Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/23453
Full metadata record
DC FieldValueLanguage
dc.contributor.authorTavoulari, S.en
dc.contributor.authorFrillingos, S.en
dc.contributor.authorKaratza, P.en
dc.contributor.authorMessinis, I. E.en
dc.contributor.authorSeferiadis, K.en
dc.date.accessioned2015-11-24T19:32:47Z-
dc.date.available2015-11-24T19:32:47Z-
dc.identifier.issn0268-1161-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/23453-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectAntibodies/pharmacologyen
dc.subjectCells, Cultureden
dc.subjectFemaleen
dc.subjectFollicle Stimulating Hormone/secretionen
dc.subjectGonadal Hormonesen
dc.subjectHumansen
dc.subjectLuteinizing Hormone/secretionen
dc.subjectMaleen
dc.subjectPeptide Fragments/genetics/immunology/metabolism/*pharmacologyen
dc.subjectPichia/metabolismen
dc.subjectPituitary Gland/cytology/secretionen
dc.subjectProtein Structure, Tertiary/physiologyen
dc.subjectProteins/antagonists & inhibitors/*pharmacologyen
dc.subjectRatsen
dc.subjectRats, Wistaren
dc.subjectRecombinant Proteins/genetics/immunology/metabolism/pharmacologyen
dc.subjectSerum Albumin/genetics/immunology/metabolism/*pharmacologyen
dc.titleThe recombinant subdomain IIIB of human serum albumin displays activity of gonadotrophin surge-attenuating factoren
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1093/humrep/deh187-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/15016777-
heal.identifier.secondaryhttp://humrep.oxfordjournals.org/content/19/4/849.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2004-
heal.abstractBACKGROUND: Gonadotrophin surge-attenuating factor (GnSAF) is an as yet unidentified ovarian factor that acts on the pituitary to attenuate the pre-ovulatory LH surge. In a previous study, GnSAF bioactivity was proposed to derive, at least in part, from a C-terminal domain (95peptide) of human serum albumin (HSA). METHODS AND RESULTS: We employ here the expression-secretion system of Pichia pastoris to produce and assay selected recombinant polypeptides of HSA for GnSAF activity. We show that the C-terminal 95peptide of HSA (residues 490-585; subdomain IIIB) can be expressed from P.pastoris in secreted form and supernatants from clones expressing this polypeptide reduce the GnRH-induced LH secretion of primary rat pituitary cultures by 50-82%. When expressed in the same system, HSA domain III (residues 381-585) or full-length HSA (residues 1-585) are inactive. The bioactive subdomain IIIB is also separable from either domain III or full-length HSA on Blue Sepharose chromatography. CONCLUSIONS: Taken together, the findings highlight the putative importance of HSA subdomain IIIB as a GnSAF-bioactive entity and introduce a unique experimental tool to engineer this molecule for structure-function analysis.en
heal.journalNameHum Reproden
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

Files in This Item:
File Description SizeFormat 
Tavoulari-2004-The recombinant subd.pdf250.35 kBAdobe PDFView/Open    Request a copy


This item is licensed under a Creative Commons License Creative Commons