Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-06

AUTHORS

Wylie Vale, Jean Rivier, Joan Vaughan, Richard McClintock, Anne Corrigan, Wilson Woo, David Karr, Joachim Spiess

ABSTRACT

A variety of hypophysiotropic peptides or proteins have been reported to be present in mammalian gonads. Inhibin, a hormone that under most circumstances selectively suppresses the secretion of follicle-stimulating hormone (FSH) but not luteinizing hormone (LH), has been isolated from the gonadal fluids of several species1–5 and characterized as a heterodimeric protein consisting of α- and β-polypeptides associated by disulphide bonds. The complete amino-acid sequences of the precursors of porcine6,7 and human7 inhibin α-subunits and two distinct porcine inhibin β-subunits (βA and βB)6 have been deduced from complementary DNA sequences. Gonadotropin releasing peptides have also been found in the gonad and have generally been shown to be active in radioreceptor assays for gonadotropin releasing hormone (GnRH) but to exhibit different chromatographic and immunological characteristics from those of GnRH8–14. During our purification of inhibin from porcine follicular fluid, we noted fractions that could stimulate the secretion of FSH by cultured anterior pituitary cells3. We report here the purification of an FSH releasing protein (FRP) and its characterization by SDS-polyacrylamide gel electrophoresis under non-reducing and reducing conditions and by partial sequence analysis. Our results indicate that porcine gonadal FRP is a homodimer consisting of two inhibin βA-chains linked by disulphide bonds. FRP is highly potent (50% effective concentration (EC50)∼25 pM) in stimulating the secretion and biosynthesis of FSH but not of LH or any other pituitary hormone. In contrast to the effects of GnRH and other reported gonadal gonadotropin releasing fractions, the action of FRP is not mediated by GnRH receptors. More... »

PAGES

776-779

Journal

TITLE

Nature

ISSUE

6072

VOLUME

321

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/321776a0

    DOI

    http://dx.doi.org/10.1038/321776a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1031000060

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/3012369


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    66 gonadal FRP
    67 gonadal fluids
    68 gonadal gonadotropin
    69 gonadotropin
    70 gonads
    71 heterodimeric protein
    72 homodimer consisting
    73 hormone
    74 human7 inhibin α
    75 hypophysiotropic peptides
    76 immunological characteristics
    77 inhibin
    78 inhibin α
    79 inhibin β
    80 mammalian gonads
    81 most circumstances
    82 ovarian follicular fluid
    83 partial sequence analysis
    84 peptides
    85 pituitary cells3
    86 pituitary hormones
    87 polypeptide
    88 porcine follicular fluid
    89 porcine gonadal FRP
    90 porcine inhibin β
    91 porcine ovarian follicular fluid
    92 precursors
    93 protein
    94 purification
    95 purification of inhibin
    96 radioreceptor assay
    97 receptors
    98 results
    99 secretion
    100 secretion of FSH
    101 sequence
    102 sequence analysis
    103 species1–5
    104 subunits
    105 variety
    106 βA
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