Inhibin A-subunit cDNAs from porcine ovary and human placenta.

Mayo, Kelly E.; Cerelli, Gail M.; Spiess, Joachim; Rivier, Jean; Rosenfeld, Michael G.; Evans, Ronald M.; Vale, Wylie

doi:10.1073/pnas.83.16.5849

Cited by 203 publications

(67 citation statements)

References 26 publications

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“…The recombinant peptide was structurally identical to natural activin A/EDF, and its biological activity was confirmed in primary cultures of pituitary cells by the promotion of follicle-stimulating hormone secretion as well as by induction of the differentiation of Friend cells (19,20). The amino acid sequence of activin A/EDF is completely conserved among humans, cows, pigs, and rats (9,(21)(22)(23).…”

Section: Methodsmentioning

confidence: 85%

Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis.

Shiozaki

Sakai

Tabuchi

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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Activin A/erythroid differentiation factor (EDF) is a human protein that induces differentiation of a murine erythroleukemia cell (the Friend cell). In this study, we demonstrate that endogenous activin A/EDF activity is present in murine bone marrow and spleen. In addition, this activity is secreted by bone marrow and spleen cells in primary culture. Administration of follistatin (a specific binding protein for activin A/EDF) to mice results in a decrease of erythroid progenitors in the bone marrow and spleen. These findings support the concept that activin A/EDF and follistatin have opposing actions in the regulation of erythropoiesis.

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Section: Methodsmentioning

confidence: 85%

Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis.

Shiozaki

Sakai

Tabuchi

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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“…Normal testis (NT) RNA served as a control. Actin signal is shown at a 100-fold decreased intensity compared with the other signals ActRIIB (Hilden et al, 1994), nucleotides 126-411 for the inhibin a-subunit (Mayo et al, 1986), nucleotides 702-946 for the inhibin PA subunit (Mason et al, 1986), nucleotides 845-1073 for the inhibin PB subunit (Mason et al, 1986) and nucleotides 508-819 for the follistatin transcript (Shimasaki et al, 1988 Figure IA); transcription levels were quantified and expressed relative to gamma actin (Figure 2). All four activin receptors were detected in seminomas, non-seminomas and spermatocytic seminomas.…”

Section: Rt-pcrmentioning

confidence: 99%

“…Human ActRIIA (nucleotides 132-791; Donaldson et al, 1992) and inhibin f.A subunit (nucleotides 309-946; Mason et al, 1986) cDNAs were cloned from K562 cells; ActRIIB (nucleotides 429-947; Hilden et al, 1994) and inhibin 1B subunit (nucleotides 263-1073; Mason et al, 1986) cDNAs were cloned from human testis. The inhibin ax-subunit cDNA (nucleotides 125-411;Mayo et al, 1986) was cloned from genomic DNA, and follistatin cDNA (nucleotides 345-819; Shimasaki et al, 1988) was cloned from placental RNA.…”

Section: Rt-pcrmentioning

confidence: 99%

Human testicular germ cell tumours express inhibin subunits, activin receptors and follistatin mRNAs

Schaik

Wierikx²,

Looijenga³

et al. 1997

Br J Cancer

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Summary Germ cell development is influenced by activin and inhibin, which are produced by Sertoli cells. Activin also affects differentiation of mouse embryonal carcinoma cells, which, to a certain extent, resemble the embryonal carcinoma component of germ cell tumours. Therefore, the expression of inhibin/activin subunits, of activin receptors and of the activin-binding protein follistatin was studied in testicular germ cell tumours, using RNAase protection assays. Testicular germ cell tumours of adolescents and adults (TGCTs) and spermatocytic seminomas expressed activin type and type 11 receptors (ActRi and ActRII respectively). Seminomas expressed significantly lower levels of ActRIIA (P<0.05, Mann-Whitney U-test) and higher levels of ActRIA (P<0.05) and ActRIB (P<0.05) compared with non-seminomas. All tumours expressed inhibin n-subunit transcripts, which are a prerequisite for activin synthesis. Non-seminomas contained significantly higher levels of the inhibin PA subunit (P<0.001) compared with seminomas. No activin PC subunit transcripts could be demonstrated by RNAase protection. Inhibin a-subunit expression was absent in the spermatocytic seminomas, in six out of nine seminomas and in 10 out of 11 nonseminomas. Follistatin was expressed predominantly in non-seminomas and spermatocytic seminomas. This expression of activin type and type 11 receptors in combination with expression of inhibin 5-subunits indicates that activin may act as a para-or autocrine factor in the regulation of growth and differentiation of tumours of human germ cells.

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“…Other studies have deduced even more complex structures for inhibin-like protein(s) from ovarian sources based on cDNA sequences (9)(10)(11). It is apparent that in the female, besides the ovary, the placenta also has the mRNA for at least one of the chains of human ovarian inhibin protein(s) (12). These reports serve to illustrate the molecular diversity of peptides/proteins that may influence gonadotropin secretion.…”

mentioning

confidence: 99%

Synthetic peptide with inhibin-like activity preferentially inhibits follitropin secretion in comparison with lutropin-releasing hormone antagonists.

Sairam¹,

Ramasharma²,

Li³

1987

Proc. Natl. Acad. Sci. U.S.A.

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Biological activity of a synthetic peptide with inhibin-like activity under in vitro and in vivo conditions was compared with three highly potent synthetic lutropin-releasing hormone antagonists. Unlike the synthetic lutropin-releasing hormone antagonists, which effectively inhibited both lutropin and follitropin secretion from the pituitary, the inhibin-like peptide showed a preferential effect by inhibiting follitropin release both in vitro and in vivo. Thus, small peptides such as inhibin-like peptide with a sequence unrelated to lutropinreleasing hormone may provide a basis for design of selective inhibitors of gonadotropin release.Inhibin is a gonadal protein or peptide with the ability to selectively inhibit the secretion of follicle-stimulating hormone (FSH) from the pituitary in various assay systems (1, 2). Advances have been made describing the structures of various molecules with inhibin-like activity. We have reported the isolation, structure, and synthesis of a 31-amino acid peptide with inhibin-like activity (ILP) (3). Subsequently, it was shown to originate from larger molecules (4). Another polypeptide from the same source, though of a different structure, was also reported to exhibit a similar activity (5). Several bull seminal plasma proteins (6-8) with a high degree of homology to fibronectins (8), also inhibit gonadotropin release from the pituitary. Other studies have deduced even more complex structures for inhibin-like protein(s) from ovarian sources based on cDNA sequences (9-11). It is apparent that in the female, besides the ovary, the placenta also has the mRNA for at least one of the chains of human ovarian inhibin protein(s) (12). These reports serve to illustrate the molecular diversity of peptides/proteins that may influence gonadotropin secretion.Lutropin-releasing hormone (LHRH), a decapeptide of hypothalamic origin (13), which arises from a larger precursor, releases both lutropin (LH) and FSH from the pituitary. Since the discovery of the structure of LHRH, more than a thousand analogs (14, 15) displaying potent agonistic or antagonistic activities have been chemically synthesized in the hope of providing new potential approaches to the control of mammalian fertility and the treatment of infertility as well as for therapeutic use in controlling certain types of cancer (16). However, due to the intrinsic LH-and FSH-releasing ability of the decapeptide, there has been no success in producing antagonistic analogs that selectively inhibit LH or FSH release. The object of this investigation was to demonstrate that, under certain in vitro and in vivo conditions, the synthetic ILP could selectively inhibit FSH release while all three LHRH antagonists, which were included for comparison, inhibited the release of both FSH and LH. MATERIALS AND METHODSILP was chemically synthesized as described (17). The synthetic LHRH analogs (Table 1) were kindly supplied by D. H. Coy.In Vitro Incubation Procedure. Male Swiss albino mice of the Hauska strain were obtained when they were 16 days...

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Inhibin A-subunit cDNAs from porcine ovary and human placenta.

Cited by 203 publications

References 26 publications

Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis.

Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis.

Human testicular germ cell tumours express inhibin subunits, activin receptors and follistatin mRNAs

Synthetic peptide with inhibin-like activity preferentially inhibits follitropin secretion in comparison with lutropin-releasing hormone antagonists.

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