Identification of the hepatic asialo-glycoprotein receptor (hepatic lectin) as a component of liver specific membrane lipoprotein (LSP)
Liver specific membrane lipoprotein (LSP), the target for anti-LSP antibodies in various liver diseases, is thought to be comprised of fragments of the hepatocellular plasma membrane. In the present study, therefore, evidence has been sought for the presence in LSP of the hepatocyte surface receptor...
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Veröffentlicht in: | Clinical and experimental immunology 1984-02, Vol.55 (2), p.347-354 |
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creator | MCFARLANE, I. G. M MCFARLANE, B. M MAJOR, G. N TOLLEY, P WILLIAMS, R |
description | Liver specific membrane lipoprotein (LSP), the target for anti-LSP antibodies in various liver diseases, is thought to be comprised of fragments of the hepatocellular plasma membrane. In the present study, therefore, evidence has been sought for the presence in LSP of the hepatocyte surface receptor (hepatic lectin) that binds desialylated glycoproteins. Eight guinea-pig anti-LSP antisera (four anti-human and four anti-rabbit LSP) were found to react by ELISA and/or RIA against affinity purified human and rabbit hepatic lectin. Binding of the antisera to 125I-hepatic lectins was inhibited by the unlabelled lectins, by human and rabbit LSP and by purified rabbit liver plasma membranes but not by a 50,000-fold excess of kidney homogenate. The results indicate that hepatic lectin is a liver specific, species cross-reactive antigen comprising about 0.25% of the protein in LSP. |
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G. M ; MCFARLANE, B. M ; MAJOR, G. N ; TOLLEY, P ; WILLIAMS, R</creator><creatorcontrib>MCFARLANE, I. G. M ; MCFARLANE, B. M ; MAJOR, G. N ; TOLLEY, P ; WILLIAMS, R</creatorcontrib><description>Liver specific membrane lipoprotein (LSP), the target for anti-LSP antibodies in various liver diseases, is thought to be comprised of fragments of the hepatocellular plasma membrane. In the present study, therefore, evidence has been sought for the presence in LSP of the hepatocyte surface receptor (hepatic lectin) that binds desialylated glycoproteins. Eight guinea-pig anti-LSP antisera (four anti-human and four anti-rabbit LSP) were found to react by ELISA and/or RIA against affinity purified human and rabbit hepatic lectin. Binding of the antisera to 125I-hepatic lectins was inhibited by the unlabelled lectins, by human and rabbit LSP and by purified rabbit liver plasma membranes but not by a 50,000-fold excess of kidney homogenate. The results indicate that hepatic lectin is a liver specific, species cross-reactive antigen comprising about 0.25% of the protein in LSP.</description><identifier>ISSN: 0009-9104</identifier><identifier>EISSN: 1365-2249</identifier><identifier>PMID: 6199139</identifier><identifier>CODEN: CEXIAL</identifier><language>eng</language><publisher>Oxford: Blackwell</publisher><subject>Animals ; Antigen-Antibody Reactions ; Antigens, Surface - analysis ; Asialoglycoprotein Receptor ; Biological and medical sciences ; Cross Reactions ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; glycoproteins ; guinea-pigs ; hepatocytes ; Humans ; immunological diseases ; Lectins - analysis ; Lectins - immunology ; Lipoproteins ; Liver - immunology ; Membrane Proteins ; plasma membranes ; Proteins ; Rabbits ; Radioimmunoassay ; receptors ; Receptors, Cell Surface - analysis ; Receptors, Cell Surface - immunology ; Tissue, organ and graft immunology</subject><ispartof>Clinical and experimental immunology, 1984-02, Vol.55 (2), p.347-354</ispartof><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1535812/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1535812/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9590915$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6199139$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MCFARLANE, I. G. M</creatorcontrib><creatorcontrib>MCFARLANE, B. M</creatorcontrib><creatorcontrib>MAJOR, G. N</creatorcontrib><creatorcontrib>TOLLEY, P</creatorcontrib><creatorcontrib>WILLIAMS, R</creatorcontrib><title>Identification of the hepatic asialo-glycoprotein receptor (hepatic lectin) as a component of liver specific membrane lipoprotein (LSP)</title><title>Clinical and experimental immunology</title><addtitle>Clin Exp Immunol</addtitle><description>Liver specific membrane lipoprotein (LSP), the target for anti-LSP antibodies in various liver diseases, is thought to be comprised of fragments of the hepatocellular plasma membrane. In the present study, therefore, evidence has been sought for the presence in LSP of the hepatocyte surface receptor (hepatic lectin) that binds desialylated glycoproteins. Eight guinea-pig anti-LSP antisera (four anti-human and four anti-rabbit LSP) were found to react by ELISA and/or RIA against affinity purified human and rabbit hepatic lectin. Binding of the antisera to 125I-hepatic lectins was inhibited by the unlabelled lectins, by human and rabbit LSP and by purified rabbit liver plasma membranes but not by a 50,000-fold excess of kidney homogenate. The results indicate that hepatic lectin is a liver specific, species cross-reactive antigen comprising about 0.25% of the protein in LSP.</description><subject>Animals</subject><subject>Antigen-Antibody Reactions</subject><subject>Antigens, Surface - analysis</subject><subject>Asialoglycoprotein Receptor</subject><subject>Biological and medical sciences</subject><subject>Cross Reactions</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>glycoproteins</subject><subject>guinea-pigs</subject><subject>hepatocytes</subject><subject>Humans</subject><subject>immunological diseases</subject><subject>Lectins - analysis</subject><subject>Lectins - immunology</subject><subject>Lipoproteins</subject><subject>Liver - immunology</subject><subject>Membrane Proteins</subject><subject>plasma membranes</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Radioimmunoassay</subject><subject>receptors</subject><subject>Receptors, Cell Surface - analysis</subject><subject>Receptors, Cell Surface - immunology</subject><subject>Tissue, organ and graft immunology</subject><issn>0009-9104</issn><issn>1365-2249</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFq3DAQhk1pSTdpH6GgQyjJwWBJlqO5FEJIm8BCC23PRh6PsyqypUraQJ4grx0t2SzpqScx8__zzS_pTbXislO1EC28rVZN00ANvGnfV8cp_Sll13XiqDrqOACXsKoeb0dasp0smmz9wvzE8obYhkKpkZlkjfP1nXtAH6LPZBcWCSlkH9nZi8sRZrucFzczDP0c_FKgO5az9xRZCoS7FWymeYhmodIPB97Z-ueP8w_Vu8m4RB_350n1--v1r6ubev392-3V5boOUvBc0witHgY5KYCRIzagFUpuuBYjkhLYcDGRQT1KBainCz4qTtoADhJkK-RJ9eWZG7bDTGVmydG4PkQ7m_jQe2P7f5XFbvo7f99zJZXmO8DnPSD6v1tKuZ9tQnKuXMtvU68bUEpc_N_IpW45F20xfnod6ZBl_0dFP93rJqFxU3lAtOlgAwUNlHRPk7OetQ</recordid><startdate>19840201</startdate><enddate>19840201</enddate><creator>MCFARLANE, I. G. M</creator><creator>MCFARLANE, B. M</creator><creator>MAJOR, G. N</creator><creator>TOLLEY, P</creator><creator>WILLIAMS, R</creator><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19840201</creationdate><title>Identification of the hepatic asialo-glycoprotein receptor (hepatic lectin) as a component of liver specific membrane lipoprotein (LSP)</title><author>MCFARLANE, I. G. M ; MCFARLANE, B. M ; MAJOR, G. N ; TOLLEY, P ; WILLIAMS, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p321t-ed948bb3f599d1cc0985c31a182dce52c012feac8d359c8f71d51e8a9cb393423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Animals</topic><topic>Antigen-Antibody Reactions</topic><topic>Antigens, Surface - analysis</topic><topic>Asialoglycoprotein Receptor</topic><topic>Biological and medical sciences</topic><topic>Cross Reactions</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>glycoproteins</topic><topic>guinea-pigs</topic><topic>hepatocytes</topic><topic>Humans</topic><topic>immunological diseases</topic><topic>Lectins - analysis</topic><topic>Lectins - immunology</topic><topic>Lipoproteins</topic><topic>Liver - immunology</topic><topic>Membrane Proteins</topic><topic>plasma membranes</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Radioimmunoassay</topic><topic>receptors</topic><topic>Receptors, Cell Surface - analysis</topic><topic>Receptors, Cell Surface - immunology</topic><topic>Tissue, organ and graft immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MCFARLANE, I. G. M</creatorcontrib><creatorcontrib>MCFARLANE, B. M</creatorcontrib><creatorcontrib>MAJOR, G. N</creatorcontrib><creatorcontrib>TOLLEY, P</creatorcontrib><creatorcontrib>WILLIAMS, R</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>Immunology Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Clinical and experimental immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MCFARLANE, I. G. M</au><au>MCFARLANE, B. M</au><au>MAJOR, G. N</au><au>TOLLEY, P</au><au>WILLIAMS, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of the hepatic asialo-glycoprotein receptor (hepatic lectin) as a component of liver specific membrane lipoprotein (LSP)</atitle><jtitle>Clinical and experimental immunology</jtitle><addtitle>Clin Exp Immunol</addtitle><date>1984-02-01</date><risdate>1984</risdate><volume>55</volume><issue>2</issue><spage>347</spage><epage>354</epage><pages>347-354</pages><issn>0009-9104</issn><eissn>1365-2249</eissn><coden>CEXIAL</coden><abstract>Liver specific membrane lipoprotein (LSP), the target for anti-LSP antibodies in various liver diseases, is thought to be comprised of fragments of the hepatocellular plasma membrane. In the present study, therefore, evidence has been sought for the presence in LSP of the hepatocyte surface receptor (hepatic lectin) that binds desialylated glycoproteins. Eight guinea-pig anti-LSP antisera (four anti-human and four anti-rabbit LSP) were found to react by ELISA and/or RIA against affinity purified human and rabbit hepatic lectin. Binding of the antisera to 125I-hepatic lectins was inhibited by the unlabelled lectins, by human and rabbit LSP and by purified rabbit liver plasma membranes but not by a 50,000-fold excess of kidney homogenate. The results indicate that hepatic lectin is a liver specific, species cross-reactive antigen comprising about 0.25% of the protein in LSP.</abstract><cop>Oxford</cop><pub>Blackwell</pub><pmid>6199139</pmid><tpages>8</tpages></addata></record> |
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subjects | Animals Antigen-Antibody Reactions Antigens, Surface - analysis Asialoglycoprotein Receptor Biological and medical sciences Cross Reactions Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Epitopes Fundamental and applied biological sciences. Psychology Fundamental immunology glycoproteins guinea-pigs hepatocytes Humans immunological diseases Lectins - analysis Lectins - immunology Lipoproteins Liver - immunology Membrane Proteins plasma membranes Proteins Rabbits Radioimmunoassay receptors Receptors, Cell Surface - analysis Receptors, Cell Surface - immunology Tissue, organ and graft immunology |
title | Identification of the hepatic asialo-glycoprotein receptor (hepatic lectin) as a component of liver specific membrane lipoprotein (LSP) |
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