/pnas.82.10.3281 |
| format | Article |
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James ; Grossberg, Sidney E.</creator><creatorcontrib>Kushnaryov, Vladimir M. ; MacDonald, Hector S. ; Sedmak, J. James ; Grossberg, Sidney E.</creatorcontrib><description>Radioiodinated mouse interferon-β (125I-MuIFN-β ) bound with high affinity (Kd= 9.8 × 10-10M) to plasma membrane of L929murine fibroblasts (4-6 × 103receptor sites per cell). The binding was saturable and inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess mouse IFN-γ (MuIFN-γ ). MuIFN-β bound at 4 degrees C was very rapidly internalized upon warming of the cells to 37 degrees C (t1/2= 1.5 min). Indirect immunoferritin labeling indicated that MuIFN-β was initially located in coated pits and subsequently internalized by receptor-mediated endocytosis. Isolated L929cell nuclei bound125I-MuIFN-β with a 7-fold higher affinity (Kd= 1.4 × 10-10M) and higher receptor density (about 104per nucleus) than that for the plasma membrane. Binding to the nuclear membrane was inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess MuIFN-γ . Trypsin treatment of nuclei decreased IFN binding by 80%, suggesting that the putative nuclear receptors are protein. Specific binding of MuIFN-β to nuclei was also shown by fluorescence and electron microscopy. We propose that the very rapid internalization of MuIFN-β by receptor-mediated endocytosis is important in the cellular processing of IFN and that its high-affinity binding to the nuclear membrane suggests the nucleus as an intracellular site of IFN action.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.82.10.3281</identifier><identifier>PMID: 3159015</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Animals ; beta -interferon ; Biological and medical sciences ; Cell Membrane - metabolism ; Cell membranes ; Cell nucleus ; Cell physiology ; Cells ; Coated Pits, Cell-Membrane - metabolism ; Endocytosis ; Ferritins ; fibroblasts ; Fundamental and applied biological sciences. Psychology ; Immunologic Techniques ; Interferon Type I - metabolism ; L cells ; L Cells (Cell Line) ; Ligands ; Mice ; Microscopy, Electron ; Molecular and cellular biology ; Nuclear Envelope - metabolism ; Nuclear membrane ; nuclear membranes ; Receptors ; Receptors, Immunologic - metabolism ; Receptors, Interferon ; T lymphocytes</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1985-05, Vol.82 (10), p.3281-3285</ispartof><rights>1985 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c587t-1fcebe2d1d0ccc2ba58d6dd46bfef5ad1af8147fde33ba06e82b6264e80987183</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/82/10.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25567$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25567$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9197755$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3159015$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kushnaryov, Vladimir M.</creatorcontrib><creatorcontrib>MacDonald, Hector S.</creatorcontrib><creatorcontrib>Sedmak, J. James</creatorcontrib><creatorcontrib>Grossberg, Sidney E.</creatorcontrib><title>Murine interferon-β Receptor-Mediated Endocytosis and Nuclear Membrane Binding</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Radioiodinated mouse interferon-β (125I-MuIFN-β ) bound with high affinity (Kd= 9.8 × 10-10M) to plasma membrane of L929murine fibroblasts (4-6 × 103receptor sites per cell). The binding was saturable and inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess mouse IFN-γ (MuIFN-γ ). MuIFN-β bound at 4 degrees C was very rapidly internalized upon warming of the cells to 37 degrees C (t1/2= 1.5 min). Indirect immunoferritin labeling indicated that MuIFN-β was initially located in coated pits and subsequently internalized by receptor-mediated endocytosis. Isolated L929cell nuclei bound125I-MuIFN-β with a 7-fold higher affinity (Kd= 1.4 × 10-10M) and higher receptor density (about 104per nucleus) than that for the plasma membrane. Binding to the nuclear membrane was inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess MuIFN-γ . Trypsin treatment of nuclei decreased IFN binding by 80%, suggesting that the putative nuclear receptors are protein. Specific binding of MuIFN-β to nuclei was also shown by fluorescence and electron microscopy. We propose that the very rapid internalization of MuIFN-β by receptor-mediated endocytosis is important in the cellular processing of IFN and that its high-affinity binding to the nuclear membrane suggests the nucleus as an intracellular site of IFN action.</description><subject>Animals</subject><subject>beta -interferon</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Cell membranes</subject><subject>Cell nucleus</subject><subject>Cell physiology</subject><subject>Cells</subject><subject>Coated Pits, Cell-Membrane - metabolism</subject><subject>Endocytosis</subject><subject>Ferritins</subject><subject>fibroblasts</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunologic Techniques</subject><subject>Interferon Type I - metabolism</subject><subject>L cells</subject><subject>L Cells (Cell Line)</subject><subject>Ligands</subject><subject>Mice</subject><subject>Microscopy, Electron</subject><subject>Molecular and cellular biology</subject><subject>Nuclear Envelope - metabolism</subject><subject>Nuclear membrane</subject><subject>nuclear membranes</subject><subject>Receptors</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, Interferon</subject><subject>T lymphocytes</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EKkNhjYQEygLBKlP_JLGzYAFV-ZE6VEKwthz7urjKOIPtIPpafZA-E7YmjOgGVtbV-c71vfcg9JTgNcGcney8imtBc7FmVJB7aEVwT-qu6fF9tMKY8lo0tHmIHsV4hTHuW4GP0BEjbY9Ju0IXmzk4D5XzCYKFMPn69qb6Ahp2aQr1BoxTCUx15s2kr9MUXayUN9XnWY-gQrWB7RBUbvDOeeP85WP0wKoxwpPlPUbf3p99Pf1Yn198-HT69rzWreCpJlbDANQQg7XWdFCtMJ0xTTdYsK0yRFlBGm4NMDYo3IGgQ0e7BgTuBSeCHaM3-767ediC0eBTUKPcBbdV4VpOysm7inff5eX0U7Ke87bP_leLP0w_ZohJbl3UMI55l2mOkneElSP-FyQNIxyzAp7sQR2mGAPYwzAEy5KVLFlJQUtdssqO53_vcOCXcLL-ctFV1Gq0-c7axQPWk7JKwV4sWOn_R73zz-t_AtLO45jgV8rksz15FXP6B5S2bcfZb6wrwKM</recordid><startdate>19850501</startdate><enddate>19850501</enddate><creator>Kushnaryov, Vladimir M.</creator><creator>MacDonald, Hector S.</creator><creator>Sedmak, J. James</creator><creator>Grossberg, Sidney E.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19850501</creationdate><title>Murine interferon-β Receptor-Mediated Endocytosis and Nuclear Membrane Binding</title><author>Kushnaryov, Vladimir M. ; MacDonald, Hector S. ; Sedmak, J. James ; Grossberg, Sidney E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c587t-1fcebe2d1d0ccc2ba58d6dd46bfef5ad1af8147fde33ba06e82b6264e80987183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Animals</topic><topic>beta -interferon</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Cell membranes</topic><topic>Cell nucleus</topic><topic>Cell physiology</topic><topic>Cells</topic><topic>Coated Pits, Cell-Membrane - metabolism</topic><topic>Endocytosis</topic><topic>Ferritins</topic><topic>fibroblasts</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunologic Techniques</topic><topic>Interferon Type I - metabolism</topic><topic>L cells</topic><topic>L Cells (Cell Line)</topic><topic>Ligands</topic><topic>Mice</topic><topic>Microscopy, Electron</topic><topic>Molecular and cellular biology</topic><topic>Nuclear Envelope - metabolism</topic><topic>Nuclear membrane</topic><topic>nuclear membranes</topic><topic>Receptors</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, Interferon</topic><topic>T lymphocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kushnaryov, Vladimir M.</creatorcontrib><creatorcontrib>MacDonald, Hector S.</creatorcontrib><creatorcontrib>Sedmak, J. James</creatorcontrib><creatorcontrib>Grossberg, Sidney E.</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kushnaryov, Vladimir M.</au><au>MacDonald, Hector S.</au><au>Sedmak, J. James</au><au>Grossberg, Sidney E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Murine interferon-β Receptor-Mediated Endocytosis and Nuclear Membrane Binding</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1985-05-01</date><risdate>1985</risdate><volume>82</volume><issue>10</issue><spage>3281</spage><epage>3285</epage><pages>3281-3285</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Radioiodinated mouse interferon-β (125I-MuIFN-β ) bound with high affinity (Kd= 9.8 × 10-10M) to plasma membrane of L929murine fibroblasts (4-6 × 103receptor sites per cell). The binding was saturable and inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess mouse IFN-γ (MuIFN-γ ). MuIFN-β bound at 4 degrees C was very rapidly internalized upon warming of the cells to 37 degrees C (t1/2= 1.5 min). Indirect immunoferritin labeling indicated that MuIFN-β was initially located in coated pits and subsequently internalized by receptor-mediated endocytosis. Isolated L929cell nuclei bound125I-MuIFN-β with a 7-fold higher affinity (Kd= 1.4 × 10-10M) and higher receptor density (about 104per nucleus) than that for the plasma membrane. Binding to the nuclear membrane was inhibited by a 100-fold excess of unlabeled MuIFN-β but not by excess MuIFN-γ . Trypsin treatment of nuclei decreased IFN binding by 80%, suggesting that the putative nuclear receptors are protein. Specific binding of MuIFN-β to nuclei was also shown by fluorescence and electron microscopy. We propose that the very rapid internalization of MuIFN-β by receptor-mediated endocytosis is important in the cellular processing of IFN and that its high-affinity binding to the nuclear membrane suggests the nucleus as an intracellular site of IFN action.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3159015</pmid><doi>10.1073/pnas.82.10.3281</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1985-05, Vol.82 (10), p.3281-3285 |
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| language | eng |
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| subjects | Animals beta -interferon Biological and medical sciences Cell Membrane - metabolism Cell membranes Cell nucleus Cell physiology Cells Coated Pits, Cell-Membrane - metabolism Endocytosis Ferritins fibroblasts Fundamental and applied biological sciences. Psychology Immunologic Techniques Interferon Type I - metabolism L cells L Cells (Cell Line) Ligands Mice Microscopy, Electron Molecular and cellular biology Nuclear Envelope - metabolism Nuclear membrane nuclear membranes Receptors Receptors, Immunologic - metabolism Receptors, Interferon T lymphocytes |
| title | Murine interferon-β Receptor-Mediated Endocytosis and Nuclear Membrane Binding |
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