Characteristics of the rat prostate androgen receptors analyzed by sucrose density gradient and high-performance liquid chromatofocusing
Rat prostate cytosolic androgen-receptor complexes were analyzed by sucrose density gradient (SDG) centrifugation and by high-performance liquid chromatofocusing (HPCF). Without protecting agents, these complexes were resolved by HPCF at basic (8.25–7.1), intermediary (7.0–5.0) and acidic (4.6–4.2)...
Gespeichert in:
Veröffentlicht in: | Journal of steroid biochemistry 1989-11, Vol.33 (5), p.993-1000 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1000 |
---|---|
container_issue | 5 |
container_start_page | 993 |
container_title | Journal of steroid biochemistry |
container_volume | 33 |
creator | Bouthillier, François Carmel, Michel Elhilali, Mostafa Radwan, Farouk Lehoux, Jean-Guy |
description | Rat prostate cytosolic androgen-receptor complexes were analyzed by sucrose density gradient (SDG) centrifugation and by high-performance liquid chromatofocusing (HPCF). Without protecting agents, these complexes were resolved by HPCF at basic (8.25–7.1), intermediary (7.0–5.0) and acidic (4.6–4.2) pH. Sodium molybdate stabilized labeled complexes which migrated in the 8–9S and 3.5–6S areas on SDG. These were further stabilized by the presence of sodium molybdate and four protease inhibitors: complexes then sedimented mainly in the 8–9S area with a shoulder at 6–7S. Forms eluting at acidic pH on HPCF were favored by the presence of sodium molybdate and further enhanced by the addition of inhibitors, to the detriment of basic ones. Furthermore, when chromatographed on phosphocellulose (P-c), unretained complexes sedimented as a symmetrical peak on SDG centrifugation in the 8–9S area, but were eluted from HPCF columns as two entities at pH 4.1 and 4.6. The P-c retained complexes subsequently detached by 0.6 M KC1, were resolved into three entities by HPCF with a major component at pH 8.2, which sedimented in the 4S areas. These results demonstrate that the gradual decrease in the negative net charge of androgen receptor correlates with the gradual reduction in mass of the androgen-receptor complex. Moreover, this can be interpreted as further evidence for a heterogeneity of androgen receptor population in rat prostate, suggesting the involvement of a multistep mechanism preceding the induction of specific gene transcription by the hormone. |
doi_str_mv | 10.1016/0022-4731(89)90251-3 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79399259</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0022473189902513</els_id><sourcerecordid>79399259</sourcerecordid><originalsourceid>FETCH-LOGICAL-c418t-322568ccc6b26de00cd3408c3f9e8034ed0467261484db7ce826a40154fc8bbc3</originalsourceid><addsrcrecordid>eNqFkc2O1DAQhH0ALcvCG4DkCwgOAf8lcS5IqxELSCtxgbPltDsToySetZ2VhifgsXGY0XKDk6XuqlK7PkJecPaOM968Z0yISrWSv9Hd246JmlfyEbl8GD8hT1P6wRjvtBIX5EI0jEulLsmv3WijhYzRp-wh0TDQPCKNNtNDDCnbjNQuLoY9LjQi4CGHmMrITsef6Gh_pGmFokTqcEk-H-k-WudxyZuPjn4_VgeMQ4izXQDp5O9W7yiMMcw2hyHAmvyyf0YeD3ZK-Pz8XpHvNx-_7T5Xt18_fdld31aguM6VFKJuNAA0vWgcMgZOKqZBDh1qJhU6pppWNFxp5foWUIvGKsZrNYDue5BX5PUpt_zubsWUzewT4DTZBcOaTNvJrhN1918hr1tRamyKUJ2EWwsp4mAO0c82Hg1nZqNjNgxmw2B0Z_7QMbLYXp7z135G92A6oyn7V-e9TWCnIZb2fPqbXe5UgvOi-3DSYWnt3mM0CUr7gM4XXNm44P99yG8T6rBj</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15722606</pqid></control><display><type>article</type><title>Characteristics of the rat prostate androgen receptors analyzed by sucrose density gradient and high-performance liquid chromatofocusing</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Bouthillier, François ; Carmel, Michel ; Elhilali, Mostafa ; Radwan, Farouk ; Lehoux, Jean-Guy</creator><creatorcontrib>Bouthillier, François ; Carmel, Michel ; Elhilali, Mostafa ; Radwan, Farouk ; Lehoux, Jean-Guy</creatorcontrib><description>Rat prostate cytosolic androgen-receptor complexes were analyzed by sucrose density gradient (SDG) centrifugation and by high-performance liquid chromatofocusing (HPCF). Without protecting agents, these complexes were resolved by HPCF at basic (8.25–7.1), intermediary (7.0–5.0) and acidic (4.6–4.2) pH. Sodium molybdate stabilized labeled complexes which migrated in the 8–9S and 3.5–6S areas on SDG. These were further stabilized by the presence of sodium molybdate and four protease inhibitors: complexes then sedimented mainly in the 8–9S area with a shoulder at 6–7S. Forms eluting at acidic pH on HPCF were favored by the presence of sodium molybdate and further enhanced by the addition of inhibitors, to the detriment of basic ones. Furthermore, when chromatographed on phosphocellulose (P-c), unretained complexes sedimented as a symmetrical peak on SDG centrifugation in the 8–9S area, but were eluted from HPCF columns as two entities at pH 4.1 and 4.6. The P-c retained complexes subsequently detached by 0.6 M KC1, were resolved into three entities by HPCF with a major component at pH 8.2, which sedimented in the 4S areas. These results demonstrate that the gradual decrease in the negative net charge of androgen receptor correlates with the gradual reduction in mass of the androgen-receptor complex. Moreover, this can be interpreted as further evidence for a heterogeneity of androgen receptor population in rat prostate, suggesting the involvement of a multistep mechanism preceding the induction of specific gene transcription by the hormone.</description><identifier>ISSN: 0022-4731</identifier><identifier>DOI: 10.1016/0022-4731(89)90251-3</identifier><identifier>PMID: 2601344</identifier><identifier>CODEN: JSTBBK</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>Animals ; Biological and medical sciences ; Centrifugation, Density Gradient ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Cytosol - analysis ; Fundamental and applied biological sciences. Psychology ; Hormone metabolism and regulation ; Isoelectric Point ; Male ; Mammalian male genital system ; Molybdenum - pharmacology ; Prostate - analysis ; Protease Inhibitors - pharmacology ; Rats ; Receptors, Androgen - analysis ; Vertebrates: reproduction</subject><ispartof>Journal of steroid biochemistry, 1989-11, Vol.33 (5), p.993-1000</ispartof><rights>1989</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-322568ccc6b26de00cd3408c3f9e8034ed0467261484db7ce826a40154fc8bbc3</citedby><cites>FETCH-LOGICAL-c418t-322568ccc6b26de00cd3408c3f9e8034ed0467261484db7ce826a40154fc8bbc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19394211$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2601344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bouthillier, François</creatorcontrib><creatorcontrib>Carmel, Michel</creatorcontrib><creatorcontrib>Elhilali, Mostafa</creatorcontrib><creatorcontrib>Radwan, Farouk</creatorcontrib><creatorcontrib>Lehoux, Jean-Guy</creatorcontrib><title>Characteristics of the rat prostate androgen receptors analyzed by sucrose density gradient and high-performance liquid chromatofocusing</title><title>Journal of steroid biochemistry</title><addtitle>J Steroid Biochem</addtitle><description>Rat prostate cytosolic androgen-receptor complexes were analyzed by sucrose density gradient (SDG) centrifugation and by high-performance liquid chromatofocusing (HPCF). Without protecting agents, these complexes were resolved by HPCF at basic (8.25–7.1), intermediary (7.0–5.0) and acidic (4.6–4.2) pH. Sodium molybdate stabilized labeled complexes which migrated in the 8–9S and 3.5–6S areas on SDG. These were further stabilized by the presence of sodium molybdate and four protease inhibitors: complexes then sedimented mainly in the 8–9S area with a shoulder at 6–7S. Forms eluting at acidic pH on HPCF were favored by the presence of sodium molybdate and further enhanced by the addition of inhibitors, to the detriment of basic ones. Furthermore, when chromatographed on phosphocellulose (P-c), unretained complexes sedimented as a symmetrical peak on SDG centrifugation in the 8–9S area, but were eluted from HPCF columns as two entities at pH 4.1 and 4.6. The P-c retained complexes subsequently detached by 0.6 M KC1, were resolved into three entities by HPCF with a major component at pH 8.2, which sedimented in the 4S areas. These results demonstrate that the gradual decrease in the negative net charge of androgen receptor correlates with the gradual reduction in mass of the androgen-receptor complex. Moreover, this can be interpreted as further evidence for a heterogeneity of androgen receptor population in rat prostate, suggesting the involvement of a multistep mechanism preceding the induction of specific gene transcription by the hormone.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Cytosol - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone metabolism and regulation</subject><subject>Isoelectric Point</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Molybdenum - pharmacology</subject><subject>Prostate - analysis</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Rats</subject><subject>Receptors, Androgen - analysis</subject><subject>Vertebrates: reproduction</subject><issn>0022-4731</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2O1DAQhH0ALcvCG4DkCwgOAf8lcS5IqxELSCtxgbPltDsToySetZ2VhifgsXGY0XKDk6XuqlK7PkJecPaOM968Z0yISrWSv9Hd246JmlfyEbl8GD8hT1P6wRjvtBIX5EI0jEulLsmv3WijhYzRp-wh0TDQPCKNNtNDDCnbjNQuLoY9LjQi4CGHmMrITsef6Gh_pGmFokTqcEk-H-k-WudxyZuPjn4_VgeMQ4izXQDp5O9W7yiMMcw2hyHAmvyyf0YeD3ZK-Pz8XpHvNx-_7T5Xt18_fdld31aguM6VFKJuNAA0vWgcMgZOKqZBDh1qJhU6pppWNFxp5foWUIvGKsZrNYDue5BX5PUpt_zubsWUzewT4DTZBcOaTNvJrhN1918hr1tRamyKUJ2EWwsp4mAO0c82Hg1nZqNjNgxmw2B0Z_7QMbLYXp7z135G92A6oyn7V-e9TWCnIZb2fPqbXe5UgvOi-3DSYWnt3mM0CUr7gM4XXNm44P99yG8T6rBj</recordid><startdate>19891101</startdate><enddate>19891101</enddate><creator>Bouthillier, François</creator><creator>Carmel, Michel</creator><creator>Elhilali, Mostafa</creator><creator>Radwan, Farouk</creator><creator>Lehoux, Jean-Guy</creator><general>Elsevier B.V</general><general>Pergamon</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19891101</creationdate><title>Characteristics of the rat prostate androgen receptors analyzed by sucrose density gradient and high-performance liquid chromatofocusing</title><author>Bouthillier, François ; Carmel, Michel ; Elhilali, Mostafa ; Radwan, Farouk ; Lehoux, Jean-Guy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-322568ccc6b26de00cd3408c3f9e8034ed0467261484db7ce826a40154fc8bbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Cytosol - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone metabolism and regulation</topic><topic>Isoelectric Point</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Molybdenum - pharmacology</topic><topic>Prostate - analysis</topic><topic>Protease Inhibitors - pharmacology</topic><topic>Rats</topic><topic>Receptors, Androgen - analysis</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bouthillier, François</creatorcontrib><creatorcontrib>Carmel, Michel</creatorcontrib><creatorcontrib>Elhilali, Mostafa</creatorcontrib><creatorcontrib>Radwan, Farouk</creatorcontrib><creatorcontrib>Lehoux, Jean-Guy</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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of steroid biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bouthillier, François</au><au>Carmel, Michel</au><au>Elhilali, Mostafa</au><au>Radwan, Farouk</au><au>Lehoux, Jean-Guy</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characteristics of the rat prostate androgen receptors analyzed by sucrose density gradient and high-performance liquid chromatofocusing</atitle><jtitle>Journal of steroid biochemistry</jtitle><addtitle>J Steroid Biochem</addtitle><date>1989-11-01</date><risdate>1989</risdate><volume>33</volume><issue>5</issue><spage>993</spage><epage>1000</epage><pages>993-1000</pages><issn>0022-4731</issn><coden>JSTBBK</coden><abstract>Rat prostate cytosolic androgen-receptor complexes were analyzed by sucrose density gradient (SDG) centrifugation and by high-performance liquid chromatofocusing (HPCF). Without protecting agents, these complexes were resolved by HPCF at basic (8.25–7.1), intermediary (7.0–5.0) and acidic (4.6–4.2) pH. Sodium molybdate stabilized labeled complexes which migrated in the 8–9S and 3.5–6S areas on SDG. These were further stabilized by the presence of sodium molybdate and four protease inhibitors: complexes then sedimented mainly in the 8–9S area with a shoulder at 6–7S. Forms eluting at acidic pH on HPCF were favored by the presence of sodium molybdate and further enhanced by the addition of inhibitors, to the detriment of basic ones. Furthermore, when chromatographed on phosphocellulose (P-c), unretained complexes sedimented as a symmetrical peak on SDG centrifugation in the 8–9S area, but were eluted from HPCF columns as two entities at pH 4.1 and 4.6. The P-c retained complexes subsequently detached by 0.6 M KC1, were resolved into three entities by HPCF with a major component at pH 8.2, which sedimented in the 4S areas. These results demonstrate that the gradual decrease in the negative net charge of androgen receptor correlates with the gradual reduction in mass of the androgen-receptor complex. Moreover, this can be interpreted as further evidence for a heterogeneity of androgen receptor population in rat prostate, suggesting the involvement of a multistep mechanism preceding the induction of specific gene transcription by the hormone.</abstract><cop>Oxford</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>2601344</pmid><doi>10.1016/0022-4731(89)90251-3</doi><tpages>8</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0022-4731 |
ispartof | Journal of steroid biochemistry, 1989-11, Vol.33 (5), p.993-1000 |
issn | 0022-4731 |
language | eng |
recordid | cdi_proquest_miscellaneous_79399259 |
source | MEDLINE; Alma/SFX Local Collection |
subjects | Animals Biological and medical sciences Centrifugation, Density Gradient Chromatography, High Pressure Liquid Chromatography, Ion Exchange Cytosol - analysis Fundamental and applied biological sciences. Psychology Hormone metabolism and regulation Isoelectric Point Male Mammalian male genital system Molybdenum - pharmacology Prostate - analysis Protease Inhibitors - pharmacology Rats Receptors, Androgen - analysis Vertebrates: reproduction |
title | Characteristics of the rat prostate androgen receptors analyzed by sucrose density gradient and high-performance liquid chromatofocusing |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T14%3A24%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characteristics%20of%20the%20rat%20prostate%20androgen%20receptors%20analyzed%20by%20sucrose%20density%20gradient%20and%20high-performance%20liquid%20chromatofocusing&rft.jtitle=Journal%20of%20steroid%20biochemistry&rft.au=Bouthillier,%20Fran%C3%A7ois&rft.date=1989-11-01&rft.volume=33&rft.issue=5&rft.spage=993&rft.epage=1000&rft.pages=993-1000&rft.issn=0022-4731&rft.coden=JSTBBK&rft_id=info:doi/10.1016/0022-4731(89)90251-3&rft_dat=%3Cproquest_cross%3E79399259%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15722606&rft_id=info:pmid/2601344&rft_els_id=0022473189902513&rfr_iscdi=true |