cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro
The complement protein C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 12...
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| Veröffentlicht in: | Immunity (Cambridge, Mass.) Mass.), 1997-02, Vol.6 (2), p.119-129 |
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| container_title | Immunity (Cambridge, Mass.) |
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| creator | Nepomuceno, R R Henschen-Edman, A H Burgess, W H Tenner, A J |
| description | The complement protein C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 126,000 M(r) cell surface protein designated C1qR(P). Amino acid sequence was obtained and the corresponding cDNA was cloned. C1qR(P) is a novel type I membrane protein with the following putative structural elements: a C-type carbohydrate recognition domain, five EGF-like domains, a transmembrane domain, and a short cytoplasmic tail. All peptides identified by amino acid sequencing are encoded by the cDNA. Additionally, an anti-peptide antiserum was generated, which is reactive with C1qR(P). The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis. |
| doi_str_mv | 10.1016/S1074-7613(00)80419-7 |
| format | Article |
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Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 126,000 M(r) cell surface protein designated C1qR(P). Amino acid sequence was obtained and the corresponding cDNA was cloned. C1qR(P) is a novel type I membrane protein with the following putative structural elements: a C-type carbohydrate recognition domain, five EGF-like domains, a transmembrane domain, and a short cytoplasmic tail. All peptides identified by amino acid sequencing are encoded by the cDNA. Additionally, an anti-peptide antiserum was generated, which is reactive with C1qR(P). The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis.</description><identifier>ISSN: 1074-7613</identifier><identifier>DOI: 10.1016/S1074-7613(00)80419-7</identifier><identifier>PMID: 9047234</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Base Sequence ; Carrier Proteins - metabolism ; Cloning, Molecular ; Collectins ; Complement Activating Enzymes - analysis ; Complement Activating Enzymes - metabolism ; Complement Activating Enzymes - physiology ; DNA, Complementary - analysis ; Humans ; Hyaluronan Receptors ; Lymphoma, Large B-Cell, Diffuse ; Macrophage Activation - physiology ; Membrane Glycoproteins ; Mitochondrial Proteins ; Molecular Sequence Data ; Phagocytosis - physiology ; Pulmonary Surfactants - metabolism ; Receptors, Complement - analysis ; Receptors, Complement - metabolism ; Receptors, Complement - physiology ; Receptors, Immunologic - analysis ; Receptors, Immunologic - metabolism ; Tumor Cells, Cultured</subject><ispartof>Immunity (Cambridge, Mass.), 1997-02, Vol.6 (2), p.119-129</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27931,27932</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9047234$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nepomuceno, R R</creatorcontrib><creatorcontrib>Henschen-Edman, A H</creatorcontrib><creatorcontrib>Burgess, W H</creatorcontrib><creatorcontrib>Tenner, A J</creatorcontrib><title>cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro</title><title>Immunity (Cambridge, Mass.)</title><addtitle>Immunity</addtitle><description>The complement protein C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. 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The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Carrier Proteins - metabolism</subject><subject>Cloning, Molecular</subject><subject>Collectins</subject><subject>Complement Activating Enzymes - analysis</subject><subject>Complement Activating Enzymes - metabolism</subject><subject>Complement Activating Enzymes - physiology</subject><subject>DNA, Complementary - analysis</subject><subject>Humans</subject><subject>Hyaluronan Receptors</subject><subject>Lymphoma, Large B-Cell, Diffuse</subject><subject>Macrophage Activation - physiology</subject><subject>Membrane Glycoproteins</subject><subject>Mitochondrial Proteins</subject><subject>Molecular Sequence Data</subject><subject>Phagocytosis - physiology</subject><subject>Pulmonary Surfactants - metabolism</subject><subject>Receptors, Complement - analysis</subject><subject>Receptors, Complement - metabolism</subject><subject>Receptors, Complement - physiology</subject><subject>Receptors, Immunologic - analysis</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>1074-7613</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF1LwzAUhnOhzDn9CYNcyQbW5atNeznnJ0wdTq9LmqZrpU26JBV27R-3w-LV4Tzn5YHzAjDF6AYjHC22GHEW8AjTGULzGDGcBPwEjP_xGTh37gshzMIEjcAoQYwTysbgR969LqGsja70Dgqdw9ZWjbAH6LztpO-s6qmoD65y0BRwhffvs838GvpSwbJrhD6ixcvterHdLKFVUrXe2P4sPGxUXgmvHFS6FFqqXl6KnZEHb466SsPvyltzAU4LUTt1OcwJ-Hy4_1g9Beu3x-fVch20BEU-oAXJZUEylogkYjwpqMRhwVm_yCSOCec9zwjJcspxmGGBMkREKMOcKlrkkk7A1Z-3tWbfKefTpnJS1bXQynQu5XEcsjhEfXA6BLus_yEdKkmH1ugvxW9t-w</recordid><startdate>19970201</startdate><enddate>19970201</enddate><creator>Nepomuceno, R R</creator><creator>Henschen-Edman, A H</creator><creator>Burgess, W H</creator><creator>Tenner, A J</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19970201</creationdate><title>cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro</title><author>Nepomuceno, R R ; Henschen-Edman, A H ; Burgess, W H ; Tenner, A J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p206t-3f2dcf2b49a96479f3c15f74964c988277a96b22bd3715b1a0b02a5c5d3e3fdc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Carrier Proteins - metabolism</topic><topic>Cloning, Molecular</topic><topic>Collectins</topic><topic>Complement Activating Enzymes - analysis</topic><topic>Complement Activating Enzymes - metabolism</topic><topic>Complement Activating Enzymes - physiology</topic><topic>DNA, Complementary - analysis</topic><topic>Humans</topic><topic>Hyaluronan Receptors</topic><topic>Lymphoma, Large B-Cell, Diffuse</topic><topic>Macrophage Activation - physiology</topic><topic>Membrane Glycoproteins</topic><topic>Mitochondrial Proteins</topic><topic>Molecular Sequence Data</topic><topic>Phagocytosis - physiology</topic><topic>Pulmonary Surfactants - metabolism</topic><topic>Receptors, Complement - analysis</topic><topic>Receptors, Complement - metabolism</topic><topic>Receptors, Complement - physiology</topic><topic>Receptors, Immunologic - analysis</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nepomuceno, R R</creatorcontrib><creatorcontrib>Henschen-Edman, A H</creatorcontrib><creatorcontrib>Burgess, W H</creatorcontrib><creatorcontrib>Tenner, A J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Immunity (Cambridge, Mass.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nepomuceno, R R</au><au>Henschen-Edman, A H</au><au>Burgess, W H</au><au>Tenner, A J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro</atitle><jtitle>Immunity (Cambridge, Mass.)</jtitle><addtitle>Immunity</addtitle><date>1997-02-01</date><risdate>1997</risdate><volume>6</volume><issue>2</issue><spage>119</spage><epage>129</epage><pages>119-129</pages><issn>1074-7613</issn><abstract>The complement protein C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 126,000 M(r) cell surface protein designated C1qR(P). Amino acid sequence was obtained and the corresponding cDNA was cloned. C1qR(P) is a novel type I membrane protein with the following putative structural elements: a C-type carbohydrate recognition domain, five EGF-like domains, a transmembrane domain, and a short cytoplasmic tail. All peptides identified by amino acid sequencing are encoded by the cDNA. Additionally, an anti-peptide antiserum was generated, which is reactive with C1qR(P). The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis.</abstract><cop>United States</cop><pmid>9047234</pmid><doi>10.1016/S1074-7613(00)80419-7</doi><tpages>11</tpages></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Sequence Base Sequence Carrier Proteins - metabolism Cloning, Molecular Collectins Complement Activating Enzymes - analysis Complement Activating Enzymes - metabolism Complement Activating Enzymes - physiology DNA, Complementary - analysis Humans Hyaluronan Receptors Lymphoma, Large B-Cell, Diffuse Macrophage Activation - physiology Membrane Glycoproteins Mitochondrial Proteins Molecular Sequence Data Phagocytosis - physiology Pulmonary Surfactants - metabolism Receptors, Complement - analysis Receptors, Complement - metabolism Receptors, Complement - physiology Receptors, Immunologic - analysis Receptors, Immunologic - metabolism Tumor Cells, Cultured |
| title | cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro |
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