Sea bass ( Dicentrarchus labrax) sex hormone binding globulin: molecular and biochemical properties and phylogenetic comparison of its orthologues in multiple fish species
Sex hormone binding globulin (SHBG) binds and transports androgens and estrogens in the blood of vertebrate species including fish. We have used oligonucleotide primers corresponding to highly conserved regions of the SHBG coding sequences within the zebrafish and fugufish genomes to obtain a 1528 b...
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| Veröffentlicht in: | Molecular and cellular endocrinology 2005-01, Vol.229 (1), p.21-29 |
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| creator | Miguel-Queralt, Solange Avvakumov, George V. Blázquez, Mercedes Piferrer, Francesc Hammond, Geoffrey L. |
| description | Sex hormone binding globulin (SHBG) binds and transports androgens and estrogens in the blood of vertebrate species including fish. We have used oligonucleotide primers corresponding to highly conserved regions of the SHBG coding sequences within the zebrafish and fugufish genomes to obtain a 1528
bp cDNA encoding SHBG from tissue RNA extracts from the European sea bass. Amino-terminal sequence analysis of recombinant sea bass SHBG indicated that its deduced precursor polypeptide includes a 35-residue secretion signal polypeptide, and the 361-residue mature sea bass SHBG sequence exhibits 45–67% sequence identity with SHBGs from other fish species that have been determined directly (for zebrafish) or deduced (for rainbow trout, medaka and fugufish) from sequences within public databases. The sea bass SHBG (39,894
Da) comprises a tandem repeat of laminin G-like domains typical of SHBG sequences; contains three
N-glycosylation sites, and exists as a 118,300
±
11,500
Da homodimer. Sea bass SHBG exhibits a high affinity (
K
d
=
8.8
nM for 17β-estradiol) and specificity for gonadal steroids and their precursors (e.g., 17β-estradiol
>
testosterone
>
dehydroepiandrosterone
>
5α-dihydrotestosterone
>
androstenedione
>
11-ketotesterone). Interestingly, the affinity of sea bass SHBG for the synthetic estrogen, 17α-ethynylestradiol was found to be essentially identical to that for 17β-estradiol. The availability of SHBG sequences in sea bass and other fish set the stage for detailed studies of SHBG function in fish reproductive physiology, as well as its potential role as a target of endocrine disruptors. |
| doi_str_mv | 10.1016/j.mce.2004.10.004 |
| format | Article |
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bp cDNA encoding SHBG from tissue RNA extracts from the European sea bass. Amino-terminal sequence analysis of recombinant sea bass SHBG indicated that its deduced precursor polypeptide includes a 35-residue secretion signal polypeptide, and the 361-residue mature sea bass SHBG sequence exhibits 45–67% sequence identity with SHBGs from other fish species that have been determined directly (for zebrafish) or deduced (for rainbow trout, medaka and fugufish) from sequences within public databases. The sea bass SHBG (39,894
Da) comprises a tandem repeat of laminin G-like domains typical of SHBG sequences; contains three
N-glycosylation sites, and exists as a 118,300
±
11,500
Da homodimer. Sea bass SHBG exhibits a high affinity (
K
d
=
8.8
nM for 17β-estradiol) and specificity for gonadal steroids and their precursors (e.g., 17β-estradiol
>
testosterone
>
dehydroepiandrosterone
>
5α-dihydrotestosterone
>
androstenedione
>
11-ketotesterone). Interestingly, the affinity of sea bass SHBG for the synthetic estrogen, 17α-ethynylestradiol was found to be essentially identical to that for 17β-estradiol. The availability of SHBG sequences in sea bass and other fish set the stage for detailed studies of SHBG function in fish reproductive physiology, as well as its potential role as a target of endocrine disruptors.</description><identifier>ISSN: 0303-7207</identifier><identifier>EISSN: 1872-8057</identifier><identifier>DOI: 10.1016/j.mce.2004.10.004</identifier><identifier>PMID: 15607525</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>17α-Ethynylestradiol ; 17β-Estradiol ; Amino Acid Sequence ; Animals ; Base Sequence ; Bass - physiology ; cDNA ; CHO Cells - drug effects ; Cloning, Molecular ; Cricetinae ; Databases, Genetic ; Gonadal Steroid Hormones - pharmacology ; Kidney - metabolism ; Liver - metabolism ; Molecular Sequence Data ; Phylogenetic tree ; Phylogeny ; Primary structure ; Rabbits ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Recombinant Proteins - metabolism ; Sea bass ; Sequence Homology, Amino Acid ; Sex hormone binding globulin ; Sex Hormone-Binding Globulin - genetics ; Sex Hormone-Binding Globulin - immunology ; Sex Hormone-Binding Globulin - metabolism ; Steroid-binding properties</subject><ispartof>Molecular and cellular endocrinology, 2005-01, Vol.229 (1), p.21-29</ispartof><rights>2004 Elsevier Ireland Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-63f06a7baa1226b7453bbc43f7973a8cd4f49eb2c94ff29e9d4674a8fdd57a7d3</citedby><cites>FETCH-LOGICAL-c382t-63f06a7baa1226b7453bbc43f7973a8cd4f49eb2c94ff29e9d4674a8fdd57a7d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.mce.2004.10.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15607525$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miguel-Queralt, Solange</creatorcontrib><creatorcontrib>Avvakumov, George V.</creatorcontrib><creatorcontrib>Blázquez, Mercedes</creatorcontrib><creatorcontrib>Piferrer, Francesc</creatorcontrib><creatorcontrib>Hammond, Geoffrey L.</creatorcontrib><title>Sea bass ( Dicentrarchus labrax) sex hormone binding globulin: molecular and biochemical properties and phylogenetic comparison of its orthologues in multiple fish species</title><title>Molecular and cellular endocrinology</title><addtitle>Mol Cell Endocrinol</addtitle><description>Sex hormone binding globulin (SHBG) binds and transports androgens and estrogens in the blood of vertebrate species including fish. We have used oligonucleotide primers corresponding to highly conserved regions of the SHBG coding sequences within the zebrafish and fugufish genomes to obtain a 1528
bp cDNA encoding SHBG from tissue RNA extracts from the European sea bass. Amino-terminal sequence analysis of recombinant sea bass SHBG indicated that its deduced precursor polypeptide includes a 35-residue secretion signal polypeptide, and the 361-residue mature sea bass SHBG sequence exhibits 45–67% sequence identity with SHBGs from other fish species that have been determined directly (for zebrafish) or deduced (for rainbow trout, medaka and fugufish) from sequences within public databases. The sea bass SHBG (39,894
Da) comprises a tandem repeat of laminin G-like domains typical of SHBG sequences; contains three
N-glycosylation sites, and exists as a 118,300
±
11,500
Da homodimer. Sea bass SHBG exhibits a high affinity (
K
d
=
8.8
nM for 17β-estradiol) and specificity for gonadal steroids and their precursors (e.g., 17β-estradiol
>
testosterone
>
dehydroepiandrosterone
>
5α-dihydrotestosterone
>
androstenedione
>
11-ketotesterone). Interestingly, the affinity of sea bass SHBG for the synthetic estrogen, 17α-ethynylestradiol was found to be essentially identical to that for 17β-estradiol. The availability of SHBG sequences in sea bass and other fish set the stage for detailed studies of SHBG function in fish reproductive physiology, as well as its potential role as a target of endocrine disruptors.</description><subject>17α-Ethynylestradiol</subject><subject>17β-Estradiol</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Bass - physiology</subject><subject>cDNA</subject><subject>CHO Cells - drug effects</subject><subject>Cloning, Molecular</subject><subject>Cricetinae</subject><subject>Databases, Genetic</subject><subject>Gonadal Steroid Hormones - pharmacology</subject><subject>Kidney - metabolism</subject><subject>Liver - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Phylogenetic tree</subject><subject>Phylogeny</subject><subject>Primary structure</subject><subject>Rabbits</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sea bass</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sex hormone binding globulin</subject><subject>Sex Hormone-Binding Globulin - genetics</subject><subject>Sex Hormone-Binding Globulin - immunology</subject><subject>Sex Hormone-Binding Globulin - metabolism</subject><subject>Steroid-binding properties</subject><issn>0303-7207</issn><issn>1872-8057</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2OFCEUhYnROO3oA7gxrIwuqqWAKqp1ZcbxJ5nEhbom_Fy66FBQQpWZeSZfUnq6E3e6usD97snlHISet2TbkrZ_c9hOBraUEF7v21oeoE07CNoMpBMP0YYwwhpBibhAT0o5EEJER4fH6KLt-uOx26Df30BhrUrBr_AHbyAuWWUzrgUHpbO6fY0L3OIx5SlFwNpH6-Me70PSa_DxLZ5SALMGlbGKtvaTGWHyRgU85zRDXjyU-9Y83oW0hwiLN9ikaVbZlxRxctgvBae8jKkCa8V9xNMaFj8HwM6XEZcZTNV5ih45FQo8O9dL9OPj9ferz83N109frt7fNIYNdGl65kivhFaqpbTXgndMa8OZEzvB1GAsd3wHmpodd47uYGd5L7ganLWdUMKyS_TypFu_8LMutMjJFwMhqAhpLbIXjHFC-X_BVjAyVMcr2J5Ak1MpGZycs59UvpMtkcco5UHWKOUxyuNTLXXmxVl81RPYvxPn7Crw7gRA9eKXhyxLdSkasD6DWaRN_h_yfwBn_rNT</recordid><startdate>20050114</startdate><enddate>20050114</enddate><creator>Miguel-Queralt, Solange</creator><creator>Avvakumov, George V.</creator><creator>Blázquez, Mercedes</creator><creator>Piferrer, Francesc</creator><creator>Hammond, Geoffrey L.</creator><general>Elsevier Ireland Ltd</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20050114</creationdate><title>Sea bass ( Dicentrarchus labrax) sex hormone binding globulin: molecular and biochemical properties and phylogenetic comparison of its orthologues in multiple fish species</title><author>Miguel-Queralt, Solange ; Avvakumov, George V. ; Blázquez, Mercedes ; Piferrer, Francesc ; Hammond, Geoffrey L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-63f06a7baa1226b7453bbc43f7973a8cd4f49eb2c94ff29e9d4674a8fdd57a7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>17α-Ethynylestradiol</topic><topic>17β-Estradiol</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Bass - physiology</topic><topic>cDNA</topic><topic>CHO Cells - drug effects</topic><topic>Cloning, Molecular</topic><topic>Cricetinae</topic><topic>Databases, Genetic</topic><topic>Gonadal Steroid Hormones - pharmacology</topic><topic>Kidney - metabolism</topic><topic>Liver - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Phylogenetic tree</topic><topic>Phylogeny</topic><topic>Primary structure</topic><topic>Rabbits</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sea bass</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sex hormone binding globulin</topic><topic>Sex Hormone-Binding Globulin - genetics</topic><topic>Sex Hormone-Binding Globulin - immunology</topic><topic>Sex Hormone-Binding Globulin - metabolism</topic><topic>Steroid-binding properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miguel-Queralt, Solange</creatorcontrib><creatorcontrib>Avvakumov, George V.</creatorcontrib><creatorcontrib>Blázquez, Mercedes</creatorcontrib><creatorcontrib>Piferrer, Francesc</creatorcontrib><creatorcontrib>Hammond, Geoffrey L.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular endocrinology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miguel-Queralt, Solange</au><au>Avvakumov, George V.</au><au>Blázquez, Mercedes</au><au>Piferrer, Francesc</au><au>Hammond, Geoffrey L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sea bass ( Dicentrarchus labrax) sex hormone binding globulin: molecular and biochemical properties and phylogenetic comparison of its orthologues in multiple fish species</atitle><jtitle>Molecular and cellular endocrinology</jtitle><addtitle>Mol Cell Endocrinol</addtitle><date>2005-01-14</date><risdate>2005</risdate><volume>229</volume><issue>1</issue><spage>21</spage><epage>29</epage><pages>21-29</pages><issn>0303-7207</issn><eissn>1872-8057</eissn><abstract>Sex hormone binding globulin (SHBG) binds and transports androgens and estrogens in the blood of vertebrate species including fish. We have used oligonucleotide primers corresponding to highly conserved regions of the SHBG coding sequences within the zebrafish and fugufish genomes to obtain a 1528
bp cDNA encoding SHBG from tissue RNA extracts from the European sea bass. Amino-terminal sequence analysis of recombinant sea bass SHBG indicated that its deduced precursor polypeptide includes a 35-residue secretion signal polypeptide, and the 361-residue mature sea bass SHBG sequence exhibits 45–67% sequence identity with SHBGs from other fish species that have been determined directly (for zebrafish) or deduced (for rainbow trout, medaka and fugufish) from sequences within public databases. The sea bass SHBG (39,894
Da) comprises a tandem repeat of laminin G-like domains typical of SHBG sequences; contains three
N-glycosylation sites, and exists as a 118,300
±
11,500
Da homodimer. Sea bass SHBG exhibits a high affinity (
K
d
=
8.8
nM for 17β-estradiol) and specificity for gonadal steroids and their precursors (e.g., 17β-estradiol
>
testosterone
>
dehydroepiandrosterone
>
5α-dihydrotestosterone
>
androstenedione
>
11-ketotesterone). Interestingly, the affinity of sea bass SHBG for the synthetic estrogen, 17α-ethynylestradiol was found to be essentially identical to that for 17β-estradiol. The availability of SHBG sequences in sea bass and other fish set the stage for detailed studies of SHBG function in fish reproductive physiology, as well as its potential role as a target of endocrine disruptors.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>15607525</pmid><doi>10.1016/j.mce.2004.10.004</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0303-7207 |
| ispartof | Molecular and cellular endocrinology, 2005-01, Vol.229 (1), p.21-29 |
| issn | 0303-7207 1872-8057 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67334024 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | 17α-Ethynylestradiol 17β-Estradiol Amino Acid Sequence Animals Base Sequence Bass - physiology cDNA CHO Cells - drug effects Cloning, Molecular Cricetinae Databases, Genetic Gonadal Steroid Hormones - pharmacology Kidney - metabolism Liver - metabolism Molecular Sequence Data Phylogenetic tree Phylogeny Primary structure Rabbits Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - metabolism Sea bass Sequence Homology, Amino Acid Sex hormone binding globulin Sex Hormone-Binding Globulin - genetics Sex Hormone-Binding Globulin - immunology Sex Hormone-Binding Globulin - metabolism Steroid-binding properties |
| title | Sea bass ( Dicentrarchus labrax) sex hormone binding globulin: molecular and biochemical properties and phylogenetic comparison of its orthologues in multiple fish species |
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