title: Gonadotrophin-binding components in porcine follicular fluid.
abstract: The follicular fluid is an important milieu for the growing and maturing oocyte and granulosa cells. In this study we investigated: (1) the properties of gonadotrophin-binding sites in the supernatant fraction of porcine follicular fluid (pFF) and compared them with those of membrane-bound receptors, and (2) the relative changes that occur in pFF and granulosa cell receptor-binding activity following hormone priming of gilts. 125I-Labelled human chorionic gonadotrophin (hCG) and 125I-labelled ovine FSH (oFSH) binding to particulate and supernatant fractions of pFF were hormone-specific and saturable. The concentration of 125I-labelled hCG-binding sites was roughly 50-fold higher in particulate than in supernatant fractions of pFF. However, 30-40% of the total 125I-labelled hCG-binding activity in pFF was present in the supernatant fraction of commercial batches of pFF. 125I-Labelled oFSH binding to pFF membranes was markedly higher than to supernatant fractions. Binding of 125I-labelled hCG and 125I-labelled oFSH to granulosa cells and supernatants of pFF showed a time-dependent variation in response to hormone priming. The results suggest that gonadotrophin-binding sites in the supernatant fraction of pFF have properties similar to those of their membrane-bound counterparts. 125I-Labelled hCG-binding activity in the supernatant fraction of pFF was shown to be more stable than detergent-solubilized LH/hCG receptors, even in glycerol-preserved preparations. Based on a number of criteria, we have speculated that pFF may have components which may be similar in structure to the extracellular domain of the LH/hCG receptor.
authors.affiliation: Reproduction Research Laboratory, Clinical Research Institute of Montreal, Quebec, Canada.
authors.forename: T A
authors.initials: TA
authors.lastname: Yarney
authors.forename: M R
authors.initials: MR
authors.lastname: Sairam
authors.forename: G N
authors.initials: GN
authors.lastname: Bhargavi
authors.forename: B R
authors.initials: BR
authors.lastname: Downey
authors.forename: A
authors.initials: A
authors.lastname: Srikandakumar
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D006063:Chorionic Gonadotropin / Q000378:metabolism; D005260:Female; D005640:Follicle Stimulating Hormone / Q000378:metabolism; D015571:Follicular Fluid / Q000502:physiology*; D006062:Gonadotropins / Q000378:metabolism*; D006107:Granulosa Cells / Q000502:physiology; D007986:Luteinizing Hormone / Q000378:metabolism; D011388:Prolactin / Q000378:metabolism; D011967:Receptors, Gonadotropin / Q000378:metabolism; D012756:Sheep; D013552:Swine
chemical_list: D006063:Chorionic Gonadotropin; D006062:Gonadotropins; D011967:Receptors, Gonadotropin; D011388:Prolactin; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone