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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A cDNA probe for the beta subunit of bovine FSH (FSH-beta) detects multiple restriction fragment length polymorphisms (RFLPs) in sheep genomic DNA consistent with an insertion/deletion polymorphism around the FSH-beta locus. The presence of the insertion/deletion was confirmed by screening over 100 individuals with two restriction enzymes detecting RFLPs. All individuals showed the same patterns of fragments with both enzymes. A partial restriction map of the FSH-beta gene in sheep suggests that the insertion/deletion is approximately 2 kb in size and located downstream from the third exon. Individual DNA samples were analysed from two flocks where the Booroola F gene is known to be segregating. Individuals that were heterozygous for the F gene were shown to be homozygous for one or other of the two alleles. Genetic recombination between the FSH-beta locus and the F gene was observed in four pedigrees and there was no evidence that the insertion/deletion is closely linked genetically to the Booroola F gene. A major gene transcript of 2.2-2.3 kb was detected on Northern blots of sheep RNA. Neither the insertion/deletion polymorphism nor the presence of the F gene appeared to influence the size of the FSH-beta gene transcript.
J Mol Endocrinol 1990 Oct
PMID:The Booroola F gene mutation in sheep is not located close to the FSH-beta gene. 197 99

The mode of action of activin A on the anterior pituitary gland (AP) was investigated using primary cultured cells. The AP cells were cultured with activin A (1 ng/ml) at various cell densities for 24-96 h, and further incubated for 3 h with activin A-free medium. When the cells were pretreated with activin A for 48 h, follicle-stimulating hormone (FSH) secretion during the following 3-h incubation was increased only at a density of 1 x 10(5) cells/200 mm2, but not at 2 x 10(5) or 4 x 10(5) cells/200 mm2. A longer pretreatment (96 h) was required in order to induce this response at a density of 2 x 10(5) cells/200 mm2. Luteinizing hormone (LH) secretion was not affected by activin A. Thus, the FSH secretory activity of the primary culture of AP was stimulated by activin A in a cell density-dependent manner. Furthermore, it was found that treatment with activin A (10 ng/ml) for 72 h increased the number of immunoreactive FSH cells by 25-41%, and that these newly induced FSH cells were low responders to gonadotropin-releasing hormone stimulation. The proportions of immunoreactive LH, thyroid-stimulating hormone, prolactin or growth hormone cells were not affected. From these results, we conclude that activin A increases FSH secretion by changing the cell population of pituitary gonadotropes.
Mol Cell Endocrinol 1990 Mar 05
PMID:Activin A increases the number of follicle-stimulating hormone cells in anterior pituitary cultures. 210 11

Conditioned medium of cultured Sertoli cells from 21-day-old rats was used as starting material for the isolation of inhibin. Inhibin activity was monitored by the dose dependent suppression of the follicle-stimulating hormone release of cultured rat pituitary cells. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis of the highly purified inhibin preparation revealed a 32 kDa protein after silver staining, which could be separated in subunits of 18 kDa and 12 kDa after reduction. Western blot analysis with an antibody recognizing the 22 N-terminal amino acids of the alpha-subunit of 32 kDa bovine inhibin confirmed the presence of a 32 kDa inhibin molecule under non-reducing conditions, whereas an 18 kDa alpha-subunit was found after reduction. An antibody recognizing the beta-A subunit of inhibin did not yield a signal after Western blotting. N-terminal amino acid sequence analysis of two highly purified preparations of inhibin obtained using different methods yielded the sequence predicted for a 32 kDa alpha beta-B dimer on basis of cDNA nucleotide sequence. This result is in agreement with the large excess of beta-B over beta-A mRNA in the rat testis.
Mol Cell Endocrinol 1990 Mar 26
PMID:Inhibin in immature rat Sertoli cell conditioned medium: a 32 kDa alpha beta-B dimer. 211 Dec 53

There are significant differences between rats and mice in the gonadal regulation of several aspects of gonadotroph function. To investigate whether these extend to the pretranslational regulation of FSH synthesis by gonadal steroids, we have measured FSH-beta mRNA levels following gonadectomy and sex-steroid replacement and have related these to serum and pituitary FSH as a reflection of overall hormone synthesis. In ovariectomized rats, FSH-beta mRNA levels increased by 8 h, decreased, and then rose progressively over the next 28 days. A similar pattern of response was observed in orchidectomized rats. In mice, there were progressive increases in FSH-beta mRNA levels in both males and females following gonadectomy, without evidence of the early peaks observed in rats. In both species, the change in FSH-beta mRNA levels after gonadectomy was greater in females than in males. These changes in FSH-beta mRNA following gonadectomy were paralleled by changes in the serum FSH concentration. In ovariectomized female rats and mice, pituitary FSH stores increased by 8 h and 3 days respectively, whereas in male rats, pituitary FSH content did not rise until 10 days after orchidectomy. The most striking species difference was the marked and prolonged reduction of pituitary FSH after orchidectomy of mice. Treatment of rats and mice from the time of ovariectomy, with a dose of oestradiol that prevents increases in serum LH, only partially attenuated the rises in FSH-beta mRNA and serum FSH and did not prevent the increase in pituitary FSH content. Treatment of intact or orchidectomized rats with testosterone suppressed FSH-beta mRNA levels to 50% below intact control values without affecting pituitary FSH content.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Endocrinol 1990 Apr
PMID:Comparison of the pretranslational regulation of FSH synthesis by gonadal steroids in rats and mice. 211 6

Electroejaculate traits and circulating follicle-stimulating hormone (FSH), luteinizing hormone (LH), and testosterone concentrations were analyzed in adult leopard cats (Felis bengalensis), a rare felid species indigenous to east Asia. The ability of leopard cat sperm to bind and penetrate zona-free hamster ova and zona-intact domestic cat oocytes in vitro was examined as a means of testing sperm function. The influence of culture media [Biggers, Whitten, Whittingham (BWW) vs. modified Krebs Ringer bicarbonate (mKRB)], seminal plasma removal, and swim-up separation on sperm motility, sperm morphology, and oocyte penetration also were assessed. Sperm treatments included dilution of raw semen (DR), ejaculate centrifugation, and either resuspension (NS) or swim-up processing (SU). The percentage of oocytes penetrated (penetration rate) and the number of penetrated sperm/oocyte (penetration index) were determined. Ejaculates from each male consisted of at least a 50% sperm motility rating, and hormone concentrations in individual males were unrelated to any ejaculate trait measured concurrently on the same day. The SU technique improved (P less than 0.05) percent sperm motility and the proportion of structurally normal sperm compared to DR and NS treatments. Leopard cat spermatozoa were capable of binding to and penetrating hamster ova and domestic cat oocytes; however, penetration was influenced by culture medium and seminal processing. In the hamster assay, a higher (P less than 0.05) penetration rate and penetration index were achieved when mKRB was used for gamete incubation instead of BWW. NS processing also increased (P less than 0.05) overall penetration compared to DR and SU. In the cat oocyte assay, zona penetration rate was similar (P greater than 0.05) in the DR, NS, and SU aliquots; however, the zona penetration index was increased (P less than 0.05) by the NS compared to the DR and SU treatments. This study 1) provides baseline ejaculate and endocrine norms for the leopard cat, 2) demonstrates that leopard cat sperm undergo nuclear decondensation in hamster ova and penetrate zona-intact domestic cat oocytes, 3) indicates that seminal plasma removal enhances leopard cat sperm fertilizing ability and ovum penetration, and 4) suggests that heterologous oocyte penetration is effective for assessing factors influencing fertilization and sperm function in this nondomestic felid.
Mol Reprod Dev 1990 Jun
PMID:Ejaculate-hormonal traits in the leopard cat (Felis bengalensis) and sperm function as measured by in vitro penetration of zona-free hamster ova and zona-intact domestic cat oocytes. 211 44

The hypothesis has been advanced that Sertoli cells produce one or more follicle-stimulating hormone (FSH)-dependent paracrine factors which stimulate Leydig cell maturation and steroidogenesis. In an attempt to identify these factors we studied the effect of coculture with Sertoli cells on the steroidogenic capacity of immature Leydig cells. It is demonstrated that coculture, during a period of 6 days, markedly increases the capacity of the Leydig cells to secrete C21-steroids (progesterone, 17 alpha-hydroxyprogesterone, 20 alpha-hydroxypregn-4-en-3-one) and C19-steroids (testosterone, androst-4-ene-3,17-dione) in response to stimulation with luteinizing hormone (LH). Pretreatment of the cocultures on days 4, 5 and 6 with low concentrations of gonadotropins further enhances the steroidogenic response to LH. This pretreatment results in an overall increase in steroid output. At low concentrations of Sertoli cells and when short incubation times are used, pretreatment with FSH is clearly more effective than pretreatment with LH. Pretreatment with gonadotropins also results in a disproportionate increase in C19 output caused by increased conversion of C21 precursors into C19-steroids. This effect is also observed in Leydig cell monocultures and is mainly due to LH action on Leydig cells. Finally pretreated cocultures display a selective increase in testosterone output. The latter effect is caused by FSH-dependent conversion of androstenedione into testosterone in Sertoli cells. Pretreated cocultures can be maintained for at least 28 days. During this entire period their basal steroid output increases. Using a two-chamber culture system it is demonstrated that direct cell-cell interactions are not required to observe the stimulatory effects of coculture. One or more diffusible factors are involved and continuous contact with these factors is required to maintain the effect. Immunoneutralization experiments using an insulin-like growth factor (IGF-I) antiserum show that IGF-I is an important permissive factor to maintain steroidogenesis in isolated Leydig cells and in cocultures. Under none of the conditions studied, however, does the antiserum neutralize the stimulatory effect of coculture. It is concluded that the stimulatory effects of coculture on the testosterone output of Leydig cells are complex and that important diffusible mediators still remain to be identified.
Mol Cell Endocrinol 1990 Jul 09
PMID:Influence of coculture with Sertoli cells on steroidogenesis in immature rat Leydig cells. 212 92

Fully grown germinal vesicle-stage oocytes are induced to resume meiosis and acquire the capacity to undergo fertilization in response to a surge of gonadotropins. The present study examined possible direct and indirect roles of gonadotropins in the maturation and fertilization of rat oocytes by determining 1) the effect of exogenous administration of gonadotropins (priming) to immature rats prior to oocyte collection on the capacity of oocytes to undergo maturation and fertilization in vitro, 2) the effect of follicle-stimulating hormone (FSH) in the maturation media on the resumption of meiosis and subsequent capacity of oocytes to undergo fertilization, and 3) the capacity of oocytes to undergo maturation and fertilization following culture in preovulatory follicular fluid or in conditioned media obtained from gonadotropin-stimulated granulosa cell (GC) cultures. In the first experiment, oocytes from unprimed rats underwent spontaneous meiotic maturation in vitro and 17% underwent subsequent fertilization. Priming increased the proportion of oocytes undergoing fertilization. Maturation of oocytes in media supplemented with various concentrations of FSH or for various lengths of time (6-16 h) in medium with 500 ng FSH/ml indicated that FSH slowed the rate of meiotic maturation, but had no effect on the capacity of the oocytes to be fertilized. Oocytes obtained from primed animals and cultured in the presence of preovulatory follicular fluid were fertilized in proportions similar to those cultured in serum-containing medium. In the third experiment, medium conditioned by FSH-stimulated GC for 40 h slowed the rate of meiotic maturation; the addition of luteinizing hormone (LH) to the FSH-stimulated cells produced a medium in which the rate of oocyte maturation was not different from that of control oocytes (in medium from unstimulated cells). Medium conditioned by FSH- or LH-stimulated GC, but not fibroblasts, increased the proportions of oocytes undergoing fertilization following maturation in those media. FSH + LH stimulation of GC increased the fertilization of oocytes to proportions significantly higher than with either gonadotropin alone. These data suggest that GC respond to gonadotropin stimulation by providing a factor(s) that regulates the rate of oocyte maturation and promotes the capacity of oocytes to undergo fertilization.
Mol Reprod Dev 1990 Aug
PMID:Effects of gonadotropins and granulosa cell secretions on the maturation and fertilization of rat oocytes in vitro. 212 Nov 69

Immature female rats (23-30 days old) were implanted subcutaneously with diethylstilbestrol (DES) in silastic capsules. After 48 h their ovaries were removed and the granulosa cells isolated (Foreman et al. (1984) Life Sci. 35, 1273-1279). The cells were incubated in Hepes balanced saline buffer with substrates with or without follicle-stimulating hormone (FSH). At the end of incubation perchloric acid extracts were made for 31P NMR spectroscopy. The resonances of fructose 1-phosphate, fructose 6-phosphate, glucose 1-phosphate, and ribose 5-phosphate were identified in the granulosa cell extracts. The relative intensities of fructose 6-phosphate to ribose 5-phosphate decreased after incubation with FSH in vitro. This suggests that FSH increases the activity of the pentose pathway within 1 h. Thus, FSH can acutely activate those metabolic pathways which provide nicotinamide-adenine dinucleotide phosphate (NADPH) to be used in steroid synthesis and cholesterol mobilization.
Mol Cell Endocrinol 1990 Oct 22
PMID:31P nuclear magnetic resonance (NMR) identification of sugar phosphates in isolated rat ovarian follicular granulosa cells and the effects of follicle-stimulating hormone. 212 82

The present study was carried out to examine the role of protein synthesis in mouse oocyte maturation in vitro. In the first part of this study, the effects of cycloheximide (CX) were tested on spontaneous meiotic maturation when oocytes were cultured in inhibitor-free medium. CX reversibly suppressed maturation of oocytes as long as maturation was either initially prevented by the phosphodiesterase inhibitor, 3-isobutyl-1-methyl-xanthine (IBMX), or delayed by follicle-stimulating hormone (FSH). In the second part of this study, the actions of protein synthesis inhibitors were tested on hormone-induced maturation. CEO were maintained in meiotic arrest for 21-22 h with hypoxanthine, and germinal vesicle breakdown (GVB) was induced with follicle-stimulating hormone (FSH). Three different protein synthesis inhibitors [CX, emetine (EM), and puromycin (PUR)] each prevented the stimulatory action of FSH on GVB in a dose-dependent fashion. This was accompanied by a dose-dependent suppression of 3H-leucine incorporation by oocyte-cumulus cell complexes. The action of these inhibitors on FSH- and epidermal growth factor (EGF)-induced GVB was next compared. All three drugs lowered the frequency of GVB in the FSH-treated groups, below even that of the controls (drug + hypoxanthine); the drugs maintained meiotic arrest at the control frequencies in the EGF-treated groups. Puromycin aminonucleoside, an analog of PUR with no inhibitory action on protein synthesis, had no effect. The three inhibitors also suppressed the stimulatory action of FSH on oocyte maturation when meiotic arrest was maintained with the cAMP analog, dbcAMP.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Reprod Dev 1990 Nov
PMID:Protein synthesis inhibitors prevent both spontaneous and hormone-dependent maturation of isolated mouse oocytes. 212 75

The medium of cultured Sertoli cells from immature rat testes contains 29 and 32 kDa proteins, which are recognized by an antiserum against the 22 N-terminal amino acids of the inhibin alpha-subunit. These proteins were detected by immunoprecipitation of labelled proteins after incubation of Sertoli cells with [35S]methionine, and by Western blotting. The amount of the 32 kDa protein was not affected by the addition of follicle-stimulating hormone (FSH) to the culture medium of the Sertoli cells, whereas FSH induced a large increase of the amount of the 29 kDa protein. Finally, the 29 and 32 kDa proteins in the medium from control and FSH-stimulated Sertoli cells were separated by sodium dodecyl sulfate-polyacrylamide electrophoresis, and inhibin bio- and immunoactivity were determined in eluates of the slices of the gel. Equal amounts of bioactivity were found in control and FSH-stimulated samples at 32 kDa, while the amount of immunoactivity at 29 kDa was increased; no bioactivity was detected in the eluates of these slices. It is concluded that FSH stimulates the secretion of a 29 kDa inhibin-like protein, which does not contain inhibin bioactivity. This indicates that results of experiments, in which antibodies against N-terminal peptides of the inhibin alpha-subunit are used to detect inhibin, do not necessarily reflect the amount of bioactive inhibin produced.
Mol Cell Endocrinol 1990 Dec 03
PMID:Follicle-stimulating hormone-stimulated secretion of an immunoreactive 29 kDa inhibin alpha-subunit complex, but not of 32 kDa bioactive inhibin, from cultured immature rat Sertoli cells. 212 27


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