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 species and characterized as a heterodimeric protein consisting of alpha- and beta-polypeptides associated by disulphide bonds. The complete amino-acid sequences of the precursors of porcine and human inhibin alpha-subunits and two distinct porcine inhibin beta-subunits (beta A and beta B) 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 GnRH. During our purification of inhibin from porcine follicular fluid, we noted fractions that could stimulate the secretion of FSH by cultured anterior pituitary cells. 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 beta A-chains linked by disulphide bonds. FRP is highly potent (50% effective concentration (EC50) approximately 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.

Amino Acid Sequence↗

PubMedDate not supplied

Importance of FSH-releasing protein and inhibin in erythrodifferentiation.

Inhibin is a hypophysiotropic hormone which selectively suppresses the secretion of pituitary follicle-stimulating hormone. It has been isolated from gonadal fluids and characterized as a protein heterodimer consisting of an alpha subunit and one of two beta subunits (beta A or beta B). FSH-releasing protein (FRP), also named activin, is a dimer consisting of two inhibin beta-chains. A factor from conditioned medium of a leukaemia cell line has been isolated which can induce mouse Friend cells to become benzidine-positive, and which shares a similar N-terminal sequence with porcine FRP. In this report, we find that FRP and inhibin modulate both the induction of haemoglobin accumulation in a human erythroleukaemic cell line, K562, and the proliferation of erythroid progenitor cells in human bone marrow culture. These two proteins could constitute a novel humoral regulatory control of erythropoiesis which would involve two types of related protein dimers with functionally opposite effects.

Activins↗

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Impaired fetal blood gas status in polyhydramnios and its relation to raised amniotic pressure.

A substantial proportion of perinatal losses in polyhydramnios occur as unexplained normally formed stillbirths. In order to investigate the relationship between fetal condition and raised amniotic pressure (AP), fetal blood gas and acid-base status were determined together with AP in 22 pregnancies with polyhydramnios. At fetal blood sampling, 8 (36%) had a venous pH value and 16 (73%) a pO2 value below the reference range. Both fetal pH and pO2 were significantly negatively correlated with the degree of elevation in AP (y = 7.43 - 0.036x, r = 0.56, p = 0.006, where y = pH and x = AP z score, and y = -1.6 - 0.48x, r = 0.54, p = 0.01, where y = pO2 z score, respectively). Although some of these fetuses were hydropic, had congenital anomalies, or were from multiple pregnancies, univariate and multiple logistic regression analyses indicated that the above associations could not be accounted for by these potentially confounding variables. This work suggests that abnormal fetal blood gas status in human pregnancies with poly-hydramnios is associated with elevated AP.

Acid-Base Equilibrium↗

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Potential for pre-implantation determination of human platelet antigen type using DNA amplification: a strategy for prevention of allo-immune thrombocytopenia.

To demonstrate that fetal human platelet antigen (HPA1) type can be determined by amplification from picogram quantities of DNA, nested oligonucleotide DNA primers were designed to amplify a portion of the platelet glycoprotein GpIIIa gene which spans the polymorphic HPA site. Specific oligonucleotides were designed to hybridise either to the amplified HPA1a allele or to the HPA1b allele. DNA dilutions were used as a template and HPA1 type, determined by this method from as little as 2 pg of DNA in 6 cases, was compared to direct typing of blood from the same individuals. In each case nested polymerase chain reaction amplified the specific HPA locus from as little as 2 pg of DNA and determination of HPA1 type agreed with typing of blood.

Antigens, Human Platelet↗

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