Different Endothelin Receptor Affinities in Dog Tissues
Abstract Endothelin (ET) is a long-lasting potent vasoconstrictor-peptide. Here we report different binding affinities of endothelin-1 (ET-1) to ET-receptors of various dog tissues. Crude microsomal fractions were prepared after homogenisation of dog tissues in 50 mM Tris/HCl, 20 mM MnCl2, 1 mM EDTA...
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| Veröffentlicht in: | Journal of receptor research 1991, Vol.11 (1-4), p.293-298 |
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| creator | LOFFLER, B.-M LOHRER, W |
| description | Abstract
Endothelin (ET) is a long-lasting potent vasoconstrictor-peptide. Here we report different binding affinities of endothelin-1 (ET-1) to ET-receptors of various dog tissues. Crude microsomal fractions were prepared after homogenisation of dog tissues in 50 mM Tris/HCl, 20 mM MnCl2, 1 mM EDTA, pH 7.4 by differential centrifugation. Aliquots of microsomal fractions (70 u.g of protein) were incubated at 25°C for 180 min in the presence of 20 pM125I-ET-1 and various concentrations of cold ET-1. Four different ET-1 receptor binding affinities were found: adrenals, cerebrum, liver, heart, skeletal muscle and stomach microsomal membranes contained high affinity binding sites (Kd 50 - 80 pM, Bmax 60 - 250 fmol/mg). In cerebellum and spleen medium affinity ET-1 receptors (Kd 350 pM, Bmax 880 and 1200 fmol/mg respectively) were present. In comparison lung and kidney microsomes contained a low affinity ET-1 receptor (Kd 800 and 880 pM, Bmax 1600 and 350 fmol/mg). Receptors of even lower affinity were present in heart, intestine and liver microsomes with Kd values of 3 - 6 nM. |
| doi_str_mv | 10.3109/10799899109066408 |
| format | Article |
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Endothelin (ET) is a long-lasting potent vasoconstrictor-peptide. Here we report different binding affinities of endothelin-1 (ET-1) to ET-receptors of various dog tissues. Crude microsomal fractions were prepared after homogenisation of dog tissues in 50 mM Tris/HCl, 20 mM MnCl2, 1 mM EDTA, pH 7.4 by differential centrifugation. Aliquots of microsomal fractions (70 u.g of protein) were incubated at 25°C for 180 min in the presence of 20 pM125I-ET-1 and various concentrations of cold ET-1. Four different ET-1 receptor binding affinities were found: adrenals, cerebrum, liver, heart, skeletal muscle and stomach microsomal membranes contained high affinity binding sites (Kd 50 - 80 pM, Bmax 60 - 250 fmol/mg). In cerebellum and spleen medium affinity ET-1 receptors (Kd 350 pM, Bmax 880 and 1200 fmol/mg respectively) were present. In comparison lung and kidney microsomes contained a low affinity ET-1 receptor (Kd 800 and 880 pM, Bmax 1600 and 350 fmol/mg). Receptors of even lower affinity were present in heart, intestine and liver microsomes with Kd values of 3 - 6 nM.</description><identifier>ISSN: 1079-9893</identifier><identifier>ISSN: 0197-5110</identifier><identifier>EISSN: 1532-4281</identifier><identifier>DOI: 10.3109/10799899109066408</identifier><identifier>PMID: 1653335</identifier><identifier>CODEN: JRERDM</identifier><language>eng</language><publisher>Basel: Informa UK Ltd</publisher><subject>550201 - Biochemistry- Tracer Techniques ; AFFINITY ; ANIMAL TISSUES ; ANIMALS ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BIOCHEMICAL REACTION KINETICS ; Biological and medical sciences ; BODY ; CELL CONSTITUENTS ; Cell receptors ; Cell structures and functions ; CENTRIFUGATION ; DAYS LIVING RADIOISOTOPES ; DOGS ; ELECTRON CAPTURE RADIOISOTOPES ; Endothelins - metabolism ; Fundamental and applied biological sciences. Psychology ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; INTERMEDIATE MASS NUCLEI ; INTERNAL CONVERSION RADIOISOTOPES ; IODINE 125 ; IODINE ISOTOPES ; Iodine Radioisotopes ; ISOTOPE APPLICATIONS ; ISOTOPES ; KINETICS ; MAMMALS ; MEMBRANE PROTEINS ; MICROSOMES ; Molecular and cellular biology ; NUCLEI ; ODD-EVEN NUCLEI ; Organ Specificity ; ORGANIC COMPOUNDS ; ORGANS ; PEPTIDES ; PROTEINS ; RADIOISOTOPES ; REACTION KINETICS ; RECEPTORS ; Receptors, Cell Surface - metabolism ; Receptors, Endothelin ; RIBOSOMES ; SEPARATION PROCESSES ; SPECIFICITY ; TISSUES ; TRACER TECHNIQUES ; ULTRACENTRIFUGATION ; VERTEBRATES</subject><ispartof>Journal of receptor research, 1991, Vol.11 (1-4), p.293-298</ispartof><rights>1991 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 1991</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c489t-9ae9a98b25d66ec0b81b73be0206454fd3f566112b76679b6a0beb20ff14663b3</citedby><cites>FETCH-LOGICAL-c489t-9ae9a98b25d66ec0b81b73be0206454fd3f566112b76679b6a0beb20ff14663b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.3109/10799899109066408$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.3109/10799899109066408$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>230,309,310,314,777,781,786,787,882,4010,4036,4037,23911,23912,25121,27904,27905,27906,59626,60415,61200,61235,61381,61416</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19695504$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1653335$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/5017625$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>LOFFLER, B.-M</creatorcontrib><creatorcontrib>LOHRER, W</creatorcontrib><title>Different Endothelin Receptor Affinities in Dog Tissues</title><title>Journal of receptor research</title><addtitle>J Recept Res</addtitle><description>Abstract
Endothelin (ET) is a long-lasting potent vasoconstrictor-peptide. Here we report different binding affinities of endothelin-1 (ET-1) to ET-receptors of various dog tissues. Crude microsomal fractions were prepared after homogenisation of dog tissues in 50 mM Tris/HCl, 20 mM MnCl2, 1 mM EDTA, pH 7.4 by differential centrifugation. Aliquots of microsomal fractions (70 u.g of protein) were incubated at 25°C for 180 min in the presence of 20 pM125I-ET-1 and various concentrations of cold ET-1. Four different ET-1 receptor binding affinities were found: adrenals, cerebrum, liver, heart, skeletal muscle and stomach microsomal membranes contained high affinity binding sites (Kd 50 - 80 pM, Bmax 60 - 250 fmol/mg). In cerebellum and spleen medium affinity ET-1 receptors (Kd 350 pM, Bmax 880 and 1200 fmol/mg respectively) were present. In comparison lung and kidney microsomes contained a low affinity ET-1 receptor (Kd 800 and 880 pM, Bmax 1600 and 350 fmol/mg). Receptors of even lower affinity were present in heart, intestine and liver microsomes with Kd values of 3 - 6 nM.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>AFFINITY</subject><subject>ANIMAL TISSUES</subject><subject>ANIMALS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BIOCHEMICAL REACTION KINETICS</subject><subject>Biological and medical sciences</subject><subject>BODY</subject><subject>CELL CONSTITUENTS</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>CENTRIFUGATION</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DOGS</subject><subject>ELECTRON CAPTURE RADIOISOTOPES</subject><subject>Endothelins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>INTERMEDIATE MASS NUCLEI</subject><subject>INTERNAL CONVERSION RADIOISOTOPES</subject><subject>IODINE 125</subject><subject>IODINE ISOTOPES</subject><subject>Iodine Radioisotopes</subject><subject>ISOTOPE APPLICATIONS</subject><subject>ISOTOPES</subject><subject>KINETICS</subject><subject>MAMMALS</subject><subject>MEMBRANE PROTEINS</subject><subject>MICROSOMES</subject><subject>Molecular and cellular biology</subject><subject>NUCLEI</subject><subject>ODD-EVEN NUCLEI</subject><subject>Organ Specificity</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANS</subject><subject>PEPTIDES</subject><subject>PROTEINS</subject><subject>RADIOISOTOPES</subject><subject>REACTION KINETICS</subject><subject>RECEPTORS</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Endothelin</subject><subject>RIBOSOMES</subject><subject>SEPARATION PROCESSES</subject><subject>SPECIFICITY</subject><subject>TISSUES</subject><subject>TRACER TECHNIQUES</subject><subject>ULTRACENTRIFUGATION</subject><subject>VERTEBRATES</subject><issn>1079-9893</issn><issn>0197-5110</issn><issn>1532-4281</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rFTEQxYMota1-AB-ERdC31UmyyW7Ql9LWP1AQpD6HJDvxpuxNrkku0m9vZG8pItSnGeb8zjA5IeQFhbecgnpHYVRqUqr1IOUA0yNyTAVn_cAm-rj1Te8bwJ-Sk1JuAKgaKRyRIyoF51wck_EieI8ZY-0u45zqBpcQu2_ocFdT7s68DzHUgKVr44v0o7sOpeyxPCNPvFkKPj_UU_L94-X1-ef-6uunL-dnV70bJlV7ZVAZNVkmZinRgZ2oHblFYCAHMfiZeyElpcyOUo7KSgMWLQPv6SAlt_yUvFr3plKDLi5UdBuXYkRXtQA6SiYa9GaFdjn9bMdVvQ3F4bKYiGlf9MhgGoD_H6RCTUwo2UC6gi6nUjJ6vctha_KtpqD_RK__ib55Xh6W7-0W53vHmnXTXx90U5xZfDbRhXKPKamEgKFxH1YuRJ_y1vxKeZl1NbdLyncm_tAZ7_-yb9AsdeNMRn2T9jm233rgEb8BoFmucA</recordid><startdate>1991</startdate><enddate>1991</enddate><creator>LOFFLER, B.-M</creator><creator>LOHRER, W</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><general>Dekker</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>OTOTI</scope></search><sort><creationdate>1991</creationdate><title>Different Endothelin Receptor Affinities in Dog Tissues</title><author>LOFFLER, B.-M ; LOHRER, W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c489t-9ae9a98b25d66ec0b81b73be0206454fd3f566112b76679b6a0beb20ff14663b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>AFFINITY</topic><topic>ANIMAL TISSUES</topic><topic>ANIMALS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BIOCHEMICAL REACTION KINETICS</topic><topic>Biological and medical sciences</topic><topic>BODY</topic><topic>CELL CONSTITUENTS</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>CENTRIFUGATION</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DOGS</topic><topic>ELECTRON CAPTURE RADIOISOTOPES</topic><topic>Endothelins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>INTERMEDIATE MASS NUCLEI</topic><topic>INTERNAL CONVERSION RADIOISOTOPES</topic><topic>IODINE 125</topic><topic>IODINE ISOTOPES</topic><topic>Iodine Radioisotopes</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>KINETICS</topic><topic>MAMMALS</topic><topic>MEMBRANE PROTEINS</topic><topic>MICROSOMES</topic><topic>Molecular and cellular biology</topic><topic>NUCLEI</topic><topic>ODD-EVEN NUCLEI</topic><topic>Organ Specificity</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANS</topic><topic>PEPTIDES</topic><topic>PROTEINS</topic><topic>RADIOISOTOPES</topic><topic>REACTION KINETICS</topic><topic>RECEPTORS</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Endothelin</topic><topic>RIBOSOMES</topic><topic>SEPARATION PROCESSES</topic><topic>SPECIFICITY</topic><topic>TISSUES</topic><topic>TRACER TECHNIQUES</topic><topic>ULTRACENTRIFUGATION</topic><topic>VERTEBRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LOFFLER, B.-M</creatorcontrib><creatorcontrib>LOHRER, W</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>OSTI.GOV</collection><jtitle>Journal of receptor research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LOFFLER, B.-M</au><au>LOHRER, W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Different Endothelin Receptor Affinities in Dog Tissues</atitle><jtitle>Journal of receptor research</jtitle><addtitle>J Recept Res</addtitle><date>1991</date><risdate>1991</risdate><volume>11</volume><issue>1-4</issue><spage>293</spage><epage>298</epage><pages>293-298</pages><issn>1079-9893</issn><issn>0197-5110</issn><eissn>1532-4281</eissn><coden>JRERDM</coden><abstract>Abstract
Endothelin (ET) is a long-lasting potent vasoconstrictor-peptide. Here we report different binding affinities of endothelin-1 (ET-1) to ET-receptors of various dog tissues. Crude microsomal fractions were prepared after homogenisation of dog tissues in 50 mM Tris/HCl, 20 mM MnCl2, 1 mM EDTA, pH 7.4 by differential centrifugation. Aliquots of microsomal fractions (70 u.g of protein) were incubated at 25°C for 180 min in the presence of 20 pM125I-ET-1 and various concentrations of cold ET-1. Four different ET-1 receptor binding affinities were found: adrenals, cerebrum, liver, heart, skeletal muscle and stomach microsomal membranes contained high affinity binding sites (Kd 50 - 80 pM, Bmax 60 - 250 fmol/mg). In cerebellum and spleen medium affinity ET-1 receptors (Kd 350 pM, Bmax 880 and 1200 fmol/mg respectively) were present. In comparison lung and kidney microsomes contained a low affinity ET-1 receptor (Kd 800 and 880 pM, Bmax 1600 and 350 fmol/mg). Receptors of even lower affinity were present in heart, intestine and liver microsomes with Kd values of 3 - 6 nM.</abstract><cop>Basel</cop><cop>Hong Kong</cop><cop>New York, NY</cop><pub>Informa UK Ltd</pub><pmid>1653335</pmid><doi>10.3109/10799899109066408</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1079-9893 |
| ispartof | Journal of receptor research, 1991, Vol.11 (1-4), p.293-298 |
| issn | 1079-9893 0197-5110 1532-4281 |
| language | eng |
| recordid | cdi_pubmed_primary_1653335 |
| source | MEDLINE; Taylor & Francis; Taylor & Francis Medical Library - CRKN |
| subjects | 550201 - Biochemistry- Tracer Techniques AFFINITY ANIMAL TISSUES ANIMALS BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BIOCHEMICAL REACTION KINETICS Biological and medical sciences BODY CELL CONSTITUENTS Cell receptors Cell structures and functions CENTRIFUGATION DAYS LIVING RADIOISOTOPES DOGS ELECTRON CAPTURE RADIOISOTOPES Endothelins - metabolism Fundamental and applied biological sciences. Psychology Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors INTERMEDIATE MASS NUCLEI INTERNAL CONVERSION RADIOISOTOPES IODINE 125 IODINE ISOTOPES Iodine Radioisotopes ISOTOPE APPLICATIONS ISOTOPES KINETICS MAMMALS MEMBRANE PROTEINS MICROSOMES Molecular and cellular biology NUCLEI ODD-EVEN NUCLEI Organ Specificity ORGANIC COMPOUNDS ORGANS PEPTIDES PROTEINS RADIOISOTOPES REACTION KINETICS RECEPTORS Receptors, Cell Surface - metabolism Receptors, Endothelin RIBOSOMES SEPARATION PROCESSES SPECIFICITY TISSUES TRACER TECHNIQUES ULTRACENTRIFUGATION VERTEBRATES |
| title | Different Endothelin Receptor Affinities in Dog Tissues |
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