Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland
Identifieur interne : 001044 ( Istex/Corpus ); précédent : 001043; suivant : 001045Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland
Auteurs : Susie I. Ymer ; Paul A. Kelly ; Adrian C. Herington ; Jean DjianeSource :
- Molecular and Cellular Endocrinology [ 0303-7207 ] ; 1987.
English descriptors
- KwdEn :
- Binding capacity, Binding proteins, Biol, Chem, Cytosol, Cytosolic, Cytosolic binding protein, Cytosolic lactogen binding protein, Djiane, Endocrinology, Friesen, Gland cytosol, Herington, Katoh, Kelly, Lactogen, Lactogen binding protein, Lactogen receptor, Mammary gland, Membrane, Membrane receptor, Mllo, Monoclonal, Monoclonal antibodies, Prolactin, Prolactin action, Receptor, Receptor preparations, Specific binding, Target tissues, Various concentrations, Ymer.
- Teeft :
- Binding capacity, Binding proteins, Biol, Chem, Cytosol, Cytosolic, Cytosolic binding protein, Cytosolic lactogen binding protein, Djiane, Endocrinology, Friesen, Gland cytosol, Herington, Katoh, Kelly, Lactogen, Lactogen binding protein, Lactogen receptor, Mammary gland, Membrane, Membrane receptor, Mllo, Monoclonal, Monoclonal antibodies, Prolactin, Prolactin action, Receptor, Receptor preparations, Specific binding, Target tissues, Various concentrations, Ymer.
Abstract
Abstract: We have recently identified and partially characterized a specific lactogen binding protein in rabbit mammary gland cytosol. In this report, studies using pregnant or lactating rabbits are described which further characterize the cytosolic lactogen binding protein in relation to the membrane-bound lactogen receptor. The data show that in pregnant or lactating rabbits the binding capacity (fmol/mg protein) of membranes is at least double that of the cytosol preparation although when expressed on a tissue content basis (fmol/g tissue) there was no membrane-cytosol difference in receptor number. Treatment of lactating rabbits with CB-154, however, caused a marked increase (100–150%) in the binding capacity of membrane-bound receptors with comparatively little effect (+20%) on the cytosolic lactogram binding protein. There was also a marked difference in the association constants for 125I-hGH, with the cytosolic lactogen binding protein exhibiting a 6-fold higher affinity than the membrane-bound receptor. Three anti-prolactin receptor monoclonal antibodies (M110, A82 (antagonists) and A917 (agonist)) have also been used to assess the relative immunological characteristics of the cytosolic lactogen binding protein and the membrane lactogen receptor. Each monoclonal antibody was able to inhibit the specific binding of 125I-hGH to both membranes and cytosol in a dose-dependent manner. However, the order of potency was not identical being M110 > A917 > A82 in membranes and M110 > A82 > A917 in cytosol. A917 was at least 10 times more active in membranes than cytosol whereas A82 was at least 10 times more active in cytosol. Thus the cytosolic lactogen binding protein shares common but not identical immunological epitopes with the classical membrane receptor. The data presented here indicate that the cytosolic lactogen binding protein can be differentiated from the membrane-bound receptor in terms of its affinity for hGH and interaction with specific monoclonal antibodies. Further, the studies with CB-154 indicate that the cytosolic lactogen binding protein may be under different physiological control.
Url:
DOI: 10.1016/0303-7207(87)90193-6
Links to Exploration step
ISTEX:5795CE67052A87A0A52D06976555EDB5D590E69ALe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title><author><name sortKey="Ymer, Susie I" sort="Ymer, Susie I" uniqKey="Ymer S" first="Susie I." last="Ymer">Susie I. Ymer</name><affiliation><mods:affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</mods:affiliation></affiliation></author><author><name sortKey="Kelly, Paul A" sort="Kelly, Paul A" uniqKey="Kelly P" first="Paul A." last="Kelly">Paul A. Kelly</name><affiliation><mods:affiliation>Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada</mods:affiliation></affiliation></author><author><name sortKey="Herington, Adrian C" sort="Herington, Adrian C" uniqKey="Herington A" first="Adrian C." last="Herington">Adrian C. Herington</name><affiliation><mods:affiliation>Address for correspondence: A.C. Herington, Medical Research Centre, Prince Henry's Hospital, St. Kilda Road, Melbourne, Victoria, Australia 3004.</mods:affiliation></affiliation><affiliation><mods:affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</mods:affiliation></affiliation></author><author><name sortKey="Djiane, Jean" sort="Djiane, Jean" uniqKey="Djiane J" first="Jean" last="Djiane">Jean Djiane</name><affiliation><mods:affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:5795CE67052A87A0A52D06976555EDB5D590E69A</idno><date when="1987" year="1987">1987</date><idno type="doi">10.1016/0303-7207(87)90193-6</idno><idno type="url">https://api.istex.fr/document/5795CE67052A87A0A52D06976555EDB5D590E69A/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001044</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001044</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title><author><name sortKey="Ymer, Susie I" sort="Ymer, Susie I" uniqKey="Ymer S" first="Susie I." last="Ymer">Susie I. Ymer</name><affiliation><mods:affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</mods:affiliation></affiliation></author><author><name sortKey="Kelly, Paul A" sort="Kelly, Paul A" uniqKey="Kelly P" first="Paul A." last="Kelly">Paul A. Kelly</name><affiliation><mods:affiliation>Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada</mods:affiliation></affiliation></author><author><name sortKey="Herington, Adrian C" sort="Herington, Adrian C" uniqKey="Herington A" first="Adrian C." last="Herington">Adrian C. Herington</name><affiliation><mods:affiliation>Address for correspondence: A.C. Herington, Medical Research Centre, Prince Henry's Hospital, St. Kilda Road, Melbourne, Victoria, Australia 3004.</mods:affiliation></affiliation><affiliation><mods:affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</mods:affiliation></affiliation></author><author><name sortKey="Djiane, Jean" sort="Djiane, Jean" uniqKey="Djiane J" first="Jean" last="Djiane">Jean Djiane</name><affiliation><mods:affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular and Cellular Endocrinology</title><title level="j" type="abbrev">MCE</title><idno type="ISSN">0303-7207</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">53</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="67">67</biblScope><biblScope unit="page" to="73">73</biblScope></imprint><idno type="ISSN">0303-7207</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0303-7207</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding capacity</term><term>Binding proteins</term><term>Biol</term><term>Chem</term><term>Cytosol</term><term>Cytosolic</term><term>Cytosolic binding protein</term><term>Cytosolic lactogen binding protein</term><term>Djiane</term><term>Endocrinology</term><term>Friesen</term><term>Gland cytosol</term><term>Herington</term><term>Katoh</term><term>Kelly</term><term>Lactogen</term><term>Lactogen binding protein</term><term>Lactogen receptor</term><term>Mammary gland</term><term>Membrane</term><term>Membrane receptor</term><term>Mllo</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Prolactin</term><term>Prolactin action</term><term>Receptor</term><term>Receptor preparations</term><term>Specific binding</term><term>Target tissues</term><term>Various concentrations</term><term>Ymer</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Binding capacity</term><term>Binding proteins</term><term>Biol</term><term>Chem</term><term>Cytosol</term><term>Cytosolic</term><term>Cytosolic binding protein</term><term>Cytosolic lactogen binding protein</term><term>Djiane</term><term>Endocrinology</term><term>Friesen</term><term>Gland cytosol</term><term>Herington</term><term>Katoh</term><term>Kelly</term><term>Lactogen</term><term>Lactogen binding protein</term><term>Lactogen receptor</term><term>Mammary gland</term><term>Membrane</term><term>Membrane receptor</term><term>Mllo</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Prolactin</term><term>Prolactin action</term><term>Receptor</term><term>Receptor preparations</term><term>Specific binding</term><term>Target tissues</term><term>Various concentrations</term><term>Ymer</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We have recently identified and partially characterized a specific lactogen binding protein in rabbit mammary gland cytosol. In this report, studies using pregnant or lactating rabbits are described which further characterize the cytosolic lactogen binding protein in relation to the membrane-bound lactogen receptor. The data show that in pregnant or lactating rabbits the binding capacity (fmol/mg protein) of membranes is at least double that of the cytosol preparation although when expressed on a tissue content basis (fmol/g tissue) there was no membrane-cytosol difference in receptor number. Treatment of lactating rabbits with CB-154, however, caused a marked increase (100–150%) in the binding capacity of membrane-bound receptors with comparatively little effect (+20%) on the cytosolic lactogram binding protein. There was also a marked difference in the association constants for 125I-hGH, with the cytosolic lactogen binding protein exhibiting a 6-fold higher affinity than the membrane-bound receptor. Three anti-prolactin receptor monoclonal antibodies (M110, A82 (antagonists) and A917 (agonist)) have also been used to assess the relative immunological characteristics of the cytosolic lactogen binding protein and the membrane lactogen receptor. Each monoclonal antibody was able to inhibit the specific binding of 125I-hGH to both membranes and cytosol in a dose-dependent manner. However, the order of potency was not identical being M110 > A917 > A82 in membranes and M110 > A82 > A917 in cytosol. A917 was at least 10 times more active in membranes than cytosol whereas A82 was at least 10 times more active in cytosol. Thus the cytosolic lactogen binding protein shares common but not identical immunological epitopes with the classical membrane receptor. The data presented here indicate that the cytosolic lactogen binding protein can be differentiated from the membrane-bound receptor in terms of its affinity for hGH and interaction with specific monoclonal antibodies. Further, the studies with CB-154 indicate that the cytosolic lactogen binding protein may be under different physiological control.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>receptor</json:string><json:string>lactogen</json:string><json:string>cytosol</json:string><json:string>cytosolic</json:string><json:string>herington</json:string><json:string>ymer</json:string><json:string>cytosolic lactogen binding protein</json:string><json:string>djiane</json:string><json:string>monoclonal</json:string><json:string>prolactin</json:string><json:string>monoclonal antibodies</json:string><json:string>biol</json:string><json:string>chem</json:string><json:string>katoh</json:string><json:string>endocrinology</json:string><json:string>binding proteins</json:string><json:string>friesen</json:string><json:string>mllo</json:string><json:string>specific binding</json:string><json:string>mammary gland</json:string><json:string>lactogen receptor</json:string><json:string>membrane receptor</json:string><json:string>cytosolic binding protein</json:string><json:string>kelly</json:string><json:string>membrane</json:string><json:string>receptor preparations</json:string><json:string>lactogen binding protein</json:string><json:string>various concentrations</json:string><json:string>prolactin action</json:string><json:string>binding capacity</json:string><json:string>target tissues</json:string><json:string>gland cytosol</json:string></teeft></keywords><author><json:item><name>Susie I. Ymer</name><affiliations><json:string>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</json:string><json:string>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</json:string></affiliations></json:item><json:item><name>Paul A. Kelly</name><affiliations><json:string>Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada</json:string></affiliations></json:item><json:item><name>Adrian C. Herington</name><affiliations><json:string>Address for correspondence: A.C. Herington, Medical Research Centre, Prince Henry's Hospital, St. Kilda Road, Melbourne, Victoria, Australia 3004.</json:string><json:string>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</json:string></affiliations></json:item><json:item><name>Jean Djiane</name><affiliations><json:string>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Prolactin receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Mammary gland</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>(Cytosol)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>(Membrane)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>(Rabbit)</value></json:item></subject><arkIstex>ark:/67375/6H6-MRSLRP3X-L</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: We have recently identified and partially characterized a specific lactogen binding protein in rabbit mammary gland cytosol. In this report, studies using pregnant or lactating rabbits are described which further characterize the cytosolic lactogen binding protein in relation to the membrane-bound lactogen receptor. The data show that in pregnant or lactating rabbits the binding capacity (fmol/mg protein) of membranes is at least double that of the cytosol preparation although when expressed on a tissue content basis (fmol/g tissue) there was no membrane-cytosol difference in receptor number. Treatment of lactating rabbits with CB-154, however, caused a marked increase (100–150%) in the binding capacity of membrane-bound receptors with comparatively little effect (+20%) on the cytosolic lactogram binding protein. There was also a marked difference in the association constants for 125I-hGH, with the cytosolic lactogen binding protein exhibiting a 6-fold higher affinity than the membrane-bound receptor. Three anti-prolactin receptor monoclonal antibodies (M110, A82 (antagonists) and A917 (agonist)) have also been used to assess the relative immunological characteristics of the cytosolic lactogen binding protein and the membrane lactogen receptor. Each monoclonal antibody was able to inhibit the specific binding of 125I-hGH to both membranes and cytosol in a dose-dependent manner. However, the order of potency was not identical being M110 > A917 > A82 in membranes and M110 > A82 > A917 in cytosol. A917 was at least 10 times more active in membranes than cytosol whereas A82 was at least 10 times more active in cytosol. Thus the cytosolic lactogen binding protein shares common but not identical immunological epitopes with the classical membrane receptor. The data presented here indicate that the cytosolic lactogen binding protein can be differentiated from the membrane-bound receptor in terms of its affinity for hGH and interaction with specific monoclonal antibodies. Further, the studies with CB-154 indicate that the cytosolic lactogen binding protein may be under different physiological control.</abstract><qualityIndicators><score>8.558</score><pdfWordCount>3558</pdfWordCount><pdfCharCount>23094</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>540 x 684 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>311</abstractWordCount><abstractCharCount>2139</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title><pmid><json:string>3666294</json:string></pmid><pii><json:string>0303-7207(87)90193-6</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Molecular and Cellular Endocrinology</title><language><json:string>unknown</json:string></language><publicationDate>1987</publicationDate><issn><json:string>0303-7207</json:string></issn><pii><json:string>S0303-7207(00)X0259-6</json:string></pii><volume>53</volume><issue>1–2</issue><pages><first>67</first><last>73</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1987</json:string><json:string>1251</json:string></date><geogName></geogName><orgName><json:string>Elsevier Scientific Publishers Ireland, Ltd</json:string><json:string>Medical Research Cenfre, Prince</json:string><json:string>Medical Research Centre, Prince</json:string><json:string>Oreal Marigny Pty.</json:string><json:string>New Zealand White</json:string><json:string>National Health and Medical Research</json:string><json:string>Hospital, Melbourne</json:string><json:string>National Hormone and Pituitary Program</json:string><json:string>I</json:string></orgName><orgName_funder><json:string>I</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Jean Djiane</json:string><json:string>Paul A. Kelly</json:string><json:string>Hemy</json:string><json:string>Henry</json:string><json:string>In</json:string><json:string>A.C. Rerington</json:string><json:string>Adrian C. Herington</json:string><json:string>Susie I. Ymer</json:string><json:string>Victoria Hospital</json:string></persName><placeName><json:string>Switzerland</json:string><json:string>Australia</json:string><json:string>Canada</json:string><json:string>Melbourne</json:string><json:string>Darmstadt</json:string><json:string>Victoria</json:string><json:string>Basel</json:string><json:string>Quebec</json:string><json:string>Capacity</json:string><json:string>Sweden</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Djiane et al.</json:string><json:string>Djiane et al., 3985</json:string><json:string>Shiu and Friesen, 1974a</json:string><json:string>Gavish et al., 1983</json:string><json:string>Scatchard, 1949</json:string><json:string>Rae-Venter et al., 1982</json:string><json:string>Herington et al., 1986</json:string><json:string>Bonifacino et al., 1978</json:string><json:string>Djiane et al., 1981</json:string><json:string>Ymer and Herington, 1986</json:string><json:string>Ymer et al., 1984</json:string><json:string>Baumann et al., 1986</json:string><json:string>Bonifacino and Dufau, 1984</json:string><json:string>Dusanter-Fourt et al.</json:string><json:string>Necessary et al., 1984</json:string><json:string>KelIy et al. (1979)</json:string><json:string>Djiane et al., 1985</json:string><json:string>Haeuptle et al., 1983</json:string><json:string>Jaffe, 1982</json:string><json:string>Sakai et al., 1985</json:string><json:string>Josefsberg et al., 1979</json:string><json:string>Ymer and Herington, 1984, 1985</json:string><json:string>Herington et al., 1986a</json:string><json:string>Hughes et al., 1983</json:string><json:string>Katoh et al., 1985b</json:string><json:string>Herington et al., 1986a, b</json:string><json:string>Sasaki et al., 1982</json:string><json:string>Suard et al., 1979</json:string><json:string>Herington et al., 1986b, c</json:string><json:string>Katoh et al., 1985a</json:string><json:string>Waters et al., 1984</json:string><json:string>Amit et al., 1984, 1985</json:string><json:string>Djiane et al., 1977</json:string><json:string>Shiu and Friesen, 1974b</json:string><json:string>Lowry et al. (1951)</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-MRSLRP3X-L</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - endocrinology & metabolism</json:string><json:string>2 - cell biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - clinical medicine</json:string><json:string>3 - endocrinology & metabolism</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Endocrinology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1987</publicationDate><copyrightDate>1987</copyrightDate><doi><json:string>10.1016/0303-7207(87)90193-6</json:string></doi><id>5795CE67052A87A0A52D06976555EDB5D590E69A</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/5795CE67052A87A0A52D06976555EDB5D590E69A/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/5795CE67052A87A0A52D06976555EDB5D590E69A/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/5795CE67052A87A0A52D06976555EDB5D590E69A/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1987</date></publicationStmt><notesStmt><note type="content">Section title: Research paper</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title><author xml:id="author-0000"><persName><forename type="first">Susie I.</forename><surname>Ymer</surname></persName><affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</affiliation><affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Paul A.</forename><surname>Kelly</surname></persName><affiliation>Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Adrian C.</forename><surname>Herington</surname></persName><affiliation>Address for correspondence: A.C. Herington, Medical Research Centre, Prince Henry's Hospital, St. Kilda Road, Melbourne, Victoria, Australia 3004.</affiliation><affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Jean</forename><surname>Djiane</surname></persName><affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</affiliation></author><idno type="istex">5795CE67052A87A0A52D06976555EDB5D590E69A</idno><idno type="DOI">10.1016/0303-7207(87)90193-6</idno><idno type="PII">0303-7207(87)90193-6</idno></analytic><monogr><title level="j">Molecular and Cellular Endocrinology</title><title level="j" type="abbrev">MCE</title><idno type="pISSN">0303-7207</idno><idno type="PII">S0303-7207(00)X0259-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987"></date><biblScope unit="volume">53</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="67">67</biblScope><biblScope unit="page" to="73">73</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1987</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>We have recently identified and partially characterized a specific lactogen binding protein in rabbit mammary gland cytosol. In this report, studies using pregnant or lactating rabbits are described which further characterize the cytosolic lactogen binding protein in relation to the membrane-bound lactogen receptor. The data show that in pregnant or lactating rabbits the binding capacity (fmol/mg protein) of membranes is at least double that of the cytosol preparation although when expressed on a tissue content basis (fmol/g tissue) there was no membrane-cytosol difference in receptor number. Treatment of lactating rabbits with CB-154, however, caused a marked increase (100–150%) in the binding capacity of membrane-bound receptors with comparatively little effect (+20%) on the cytosolic lactogram binding protein. There was also a marked difference in the association constants for 125I-hGH, with the cytosolic lactogen binding protein exhibiting a 6-fold higher affinity than the membrane-bound receptor. Three anti-prolactin receptor monoclonal antibodies (M110, A82 (antagonists) and A917 (agonist)) have also been used to assess the relative immunological characteristics of the cytosolic lactogen binding protein and the membrane lactogen receptor. Each monoclonal antibody was able to inhibit the specific binding of 125I-hGH to both membranes and cytosol in a dose-dependent manner. However, the order of potency was not identical being M110 > A917 > A82 in membranes and M110 > A82 > A917 in cytosol. A917 was at least 10 times more active in membranes than cytosol whereas A82 was at least 10 times more active in cytosol. Thus the cytosolic lactogen binding protein shares common but not identical immunological epitopes with the classical membrane receptor. The data presented here indicate that the cytosolic lactogen binding protein can be differentiated from the membrane-bound receptor in terms of its affinity for hGH and interaction with specific monoclonal antibodies. Further, the studies with CB-154 indicate that the cytosolic lactogen binding protein may be under different physiological control.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Prolactin receptor</term></item><item><term>Mammary gland</term></item><item><term>(Cytosol)</term></item><item><term>(Membrane)</term></item><item><term>(Rabbit)</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1987">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/5795CE67052A87A0A52D06976555EDB5D590E69A/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>MCE</jid><aid>87901936</aid><ce:pii>0303-7207(87)90193-6</ce:pii><ce:doi>10.1016/0303-7207(87)90193-6</ce:doi><ce:copyright type="unknown" year="1987"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Research paper</ce:textfn></ce:dochead><ce:title>Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</ce:title><ce:author-group><ce:author><ce:given-name>Susie I.</ce:given-name><ce:surname>Ymer</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Paul A.</ce:given-name><ce:surname>Kelly</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>3</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Adrian C.</ce:given-name><ce:surname>Herington</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean</ce:given-name><ce:surname>Djiane</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>1</ce:label><ce:textfn>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>2</ce:label><ce:textfn>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>3</ce:label><ce:textfn>Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Address for correspondence: A.C. Herington, Medical Research Centre, Prince Henry's Hospital, St. Kilda Road, Melbourne, Victoria, Australia 3004.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="2" month="3" year="1987"></ce:date-received><ce:date-accepted day="22" month="4" year="1987"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>We have recently identified and partially characterized a specific lactogen binding protein in rabbit mammary gland cytosol. In this report, studies using pregnant or lactating rabbits are described which further characterize the cytosolic lactogen binding protein in relation to the membrane-bound lactogen receptor. The data show that in pregnant or lactating rabbits the binding capacity (fmol/mg protein) of membranes is at least double that of the cytosol preparation although when expressed on a tissue content basis (fmol/g tissue) there was no membrane-cytosol difference in receptor number. Treatment of lactating rabbits with CB-154, however, caused a marked increase (100–150%) in the binding capacity of membrane-bound receptors with comparatively little effect (+20%) on the cytosolic lactogram binding protein. There was also a marked difference in the association constants for <ce:sup loc="pre">125</ce:sup>I-hGH, with the cytosolic lactogen binding protein exhibiting a 6-fold higher affinity than the membrane-bound receptor. Three anti-prolactin receptor monoclonal antibodies (M110, A82 (antagonists) and A917 (agonist)) have also been used to assess the relative immunological characteristics of the cytosolic lactogen binding protein and the membrane lactogen receptor. Each monoclonal antibody was able to inhibit the specific binding of <ce:sup loc="pre">125</ce:sup>I-hGH to both membranes and cytosol in a dose-dependent manner. However, the order of potency was not identical being M110 > A917 > A82 in membranes and M110 > A82 > A917 in cytosol. A917 was at least 10 times more active in membranes than cytosol whereas A82 was at least 10 times more active in cytosol. Thus the cytosolic lactogen binding protein shares common but not identical immunological epitopes with the classical membrane receptor.</ce:simple-para><ce:simple-para>The data presented here indicate that the cytosolic lactogen binding protein can be differentiated from the membrane-bound receptor in terms of its affinity for hGH and interaction with specific monoclonal antibodies. Further, the studies with CB-154 indicate that the cytosolic lactogen binding protein may be under different physiological control.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Prolactin receptor</ce:text></ce:keyword><ce:keyword><ce:text>Mammary gland</ce:text></ce:keyword><ce:keyword><ce:text>(Cytosol)</ce:text></ce:keyword><ce:keyword><ce:text>(Membrane)</ce:text></ce:keyword><ce:keyword><ce:text>(Rabbit)</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland</title></titleInfo><name type="personal"><namePart type="given">Susie I.</namePart><namePart type="family">Ymer</namePart><affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</affiliation><affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Paul A.</namePart><namePart type="family">Kelly</namePart><affiliation>Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec H3A 1A1, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Adrian C.</namePart><namePart type="family">Herington</namePart><affiliation>Address for correspondence: A.C. Herington, Medical Research Centre, Prince Henry's Hospital, St. Kilda Road, Melbourne, Victoria, Australia 3004.</affiliation><affiliation>Medical Research Centre, Prince Henry's Hospital, Melbourne 3004, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean</namePart><namePart type="family">Djiane</namePart><affiliation>Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1987</dateIssued><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: We have recently identified and partially characterized a specific lactogen binding protein in rabbit mammary gland cytosol. In this report, studies using pregnant or lactating rabbits are described which further characterize the cytosolic lactogen binding protein in relation to the membrane-bound lactogen receptor. The data show that in pregnant or lactating rabbits the binding capacity (fmol/mg protein) of membranes is at least double that of the cytosol preparation although when expressed on a tissue content basis (fmol/g tissue) there was no membrane-cytosol difference in receptor number. Treatment of lactating rabbits with CB-154, however, caused a marked increase (100–150%) in the binding capacity of membrane-bound receptors with comparatively little effect (+20%) on the cytosolic lactogram binding protein. There was also a marked difference in the association constants for 125I-hGH, with the cytosolic lactogen binding protein exhibiting a 6-fold higher affinity than the membrane-bound receptor. Three anti-prolactin receptor monoclonal antibodies (M110, A82 (antagonists) and A917 (agonist)) have also been used to assess the relative immunological characteristics of the cytosolic lactogen binding protein and the membrane lactogen receptor. Each monoclonal antibody was able to inhibit the specific binding of 125I-hGH to both membranes and cytosol in a dose-dependent manner. However, the order of potency was not identical being M110 > A917 > A82 in membranes and M110 > A82 > A917 in cytosol. A917 was at least 10 times more active in membranes than cytosol whereas A82 was at least 10 times more active in cytosol. Thus the cytosolic lactogen binding protein shares common but not identical immunological epitopes with the classical membrane receptor. The data presented here indicate that the cytosolic lactogen binding protein can be differentiated from the membrane-bound receptor in terms of its affinity for hGH and interaction with specific monoclonal antibodies. Further, the studies with CB-154 indicate that the cytosolic lactogen binding protein may be under different physiological control.</abstract><note type="content">Section title: Research paper</note><subject><genre>Keywords</genre><topic>Prolactin receptor</topic><topic>Mammary gland</topic><topic>(Cytosol)</topic><topic>(Membrane)</topic><topic>(Rabbit)</topic></subject><relatedItem type="host"><titleInfo><title>Molecular and Cellular Endocrinology</title></titleInfo><titleInfo type="abbreviated"><title>MCE</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">198709</dateIssued></originInfo><identifier type="ISSN">0303-7207</identifier><identifier type="PII">S0303-7207(00)X0259-6</identifier><part><date>198709</date><detail type="volume"><number>53</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>152</end></extent><extent unit="pages"><start>67</start><end>73</end></extent></part></relatedItem><identifier type="istex">5795CE67052A87A0A52D06976555EDB5D590E69A</identifier><identifier type="ark">ark:/67375/6H6-MRSLRP3X-L</identifier><identifier type="DOI">10.1016/0303-7207(87)90193-6</identifier><identifier type="PII">0303-7207(87)90193-6</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/5795CE67052A87A0A52D06976555EDB5D590E69A/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001044 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 001044 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Asie
|area= AustralieFrV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:5795CE67052A87A0A52D06976555EDB5D590E69A
|texte= Immunological relationship and binding capacity of prolactin receptors in cytosolic and membrane fractions of rabbit mammary gland
}}
| This area was generated with Dilib version V0.6.33. |  |