Renal Aldosterone Receptors: Studies with [3H]Aldosterone and the Anti-Mineralocorticoid [3H]Spirolactone (SC-26304)
In vivo, a spirolactone (SC-26304) inhibited the effects of aldosterone on urinary K+:Na+ratios and the binding of [3H]aldosterone to renal cytoplasmic and nuclear receptors. Cytoplasmic binding of [3H]aldosterone and [3H]spirolactone (SC-26304) was similar in magnitude and involved the same set of...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1974-04, Vol.71 (4), p.1431-1435 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Marver, Diana Stewart, John Funder, John W. Feldman, David Edelman, Isidore S. |
| description | In vivo, a spirolactone (SC-26304) inhibited the effects of aldosterone on urinary K+:Na+ratios and the binding of [3H]aldosterone to renal cytoplasmic and nuclear receptors. Cytoplasmic binding of [3H]aldosterone and [3H]spirolactone (SC-26304) was similar in magnitude and involved the same set of sites. Under three sets of conditions--(i) in the intact rat, (ii) in kidney slices, and (iii) in reconstitution studies (mixing prelabeled cytoplasm with either purified renal nuclei or chromatin), [3H]spirolactone (SC-26304) did not yield specific nuclear complexes in contrast to the reproducible generation of these complexes with [3H]aldosterone. In glycerol density gradients, cytoplasmic [3H]aldosterone receptor complexes sedimented at 8.5 S and 4 S in low concentrations of salt and at 4.5 S in high concentrations of salt. Cytoplasmic [3H]spirolactone (SC-26304) receptor complexes sedimented at 3 S in low concentrations of salt and 4 S in high concentrations of salt. These results are discussed in terms of an allosteric model of the receptor system. |
| doi_str_mv | 10.1073/pnas.71.4.1431 |
| format | Article |
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Cytoplasmic binding of [3H]aldosterone and [3H]spirolactone (SC-26304) was similar in magnitude and involved the same set of sites. Under three sets of conditions--(i) in the intact rat, (ii) in kidney slices, and (iii) in reconstitution studies (mixing prelabeled cytoplasm with either purified renal nuclei or chromatin), [3H]spirolactone (SC-26304) did not yield specific nuclear complexes in contrast to the reproducible generation of these complexes with [3H]aldosterone. In glycerol density gradients, cytoplasmic [3H]aldosterone receptor complexes sedimented at 8.5 S and 4 S in low concentrations of salt and at 4.5 S in high concentrations of salt. Cytoplasmic [3H]spirolactone (SC-26304) receptor complexes sedimented at 3 S in low concentrations of salt and 4 S in high concentrations of salt. These results are discussed in terms of an allosteric model of the receptor system.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.71.4.1431</identifier><identifier>PMID: 4364539</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adrenalectomy ; Aldosterone - metabolism ; Animals ; Binding Sites - drug effects ; Binding, Competitive ; Biological Sciences: Medical Sciences ; Body weight ; Cell Fractionation ; Cell Nucleus - metabolism ; Centrifugation ; Centrifugation, Density Gradient ; Chromatin ; Cytoplasm ; Cytoplasm - metabolism ; Homogenization ; In Vitro Techniques ; Kidney - cytology ; Kidney - drug effects ; Kidney - metabolism ; Kidney Function Tests ; Kidneys ; Lactones - pharmacology ; Low concentrations ; Mineralocorticoid Receptor Antagonists ; Protein Binding ; Rats ; Receptors ; Receptors, Cell Surface - drug effects ; Salts ; Spiro Compounds - pharmacology ; Steroids ; Tritium</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1974-04, Vol.71 (4), p.1431-1435</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-6bce327fcc67b34d4161486f3dac4b07b72f42f3f8705d3ad4f4a23f85d41ca93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/71/4.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/63343$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/63343$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27923,27924,53790,53792,58016,58249</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4364539$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marver, Diana</creatorcontrib><creatorcontrib>Stewart, John</creatorcontrib><creatorcontrib>Funder, John W.</creatorcontrib><creatorcontrib>Feldman, David</creatorcontrib><creatorcontrib>Edelman, Isidore S.</creatorcontrib><title>Renal Aldosterone Receptors: Studies with [3H]Aldosterone and the Anti-Mineralocorticoid [3H]Spirolactone (SC-26304)</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>In vivo, a spirolactone (SC-26304) inhibited the effects of aldosterone on urinary K+:Na+ratios and the binding of [3H]aldosterone to renal cytoplasmic and nuclear receptors. Cytoplasmic binding of [3H]aldosterone and [3H]spirolactone (SC-26304) was similar in magnitude and involved the same set of sites. Under three sets of conditions--(i) in the intact rat, (ii) in kidney slices, and (iii) in reconstitution studies (mixing prelabeled cytoplasm with either purified renal nuclei or chromatin), [3H]spirolactone (SC-26304) did not yield specific nuclear complexes in contrast to the reproducible generation of these complexes with [3H]aldosterone. In glycerol density gradients, cytoplasmic [3H]aldosterone receptor complexes sedimented at 8.5 S and 4 S in low concentrations of salt and at 4.5 S in high concentrations of salt. Cytoplasmic [3H]spirolactone (SC-26304) receptor complexes sedimented at 3 S in low concentrations of salt and 4 S in high concentrations of salt. These results are discussed in terms of an allosteric model of the receptor system.</description><subject>Adrenalectomy</subject><subject>Aldosterone - metabolism</subject><subject>Animals</subject><subject>Binding Sites - drug effects</subject><subject>Binding, Competitive</subject><subject>Biological Sciences: Medical Sciences</subject><subject>Body weight</subject><subject>Cell Fractionation</subject><subject>Cell Nucleus - metabolism</subject><subject>Centrifugation</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromatin</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>Homogenization</subject><subject>In Vitro Techniques</subject><subject>Kidney - cytology</subject><subject>Kidney - drug effects</subject><subject>Kidney - metabolism</subject><subject>Kidney Function Tests</subject><subject>Kidneys</subject><subject>Lactones - pharmacology</subject><subject>Low concentrations</subject><subject>Mineralocorticoid Receptor Antagonists</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Receptors</subject><subject>Receptors, Cell Surface - drug effects</subject><subject>Salts</subject><subject>Spiro Compounds - pharmacology</subject><subject>Steroids</subject><subject>Tritium</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkd1rFDEUxYNY6rb66oMgzJPUhxnzNclMwYdlsVaoCF19EgmZfLgps8mYZPz47zvTXZcVfArh_M4993IAeI5ghSAnbwYvU8VRRStECXoEFgi2qGS0hY_BAkLMy4Zi-gScpXQHIWzrBp6CU0oYrUm7APnWeNkXy16HlE0M3hS3Rpkhh5gui3UetTOp-OXypvhKrr8dc9LrIm9MsfTZlR-dN1H2QYWYnQpOP-DrwcXQS5Vn_mK9KjEjkL5-Ck6s7JN5tn_PwZerd59X1-XNp_cfVsubUtGa5ZJ1yhDMrVKMd4RqihiiDbNES0U7yDuOLcWW2IbDWhOpqaUST996QpVsyTl4u5s7jN3WaGV8nnYUQ3RbGf-IIJ34V_FuI76Hn4I0DaZk8r_a-2P4MZqUxdYlZfpeehPGJBpMGG_wHFTtQBVDStHYQwaCYq5JzDUJjgQVc02T4eXxZgd838tR8uz7qx78wo59n83vfDTov-Ckv9jpd2mq9AAwQqb77gGbvrBO</recordid><startdate>19740401</startdate><enddate>19740401</enddate><creator>Marver, Diana</creator><creator>Stewart, John</creator><creator>Funder, John W.</creator><creator>Feldman, David</creator><creator>Edelman, Isidore S.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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><scope>5PM</scope></search><sort><creationdate>19740401</creationdate><title>Renal Aldosterone Receptors: Studies with [3H]Aldosterone and the Anti-Mineralocorticoid [3H]Spirolactone (SC-26304)</title><author>Marver, Diana ; Stewart, John ; Funder, John W. ; Feldman, David ; Edelman, Isidore S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-6bce327fcc67b34d4161486f3dac4b07b72f42f3f8705d3ad4f4a23f85d41ca93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Adrenalectomy</topic><topic>Aldosterone - metabolism</topic><topic>Animals</topic><topic>Binding Sites - drug effects</topic><topic>Binding, Competitive</topic><topic>Biological Sciences: Medical Sciences</topic><topic>Body weight</topic><topic>Cell Fractionation</topic><topic>Cell Nucleus - metabolism</topic><topic>Centrifugation</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromatin</topic><topic>Cytoplasm</topic><topic>Cytoplasm - metabolism</topic><topic>Homogenization</topic><topic>In Vitro Techniques</topic><topic>Kidney - cytology</topic><topic>Kidney - drug effects</topic><topic>Kidney - metabolism</topic><topic>Kidney Function Tests</topic><topic>Kidneys</topic><topic>Lactones - pharmacology</topic><topic>Low concentrations</topic><topic>Mineralocorticoid Receptor Antagonists</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Receptors</topic><topic>Receptors, Cell Surface - drug effects</topic><topic>Salts</topic><topic>Spiro Compounds - pharmacology</topic><topic>Steroids</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marver, Diana</creatorcontrib><creatorcontrib>Stewart, John</creatorcontrib><creatorcontrib>Funder, John W.</creatorcontrib><creatorcontrib>Feldman, David</creatorcontrib><creatorcontrib>Edelman, Isidore S.</creatorcontrib><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><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>Marver, Diana</au><au>Stewart, John</au><au>Funder, John W.</au><au>Feldman, David</au><au>Edelman, Isidore S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Renal Aldosterone Receptors: Studies with [3H]Aldosterone and the Anti-Mineralocorticoid [3H]Spirolactone (SC-26304)</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1974-04-01</date><risdate>1974</risdate><volume>71</volume><issue>4</issue><spage>1431</spage><epage>1435</epage><pages>1431-1435</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>In vivo, a spirolactone (SC-26304) inhibited the effects of aldosterone on urinary K+:Na+ratios and the binding of [3H]aldosterone to renal cytoplasmic and nuclear receptors. Cytoplasmic binding of [3H]aldosterone and [3H]spirolactone (SC-26304) was similar in magnitude and involved the same set of sites. Under three sets of conditions--(i) in the intact rat, (ii) in kidney slices, and (iii) in reconstitution studies (mixing prelabeled cytoplasm with either purified renal nuclei or chromatin), [3H]spirolactone (SC-26304) did not yield specific nuclear complexes in contrast to the reproducible generation of these complexes with [3H]aldosterone. In glycerol density gradients, cytoplasmic [3H]aldosterone receptor complexes sedimented at 8.5 S and 4 S in low concentrations of salt and at 4.5 S in high concentrations of salt. Cytoplasmic [3H]spirolactone (SC-26304) receptor complexes sedimented at 3 S in low concentrations of salt and 4 S in high concentrations of salt. 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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adrenalectomy Aldosterone - metabolism Animals Binding Sites - drug effects Binding, Competitive Biological Sciences: Medical Sciences Body weight Cell Fractionation Cell Nucleus - metabolism Centrifugation Centrifugation, Density Gradient Chromatin Cytoplasm Cytoplasm - metabolism Homogenization In Vitro Techniques Kidney - cytology Kidney - drug effects Kidney - metabolism Kidney Function Tests Kidneys Lactones - pharmacology Low concentrations Mineralocorticoid Receptor Antagonists Protein Binding Rats Receptors Receptors, Cell Surface - drug effects Salts Spiro Compounds - pharmacology Steroids Tritium |
| title | Renal Aldosterone Receptors: Studies with [3H]Aldosterone and the Anti-Mineralocorticoid [3H]Spirolactone (SC-26304) |
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