Localization and characterization of secretin binding sites expressed by rat bile duct epithelium
The goal of the present studies was to identify and characterize the site of secretin action in the liver. Sections of normal and bile duct-ligated rat livers were used for in vitro 125I-secretin receptor autoradiography. Saturable binding was observed in both normal and bile duct-ligated livers but...
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| Veröffentlicht in: | Gastroenterology (New York, N.Y. 1943) N.Y. 1943), 1992-03, Vol.102 (3), p.963-968 |
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| container_title | Gastroenterology (New York, N.Y. 1943) |
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| creator | Farouk, Marwan Vigna, Steven R. McVey, Douglas C. Meyers, William C. |
| description | The goal of the present studies was to identify and characterize the site of secretin action in the liver. Sections of normal and bile duct-ligated rat livers were used for in vitro 125I-secretin receptor autoradiography. Saturable binding was observed in both normal and bile duct-ligated livers but was much greater in the bile duct-ligated preparations. Binding was limited to biliary epithelium and the increased secretin binding observed in the ligated livers correlated with the increase in ductular tissue. Saturable binding was inhibited in a dose-dependent fashion by increasing concentrations of nonradioactive secretin. Analysis of saturation binding showed that 125I-secretin binding was best fit by a one-site receptor model with a Kd of 5.3 ± 1.1 nmol/L. Glucagon, vasoactive intestinal polypeptide, gastric inhibitory polypeptide, growth hormone-releasing hormone, and cholecystokinin did not inhibit saturable 125I-secretin binding at concentrations of 1 pmol/L to 1 μmol/L. The authors conclude that high-affinity, specific secretin binding sites are present in rat intrahepatic biliary epithelium. When bile ducts are stimulated to proliferate by bile duct ligation, secretin binding is also increased. |
| doi_str_mv | 10.1016/0016-5085(92)90183-Y |
| format | Article |
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Sections of normal and bile duct-ligated rat livers were used for in vitro 125I-secretin receptor autoradiography. Saturable binding was observed in both normal and bile duct-ligated livers but was much greater in the bile duct-ligated preparations. Binding was limited to biliary epithelium and the increased secretin binding observed in the ligated livers correlated with the increase in ductular tissue. Saturable binding was inhibited in a dose-dependent fashion by increasing concentrations of nonradioactive secretin. Analysis of saturation binding showed that 125I-secretin binding was best fit by a one-site receptor model with a Kd of 5.3 ± 1.1 nmol/L. Glucagon, vasoactive intestinal polypeptide, gastric inhibitory polypeptide, growth hormone-releasing hormone, and cholecystokinin did not inhibit saturable 125I-secretin binding at concentrations of 1 pmol/L to 1 μmol/L. The authors conclude that high-affinity, specific secretin binding sites are present in rat intrahepatic biliary epithelium. When bile ducts are stimulated to proliferate by bile duct ligation, secretin binding is also increased.</description><identifier>ISSN: 0016-5085</identifier><identifier>EISSN: 1528-0012</identifier><identifier>DOI: 10.1016/0016-5085(92)90183-Y</identifier><identifier>PMID: 1537532</identifier><identifier>CODEN: GASTAB</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Animals ; Autoradiography ; Bile Ducts - metabolism ; Binding Sites ; Binding, Competitive - drug effects ; Biological and medical sciences ; Cholecystokinin - pharmacology ; Dose-Response Relationship, Drug ; Epithelium - metabolism ; Fundamental and applied biological sciences. Psychology ; Gastric Inhibitory Polypeptide - pharmacology ; Glucagon - pharmacology ; Growth Hormone-Releasing Hormone - pharmacology ; Hyperplasia - metabolism ; Liver - metabolism ; Liver - pathology ; Male ; Rats ; Rats, Inbred Strains ; Receptors, G-Protein-Coupled ; Receptors, Gastrointestinal Hormone - biosynthesis ; Secretin - metabolism ; Vasoactive Intestinal Peptide - pharmacology ; Vertebrates: digestive system</subject><ispartof>Gastroenterology (New York, N.Y. 1943), 1992-03, Vol.102 (3), p.963-968</ispartof><rights>1992</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c498t-1dd1eaee8a479774c79febbf132942e1e4e79cc85c4e539cd6766d67ec073e5e3</citedby><cites>FETCH-LOGICAL-c498t-1dd1eaee8a479774c79febbf132942e1e4e79cc85c4e539cd6766d67ec073e5e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0016-5085(92)90183-Y$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4311908$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1537532$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Farouk, Marwan</creatorcontrib><creatorcontrib>Vigna, Steven R.</creatorcontrib><creatorcontrib>McVey, Douglas C.</creatorcontrib><creatorcontrib>Meyers, William C.</creatorcontrib><title>Localization and characterization of secretin binding sites expressed by rat bile duct epithelium</title><title>Gastroenterology (New York, N.Y. 1943)</title><addtitle>Gastroenterology</addtitle><description>The goal of the present studies was to identify and characterize the site of secretin action in the liver. Sections of normal and bile duct-ligated rat livers were used for in vitro 125I-secretin receptor autoradiography. Saturable binding was observed in both normal and bile duct-ligated livers but was much greater in the bile duct-ligated preparations. Binding was limited to biliary epithelium and the increased secretin binding observed in the ligated livers correlated with the increase in ductular tissue. Saturable binding was inhibited in a dose-dependent fashion by increasing concentrations of nonradioactive secretin. Analysis of saturation binding showed that 125I-secretin binding was best fit by a one-site receptor model with a Kd of 5.3 ± 1.1 nmol/L. Glucagon, vasoactive intestinal polypeptide, gastric inhibitory polypeptide, growth hormone-releasing hormone, and cholecystokinin did not inhibit saturable 125I-secretin binding at concentrations of 1 pmol/L to 1 μmol/L. The authors conclude that high-affinity, specific secretin binding sites are present in rat intrahepatic biliary epithelium. When bile ducts are stimulated to proliferate by bile duct ligation, secretin binding is also increased.</description><subject>Animals</subject><subject>Autoradiography</subject><subject>Bile Ducts - metabolism</subject><subject>Binding Sites</subject><subject>Binding, Competitive - drug effects</subject><subject>Biological and medical sciences</subject><subject>Cholecystokinin - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Epithelium - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gastric Inhibitory Polypeptide - pharmacology</subject><subject>Glucagon - pharmacology</subject><subject>Growth Hormone-Releasing Hormone - pharmacology</subject><subject>Hyperplasia - metabolism</subject><subject>Liver - metabolism</subject><subject>Liver - pathology</subject><subject>Male</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Receptors, Gastrointestinal Hormone - biosynthesis</subject><subject>Secretin - metabolism</subject><subject>Vasoactive Intestinal Peptide - pharmacology</subject><subject>Vertebrates: digestive system</subject><issn>0016-5085</issn><issn>1528-0012</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1P3DAQhq2Kallo_0GRfEAIDmntOIntCxJCfEkr9dIeOFnOeFKMssliOwj49fV2t8uNy4w07zOj0UPIN86-c8abHyyXomaqPtXlmWZcieL-E5nzulRFzso9Mt8h--QgxkfGmBaKz8iM10LWopwTuxjB9v7NJj8O1A6OwoMNFhKG_8OxoxEhYPIDbf3g_PCHRp8wUnxZBYwRHW1fabApxz1SN0GiuPLpAXs_Lb-Qz53tI37d9kPy-_rq1-Vtsfh5c3d5sSig0ioV3DmOFlHZSmopK5C6w7btuCh1VSLHCqUGUDVUWAsNrpFNkwsCkwJrFIfkZHN3FcanCWMySx8B-94OOE7RyFLxhkmewWoDQhhjDNiZVfBLG14NZ2Zt1qy1mbU2o0vzz6y5z2tH2_tTu0T3vrRRmfPjbW5jVtoFO4CPO6wSnGumMna-wTC7ePYYTASPA6DzASEZN_qP__gLmYiWoA</recordid><startdate>19920301</startdate><enddate>19920301</enddate><creator>Farouk, Marwan</creator><creator>Vigna, Steven R.</creator><creator>McVey, Douglas C.</creator><creator>Meyers, William C.</creator><general>Elsevier Inc</general><general>Elsevier</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>19920301</creationdate><title>Localization and characterization of secretin binding sites expressed by rat bile duct epithelium</title><author>Farouk, Marwan ; Vigna, Steven R. ; McVey, Douglas C. ; Meyers, William C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-1dd1eaee8a479774c79febbf132942e1e4e79cc85c4e539cd6766d67ec073e5e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Autoradiography</topic><topic>Bile Ducts - metabolism</topic><topic>Binding Sites</topic><topic>Binding, Competitive - drug effects</topic><topic>Biological and medical sciences</topic><topic>Cholecystokinin - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Epithelium - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gastric Inhibitory Polypeptide - pharmacology</topic><topic>Glucagon - pharmacology</topic><topic>Growth Hormone-Releasing Hormone - pharmacology</topic><topic>Hyperplasia - metabolism</topic><topic>Liver - metabolism</topic><topic>Liver - pathology</topic><topic>Male</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Receptors, G-Protein-Coupled</topic><topic>Receptors, Gastrointestinal Hormone - biosynthesis</topic><topic>Secretin - metabolism</topic><topic>Vasoactive Intestinal Peptide - pharmacology</topic><topic>Vertebrates: digestive system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Farouk, Marwan</creatorcontrib><creatorcontrib>Vigna, Steven R.</creatorcontrib><creatorcontrib>McVey, Douglas C.</creatorcontrib><creatorcontrib>Meyers, William C.</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>Gastroenterology (New York, N.Y. 1943)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Farouk, Marwan</au><au>Vigna, Steven R.</au><au>McVey, Douglas C.</au><au>Meyers, William C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization and characterization of secretin binding sites expressed by rat bile duct epithelium</atitle><jtitle>Gastroenterology (New York, N.Y. 1943)</jtitle><addtitle>Gastroenterology</addtitle><date>1992-03-01</date><risdate>1992</risdate><volume>102</volume><issue>3</issue><spage>963</spage><epage>968</epage><pages>963-968</pages><issn>0016-5085</issn><eissn>1528-0012</eissn><coden>GASTAB</coden><abstract>The goal of the present studies was to identify and characterize the site of secretin action in the liver. Sections of normal and bile duct-ligated rat livers were used for in vitro 125I-secretin receptor autoradiography. Saturable binding was observed in both normal and bile duct-ligated livers but was much greater in the bile duct-ligated preparations. Binding was limited to biliary epithelium and the increased secretin binding observed in the ligated livers correlated with the increase in ductular tissue. Saturable binding was inhibited in a dose-dependent fashion by increasing concentrations of nonradioactive secretin. Analysis of saturation binding showed that 125I-secretin binding was best fit by a one-site receptor model with a Kd of 5.3 ± 1.1 nmol/L. Glucagon, vasoactive intestinal polypeptide, gastric inhibitory polypeptide, growth hormone-releasing hormone, and cholecystokinin did not inhibit saturable 125I-secretin binding at concentrations of 1 pmol/L to 1 μmol/L. The authors conclude that high-affinity, specific secretin binding sites are present in rat intrahepatic biliary epithelium. When bile ducts are stimulated to proliferate by bile duct ligation, secretin binding is also increased.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>1537532</pmid><doi>10.1016/0016-5085(92)90183-Y</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Gastroenterology (New York, N.Y. 1943), 1992-03, Vol.102 (3), p.963-968 |
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| language | eng |
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| subjects | Animals Autoradiography Bile Ducts - metabolism Binding Sites Binding, Competitive - drug effects Biological and medical sciences Cholecystokinin - pharmacology Dose-Response Relationship, Drug Epithelium - metabolism Fundamental and applied biological sciences. Psychology Gastric Inhibitory Polypeptide - pharmacology Glucagon - pharmacology Growth Hormone-Releasing Hormone - pharmacology Hyperplasia - metabolism Liver - metabolism Liver - pathology Male Rats Rats, Inbred Strains Receptors, G-Protein-Coupled Receptors, Gastrointestinal Hormone - biosynthesis Secretin - metabolism Vasoactive Intestinal Peptide - pharmacology Vertebrates: digestive system |
| title | Localization and characterization of secretin binding sites expressed by rat bile duct epithelium |
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