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Hum. Reprod. Advance Access originally published online on March 11, 2004
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Human Reproduction, Vol. 19, No. 4, 849-858, April 2004
© 2004 European Society of Human Reproduction and Embryology

The recombinant subdomain IIIB of human serum albumin displays activity of gonadotrophin surge-attenuating factor

Sotiria Tavoulari1, Stathis Frillingos1,3, Panayiota Karatza1, Ioannis E. Messinis2 and Konstantin Seferiadis1

1 Laboratory of Biological Chemistry, University of Ioannina Medical School, Ioannina 45110 and 2 Department of Obstetrics and Gynecology, University of Thessalia Medical School, Larissa 41222, Greece

3 To whom correspondence should be addressed. e-mail: efriligo{at}cc.uoi.gr

BACKGROUND: 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.

Key words: albumin/GnRH/GnSAF/LH/Pichia pastoris


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