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Article: Expression of rabbit sex hormone-binding globulin during pregnancy and prenatal development and identification of a novel isoform

TitleExpression of rabbit sex hormone-binding globulin during pregnancy and prenatal development and identification of a novel isoform
Authors
Issue Date2005
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 2005, v. 146 n. 4, p. 1965-1972 How to Cite?
AbstractSHBG is a homodimeric plasma glycoprotein. It functions as a carrier for sex steroids in blood and regulates their access to target cells. In human and rabbit, SHBG is a single-copy gene comprised of eight exons and is expressed primarily in the liver and testis. In the present study, the ontogeny of rabbit SHBG (rbSHBG) gene expression was examined in both fetus and mothers. Trace amounts of rbSHBG mRNA were detected in fetal liver from d 11 to d 29 gestation. These levels increased dramatically at d 30 and remained high until parturition (d 33). In contrast, high levels of rbSHBG mRNA were detected in the maternal liver early during pregnancy, with maximal levels being attained by d 22 and declining markedly thereafter. A rbSHBG transcript lacking the exon 4 sequences was consistently expressed along with the rbSHBG mRNA. When expressed as a glutathione-S-transferase-fusion protein, this alternatively spliced rbSHBG transcript resulted in a product with almost no steroid binding activity, unlike the full-length rbSHBG-glutathione-S-transferase fusion protein, which bound 5α-dihydrotestosterone. Antibody specific to the novel rbSHBG isoform lacking the exon 4-encoding domain was raised, and a single immunoreactive protein of 33-35 kDa was detected by Western blot analysis in both fetal and maternal liver, and this indicates that the rbSHBG transcripts lacking exon 4 sequences are translated in vivo. An RT-PCR analysis further revealed that this alternatively spliced SHBG transcript is present in human HepG2 cells as well as human and mouse testes, indicating that exon 4 splicing in SHBG transcription is conserved among mammalian species. To our knowledge, this is the first report of the identification of a SHBG exon 4 splice variant that is translated. Because the SHBG isoform it encodes lacks appreciable steroid-binding activity, it may function beyond that of the widely accepted role of SHBG as a steroid-transport protein. Copyright © 2005 by The Endocrine Society.
Persistent Identifierhttp://hdl.handle.net/10722/84638
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorNg, KMen_HK
dc.contributor.authorSo, MTen_HK
dc.contributor.authorLee, WMen_HK
dc.date.accessioned2010-09-06T08:55:23Z-
dc.date.available2010-09-06T08:55:23Z-
dc.date.issued2005en_HK
dc.identifier.citationEndocrinology, 2005, v. 146 n. 4, p. 1965-1972en_HK
dc.identifier.issn0013-7227en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84638-
dc.description.abstractSHBG is a homodimeric plasma glycoprotein. It functions as a carrier for sex steroids in blood and regulates their access to target cells. In human and rabbit, SHBG is a single-copy gene comprised of eight exons and is expressed primarily in the liver and testis. In the present study, the ontogeny of rabbit SHBG (rbSHBG) gene expression was examined in both fetus and mothers. Trace amounts of rbSHBG mRNA were detected in fetal liver from d 11 to d 29 gestation. These levels increased dramatically at d 30 and remained high until parturition (d 33). In contrast, high levels of rbSHBG mRNA were detected in the maternal liver early during pregnancy, with maximal levels being attained by d 22 and declining markedly thereafter. A rbSHBG transcript lacking the exon 4 sequences was consistently expressed along with the rbSHBG mRNA. When expressed as a glutathione-S-transferase-fusion protein, this alternatively spliced rbSHBG transcript resulted in a product with almost no steroid binding activity, unlike the full-length rbSHBG-glutathione-S-transferase fusion protein, which bound 5α-dihydrotestosterone. Antibody specific to the novel rbSHBG isoform lacking the exon 4-encoding domain was raised, and a single immunoreactive protein of 33-35 kDa was detected by Western blot analysis in both fetal and maternal liver, and this indicates that the rbSHBG transcripts lacking exon 4 sequences are translated in vivo. An RT-PCR analysis further revealed that this alternatively spliced SHBG transcript is present in human HepG2 cells as well as human and mouse testes, indicating that exon 4 splicing in SHBG transcription is conserved among mammalian species. To our knowledge, this is the first report of the identification of a SHBG exon 4 splice variant that is translated. Because the SHBG isoform it encodes lacks appreciable steroid-binding activity, it may function beyond that of the widely accepted role of SHBG as a steroid-transport protein. Copyright © 2005 by The Endocrine Society.en_HK
dc.languageengen_HK
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_HK
dc.relation.ispartofEndocrinologyen_HK
dc.rightsEndocrinology. Copyright © The Endocrine Society.en_HK
dc.titleExpression of rabbit sex hormone-binding globulin during pregnancy and prenatal development and identification of a novel isoformen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0013-7227&volume=146&spage=1965&epage=1972&date=2005&atitle=Expression+of+Rabbit+Sex+Hormone-Binding+Globulin+during+Pregnancy+and+Prenatal+Development+and+Identification+of+a+Novel+Isoformen_HK
dc.identifier.emailNg, KM: skykmng@hkucc.hku.hken_HK
dc.identifier.emailLee, WM: hrszlwm@hku.hken_HK
dc.identifier.authorityNg, KM=rp01670en_HK
dc.identifier.authorityLee, WM=rp00728en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1210/en.2004-1173en_HK
dc.identifier.pmid15625245-
dc.identifier.scopuseid_2-s2.0-15444370810en_HK
dc.identifier.hkuros98893en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-15444370810&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume146en_HK
dc.identifier.issue4en_HK
dc.identifier.spage1965en_HK
dc.identifier.epage1972en_HK
dc.identifier.isiWOS:000227667400037-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridNg, KM=25122990200en_HK
dc.identifier.scopusauthoridSo, MT=8748542200en_HK
dc.identifier.scopusauthoridLee, WM=24799156600en_HK

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