Evidence for an androgen binding protein in the testis of a teleost fish ( Salmo gairdneri R.): A potential marker of sertoli cell function
A factor binding tritiated testosterone was detected using “steady-state” polyacrylamide-gel electrophoresis, in rainbow trout genital tract. It migrated with a R f identical to that of rat ABP. This binding was thermolabile, and was competitively inhibited by unlabelled testosterone. The steroid bi...
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Veröffentlicht in: | Journal of steroid biochemistry 1989-04, Vol.32 (4), p.545-552 |
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description | A factor binding tritiated testosterone was detected using “steady-state” polyacrylamide-gel electrophoresis, in rainbow trout genital tract. It migrated with a
R
f
identical to that of rat ABP. This binding was thermolabile, and was competitively inhibited by unlabelled testosterone. The steroid binding protein was found in cytosols from trout testes which had been previously perfused to avoid blood contamination, trout seminal plasma and in testicular explants incubation media. Using a quantitative assay and a Scatchard analysis, 25–50 pmol binding sites per gram gonad were found in testis cytosol. Binding affinity constant for testosterone in the various samples was close to 4 × 10
8 M
−1. The dissociation of steroid-protein complex was rapid (
t
1
2
≈ 1.5 min). Hormonal specificity was studied by the competition of
3H-T binding with several concentrations of unlabelled competitors and the following order for affinities was obtained: dihydrotestosterone ≈ androstenedione > testosterone > oestradiol > 17α, 20β DHP > 11KT > cyproterone acetate > cortisol.
High testicular cytosol and seminal plasma concentrations and apparent
in vitro production indicate that the testis may synthesize an ABP-like protein in the trout. Such a factor would provide a unique marker of Sertoli cell activity and regulation in various physiological or experimental situations. |
doi_str_mv | 10.1016/0022-4731(89)90388-9 |
format | Article |
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R
f
identical to that of rat ABP. This binding was thermolabile, and was competitively inhibited by unlabelled testosterone. The steroid binding protein was found in cytosols from trout testes which had been previously perfused to avoid blood contamination, trout seminal plasma and in testicular explants incubation media. Using a quantitative assay and a Scatchard analysis, 25–50 pmol binding sites per gram gonad were found in testis cytosol. Binding affinity constant for testosterone in the various samples was close to 4 × 10
8 M
−1. The dissociation of steroid-protein complex was rapid (
t
1
2
≈ 1.5 min). Hormonal specificity was studied by the competition of
3H-T binding with several concentrations of unlabelled competitors and the following order for affinities was obtained: dihydrotestosterone ≈ androstenedione > testosterone > oestradiol > 17α, 20β DHP > 11KT > cyproterone acetate > cortisol.
High testicular cytosol and seminal plasma concentrations and apparent
in vitro production indicate that the testis may synthesize an ABP-like protein in the trout. Such a factor would provide a unique marker of Sertoli cell activity and regulation in various physiological or experimental situations.</description><identifier>ISSN: 0022-4731</identifier><identifier>DOI: 10.1016/0022-4731(89)90388-9</identifier><identifier>PMID: 2724958</identifier><identifier>CODEN: JSTBBK</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>Androgen-Binding Protein - isolation & purification ; Androgen-Binding Protein - metabolism ; Animals ; Binding, Competitive ; Biological and medical sciences ; Cytosol - metabolism ; Freshwater ; Fundamental and applied biological sciences. Psychology ; Hormone metabolism and regulation ; Kinetics ; Male ; Mammalian male genital system ; Organ Culture Techniques ; Sertoli Cells - cytology ; Sexual Maturation ; Statistics ; Statistics Theory ; Testis - metabolism ; Trout ; Vertebrates: reproduction</subject><ispartof>Journal of steroid biochemistry, 1989-04, Vol.32 (4), p.545-552</ispartof><rights>1989</rights><rights>1991 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c498t-d4d9167cc69d010973f4aef63105ffd462c044dc1e74d719020552257dd8557c3</citedby><cites>FETCH-LOGICAL-c498t-d4d9167cc69d010973f4aef63105ffd462c044dc1e74d719020552257dd8557c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19329615$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2724958$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02728270$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Foucher, Jean-Luc</creatorcontrib><creatorcontrib>Le Gac, Florence</creatorcontrib><title>Evidence for an androgen binding protein in the testis of a teleost fish ( Salmo gairdneri R.): A potential marker of sertoli cell function</title><title>Journal of steroid biochemistry</title><addtitle>J Steroid Biochem</addtitle><description>A factor binding tritiated testosterone was detected using “steady-state” polyacrylamide-gel electrophoresis, in rainbow trout genital tract. It migrated with a
R
f
identical to that of rat ABP. This binding was thermolabile, and was competitively inhibited by unlabelled testosterone. The steroid binding protein was found in cytosols from trout testes which had been previously perfused to avoid blood contamination, trout seminal plasma and in testicular explants incubation media. Using a quantitative assay and a Scatchard analysis, 25–50 pmol binding sites per gram gonad were found in testis cytosol. Binding affinity constant for testosterone in the various samples was close to 4 × 10
8 M
−1. The dissociation of steroid-protein complex was rapid (
t
1
2
≈ 1.5 min). Hormonal specificity was studied by the competition of
3H-T binding with several concentrations of unlabelled competitors and the following order for affinities was obtained: dihydrotestosterone ≈ androstenedione > testosterone > oestradiol > 17α, 20β DHP > 11KT > cyproterone acetate > cortisol.
High testicular cytosol and seminal plasma concentrations and apparent
in vitro production indicate that the testis may synthesize an ABP-like protein in the trout. Such a factor would provide a unique marker of Sertoli cell activity and regulation in various physiological or experimental situations.</description><subject>Androgen-Binding Protein - isolation & purification</subject><subject>Androgen-Binding Protein - metabolism</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cytosol - metabolism</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone metabolism and regulation</subject><subject>Kinetics</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Organ Culture Techniques</subject><subject>Sertoli Cells - cytology</subject><subject>Sexual Maturation</subject><subject>Statistics</subject><subject>Statistics Theory</subject><subject>Testis - metabolism</subject><subject>Trout</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>eNqFUl2LGyEUnYeW7Xa3_6AFX1o2D7NVxxm1Dwth2S8IFPrxLK5eE9uJpmoC_Q390-tsQvrWwgXl3nMOx3tsmrcEXxJMho8YU9oy3pELIWcSd0K08kVzemy_al7n_ANjIgWjJ80J5ZTJXpw2f2523kIwgFxMSIdaNsUlBPTog_VhiTYpFvAB1SorQAVy8RlFh3S9jxBzQc7nFbpAX_W4jmipfbIBkkdfLmef0BxtKj8Ur0e01uknpImbIZU4emRgHJHbBlN8DOfNS6fHDG8O51nz_fbm2_V9u_h893A9X7SGSVFay6wkAzdmkBYTLHnnmAY3dAT3zlk2UIMZs4YAZ5YTiSnue0p7bq3oe266s2a2113pUW2Sr7Z-q6i9up8v1NTDdT2CcrwjFfthj61r-LWtb1drnyfXOkDcZsWF5FIO_weSaoFSLCqQ7YEmxZwTuKMFgtUUpppSU1NqSkj1HKaSlfbuoL99XIM9kg5J1vn7w1xno0eXdDA-_9WWHa02-4q72uOgbnjnIals_PQBrE9girLR_9vIE50Cu5U</recordid><startdate>19890401</startdate><enddate>19890401</enddate><creator>Foucher, Jean-Luc</creator><creator>Le Gac, Florence</creator><general>Elsevier B.V</general><general>Pergamon</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>7TK</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>H98</scope><scope>L.G</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope></search><sort><creationdate>19890401</creationdate><title>Evidence for an androgen binding protein in the testis of a teleost fish ( Salmo gairdneri R.): A potential marker of sertoli cell function</title><author>Foucher, Jean-Luc ; Le Gac, Florence</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-d4d9167cc69d010973f4aef63105ffd462c044dc1e74d719020552257dd8557c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Androgen-Binding Protein - isolation & purification</topic><topic>Androgen-Binding Protein - metabolism</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cytosol - metabolism</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone metabolism and regulation</topic><topic>Kinetics</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Organ Culture Techniques</topic><topic>Sertoli Cells - cytology</topic><topic>Sexual Maturation</topic><topic>Statistics</topic><topic>Statistics Theory</topic><topic>Testis - metabolism</topic><topic>Trout</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Foucher, Jean-Luc</creatorcontrib><creatorcontrib>Le Gac, Florence</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>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>Journal of steroid biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Foucher, Jean-Luc</au><au>Le Gac, Florence</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for an androgen binding protein in the testis of a teleost fish ( Salmo gairdneri R.): A potential marker of sertoli cell function</atitle><jtitle>Journal of steroid biochemistry</jtitle><addtitle>J Steroid Biochem</addtitle><date>1989-04-01</date><risdate>1989</risdate><volume>32</volume><issue>4</issue><spage>545</spage><epage>552</epage><pages>545-552</pages><issn>0022-4731</issn><coden>JSTBBK</coden><abstract>A factor binding tritiated testosterone was detected using “steady-state” polyacrylamide-gel electrophoresis, in rainbow trout genital tract. It migrated with a
R
f
identical to that of rat ABP. This binding was thermolabile, and was competitively inhibited by unlabelled testosterone. The steroid binding protein was found in cytosols from trout testes which had been previously perfused to avoid blood contamination, trout seminal plasma and in testicular explants incubation media. Using a quantitative assay and a Scatchard analysis, 25–50 pmol binding sites per gram gonad were found in testis cytosol. Binding affinity constant for testosterone in the various samples was close to 4 × 10
8 M
−1. The dissociation of steroid-protein complex was rapid (
t
1
2
≈ 1.5 min). Hormonal specificity was studied by the competition of
3H-T binding with several concentrations of unlabelled competitors and the following order for affinities was obtained: dihydrotestosterone ≈ androstenedione > testosterone > oestradiol > 17α, 20β DHP > 11KT > cyproterone acetate > cortisol.
High testicular cytosol and seminal plasma concentrations and apparent
in vitro production indicate that the testis may synthesize an ABP-like protein in the trout. Such a factor would provide a unique marker of Sertoli cell activity and regulation in various physiological or experimental situations.</abstract><cop>Oxford</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>2724958</pmid><doi>10.1016/0022-4731(89)90388-9</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Androgen-Binding Protein - isolation & purification Androgen-Binding Protein - metabolism Animals Binding, Competitive Biological and medical sciences Cytosol - metabolism Freshwater Fundamental and applied biological sciences. Psychology Hormone metabolism and regulation Kinetics Male Mammalian male genital system Organ Culture Techniques Sertoli Cells - cytology Sexual Maturation Statistics Statistics Theory Testis - metabolism Trout Vertebrates: reproduction |
title | Evidence for an androgen binding protein in the testis of a teleost fish ( Salmo gairdneri R.): A potential marker of sertoli cell function |
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