Prolactin and Testicular Leydig Cell Function: Characterization of Prolactin Receptors in the Murine MA-10 Testicular Leydig Cell Line
Abstract The direct role of prolactin (PRL) in testicular function is still unclear, mostly because of lack of a suitable in vitro model. To establish the suitability of the MA-10 murine tumor Leydig cell line for the study of PRL receptors (PRLR) and effects on steroidogenesis, we initially charact...
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| Veröffentlicht in: | Experimental biology and medicine (Maywood, N.J.) N.J.), 1994-07, Vol.206 (3), p.243-248 |
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| container_title | Experimental biology and medicine (Maywood, N.J.) |
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| creator | Barkey, Ronnie J. Weiss-Messer, Esther Hacham, Haim Herscovich, Sara Ber, Rosalie Amit, Tamar |
| description | Abstract
The direct role of prolactin (PRL) in testicular function is still unclear, mostly because of lack of a suitable in vitro model. To establish the suitability of the MA-10 murine tumor Leydig cell line for the study of PRL receptors (PRLR) and effects on steroidogenesis, we initially characterized PRLR on cultured MA-10 cells. The specific binding (Bs) of [125l]human growth hormone (hGH) depends on time, temperature, and Mg2+ ion and protein concentrations, with absolute specificity for the lactogenic hormones hGH and ovine PRL. Bs is saturable and is to a single class of high-affinity (Ka
= 3.6 × 109
M
-1) low-capacity (B
max = 19.5 fmol/mg protein) binding sites. The molecular weight of PRLR, determined by cross-linking to [125l]hGH, SDS-PAGE and autoradiography, is 35 kDa for the free receptor, suggesting that the short-form PRLR protein, previously described in liver and mammary glands, is that primarily found in MA-10 cells. Thus, the demonstration of specific PRL binding sites on MA-10 Leydig cells, with characteristics similar to primary Leydig cell PRLR, suggests that this cell line can serve as a good model for both the study of PRLR mechanism of action and the role of PRL in Leydig cell function. |
| doi_str_mv | 10.3181/00379727-206-43752 |
| format | Article |
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The direct role of prolactin (PRL) in testicular function is still unclear, mostly because of lack of a suitable in vitro model. To establish the suitability of the MA-10 murine tumor Leydig cell line for the study of PRL receptors (PRLR) and effects on steroidogenesis, we initially characterized PRLR on cultured MA-10 cells. The specific binding (Bs) of [125l]human growth hormone (hGH) depends on time, temperature, and Mg2+ ion and protein concentrations, with absolute specificity for the lactogenic hormones hGH and ovine PRL. Bs is saturable and is to a single class of high-affinity (Ka
= 3.6 × 109
M
-1) low-capacity (B
max = 19.5 fmol/mg protein) binding sites. The molecular weight of PRLR, determined by cross-linking to [125l]hGH, SDS-PAGE and autoradiography, is 35 kDa for the free receptor, suggesting that the short-form PRLR protein, previously described in liver and mammary glands, is that primarily found in MA-10 cells. Thus, the demonstration of specific PRL binding sites on MA-10 Leydig cells, with characteristics similar to primary Leydig cell PRLR, suggests that this cell line can serve as a good model for both the study of PRLR mechanism of action and the role of PRL in Leydig cell function.</description><identifier>ISSN: 0037-9727</identifier><identifier>ISSN: 1535-3702</identifier><identifier>EISSN: 1535-3699</identifier><identifier>DOI: 10.3181/00379727-206-43752</identifier><identifier>PMID: 8016159</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Animals ; Binding Sites ; Growth Hormone - metabolism ; Growth Hormone - pharmacology ; Kinetics ; Leydig Cell Tumor ; Leydig Cells - physiology ; Magnesium - pharmacology ; Male ; Mice ; Molecular Weight ; Prolactin - pharmacology ; Prolactin - physiology ; Receptors, Prolactin - chemistry ; Receptors, Prolactin - physiology ; Tumor Cells, Cultured</subject><ispartof>Experimental biology and medicine (Maywood, N.J.), 1994-07, Vol.206 (3), p.243-248</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c338t-f362173cb151b50aa29c9965bae1a3de2ffe59460bfb01c355a1e5666e27c6db3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8016159$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Barkey, Ronnie J.</creatorcontrib><creatorcontrib>Weiss-Messer, Esther</creatorcontrib><creatorcontrib>Hacham, Haim</creatorcontrib><creatorcontrib>Herscovich, Sara</creatorcontrib><creatorcontrib>Ber, Rosalie</creatorcontrib><creatorcontrib>Amit, Tamar</creatorcontrib><title>Prolactin and Testicular Leydig Cell Function: Characterization of Prolactin Receptors in the Murine MA-10 Testicular Leydig Cell Line</title><title>Experimental biology and medicine (Maywood, N.J.)</title><addtitle>Proc Soc Exp Biol Med</addtitle><description>Abstract
The direct role of prolactin (PRL) in testicular function is still unclear, mostly because of lack of a suitable in vitro model. To establish the suitability of the MA-10 murine tumor Leydig cell line for the study of PRL receptors (PRLR) and effects on steroidogenesis, we initially characterized PRLR on cultured MA-10 cells. The specific binding (Bs) of [125l]human growth hormone (hGH) depends on time, temperature, and Mg2+ ion and protein concentrations, with absolute specificity for the lactogenic hormones hGH and ovine PRL. Bs is saturable and is to a single class of high-affinity (Ka
= 3.6 × 109
M
-1) low-capacity (B
max = 19.5 fmol/mg protein) binding sites. The molecular weight of PRLR, determined by cross-linking to [125l]hGH, SDS-PAGE and autoradiography, is 35 kDa for the free receptor, suggesting that the short-form PRLR protein, previously described in liver and mammary glands, is that primarily found in MA-10 cells. Thus, the demonstration of specific PRL binding sites on MA-10 Leydig cells, with characteristics similar to primary Leydig cell PRLR, suggests that this cell line can serve as a good model for both the study of PRLR mechanism of action and the role of PRL in Leydig cell function.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Growth Hormone - metabolism</subject><subject>Growth Hormone - pharmacology</subject><subject>Kinetics</subject><subject>Leydig Cell Tumor</subject><subject>Leydig Cells - physiology</subject><subject>Magnesium - pharmacology</subject><subject>Male</subject><subject>Mice</subject><subject>Molecular Weight</subject><subject>Prolactin - pharmacology</subject><subject>Prolactin - physiology</subject><subject>Receptors, Prolactin - chemistry</subject><subject>Receptors, Prolactin - physiology</subject><subject>Tumor Cells, Cultured</subject><issn>0037-9727</issn><issn>1535-3702</issn><issn>1535-3699</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1OwzAQRi0EKqVwASQkr9iZ-qd2EnaoooAUBEJlbTnOpE2VJsVOFuUAnBuHFljBamTPm6eZD6FzRq8Ei9mYUhElEY8Ip4pMRCT5ARoyKSQRKkkO0bAHSE8coxPvV5QyGXE1QIOYMsVkMkQfz66pjG3LGps6x3PwbWm7yjicwjYvF3gKVYVnXR2Qpr7G06VxAQdXvpv-BzcF_lW8gIVN2ziPw6NdAn7sXFmHckMY_UueBuIUHRWm8nC2ryP0OrudT-9J-nT3ML1JiRUibkkhFGeRsBmTLJPUGJ7YJFEyM8CMyIEXBchkomhWZJRZIaVhIJVSwCOr8kyM0OXOu3HNWxf20evS27CFqaHpvI6UVBMR0wDyHWhd472DQm9cuTZuqxnVffj6O3wdwtdf4Yehi729y9aQ_4zs0w798a7vzQL0qulcHY79z_gJzxqOBA</recordid><startdate>19940701</startdate><enddate>19940701</enddate><creator>Barkey, Ronnie J.</creator><creator>Weiss-Messer, Esther</creator><creator>Hacham, Haim</creator><creator>Herscovich, Sara</creator><creator>Ber, Rosalie</creator><creator>Amit, Tamar</creator><general>SAGE Publications</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></search><sort><creationdate>19940701</creationdate><title>Prolactin and Testicular Leydig Cell Function: Characterization of Prolactin Receptors in the Murine MA-10 Testicular Leydig Cell Line</title><author>Barkey, Ronnie J. ; Weiss-Messer, Esther ; Hacham, Haim ; Herscovich, Sara ; Ber, Rosalie ; Amit, Tamar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c338t-f362173cb151b50aa29c9965bae1a3de2ffe59460bfb01c355a1e5666e27c6db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Growth Hormone - metabolism</topic><topic>Growth Hormone - pharmacology</topic><topic>Kinetics</topic><topic>Leydig Cell Tumor</topic><topic>Leydig Cells - physiology</topic><topic>Magnesium - pharmacology</topic><topic>Male</topic><topic>Mice</topic><topic>Molecular Weight</topic><topic>Prolactin - pharmacology</topic><topic>Prolactin - physiology</topic><topic>Receptors, Prolactin - chemistry</topic><topic>Receptors, Prolactin - physiology</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barkey, Ronnie J.</creatorcontrib><creatorcontrib>Weiss-Messer, Esther</creatorcontrib><creatorcontrib>Hacham, Haim</creatorcontrib><creatorcontrib>Herscovich, Sara</creatorcontrib><creatorcontrib>Ber, Rosalie</creatorcontrib><creatorcontrib>Amit, Tamar</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><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barkey, Ronnie J.</au><au>Weiss-Messer, Esther</au><au>Hacham, Haim</au><au>Herscovich, Sara</au><au>Ber, Rosalie</au><au>Amit, Tamar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prolactin and Testicular Leydig Cell Function: Characterization of Prolactin Receptors in the Murine MA-10 Testicular Leydig Cell Line</atitle><jtitle>Experimental biology and medicine (Maywood, N.J.)</jtitle><addtitle>Proc Soc Exp Biol Med</addtitle><date>1994-07-01</date><risdate>1994</risdate><volume>206</volume><issue>3</issue><spage>243</spage><epage>248</epage><pages>243-248</pages><issn>0037-9727</issn><issn>1535-3702</issn><eissn>1535-3699</eissn><abstract>Abstract
The direct role of prolactin (PRL) in testicular function is still unclear, mostly because of lack of a suitable in vitro model. To establish the suitability of the MA-10 murine tumor Leydig cell line for the study of PRL receptors (PRLR) and effects on steroidogenesis, we initially characterized PRLR on cultured MA-10 cells. The specific binding (Bs) of [125l]human growth hormone (hGH) depends on time, temperature, and Mg2+ ion and protein concentrations, with absolute specificity for the lactogenic hormones hGH and ovine PRL. Bs is saturable and is to a single class of high-affinity (Ka
= 3.6 × 109
M
-1) low-capacity (B
max = 19.5 fmol/mg protein) binding sites. The molecular weight of PRLR, determined by cross-linking to [125l]hGH, SDS-PAGE and autoradiography, is 35 kDa for the free receptor, suggesting that the short-form PRLR protein, previously described in liver and mammary glands, is that primarily found in MA-10 cells. Thus, the demonstration of specific PRL binding sites on MA-10 Leydig cells, with characteristics similar to primary Leydig cell PRLR, suggests that this cell line can serve as a good model for both the study of PRLR mechanism of action and the role of PRL in Leydig cell function.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>8016159</pmid><doi>10.3181/00379727-206-43752</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Binding Sites Growth Hormone - metabolism Growth Hormone - pharmacology Kinetics Leydig Cell Tumor Leydig Cells - physiology Magnesium - pharmacology Male Mice Molecular Weight Prolactin - pharmacology Prolactin - physiology Receptors, Prolactin - chemistry Receptors, Prolactin - physiology Tumor Cells, Cultured |
| title | Prolactin and Testicular Leydig Cell Function: Characterization of Prolactin Receptors in the Murine MA-10 Testicular Leydig Cell Line |
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