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PubMed1995

Cloning of the mouse gonadotropin beta-subunit-encoding genes, I. Structure of the follicle-stimulating hormone beta-subunit-encoding gene.

More than 16kb of genomic sequence encompassing the mouse follicle-stimulating hormone beta subunit (FSH beta)-encoding gene was isolated from a 129SvEv mouse genomic library. Comparisons of the nucleotide and deduced amino-acid sequences to the FSH beta sequences of other mammalian species confirm an evolutionarily conserved role of this important protein in reproduction.

Amino Acid Sequence↗
PubMed1993

Transcription rate of the follicle stimulating hormone (FSH) beta subunit gene is reduced by inhibin in sheep but this does not fully explain the decrease in mRNA.

Studies were conducted in vitro and in vivo to determine whether or not inhibin affects the transcription rate of the gene for the beta subunit of follicle stimulating hormone (FSH beta). Pituitary cells in primary culture were incubated with 0-3000 milli-units/ml inhibin; a dose-related decrement in mRNA was obtained but a parallel effect was not observed for the transcription rate of the FSH beta gene in a nuclear run-on experiment. To determine effects in vivo, ovariectomized ewes were treated with saline (group 1), 75 micrograms inhibin 6 h before slaughter (group 2), inhibin 6 h and 12 h before slaughter (group 3) or inhibin 12 h before slaughter (group 4). In samples taken each 2 h, plasma FSH levels were seen to be maximally reduced 6 h after a single injection of inhibin; at this time mRNA levels were reduced up to 100% whereas FSH beta gene transcription rate was reduced by 50%. A second injection at 6 h (group 3) caused a further reduction in plasma FSH levels with no additional effect on transcription rate. In those sheep killed 12 h after a single inhibin injection, transcription rate for the FSH beta gene, cytoplasmic mRNA levels and plasma FSH concentrations had recovered. These studies show that the rapid effect of inhibin on FSH beta mRNA levels may be due, in part, to an effect on transcription rate of the FSH beta gene. An additional mechanism is required, however, to fully explain the inhibin effect on FSH beta mRNA levels.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1988

Nucleotide sequence of the bovine gene for follicle-stimulating hormone beta-subunit.

The gene for the beta-subunit of follicle-stimulating hormone (FSH-beta) was isolated from a library of bovine DNA fragments cloned in bacteriophage gamma and the complete nucleotide sequence of the gene was determined. The bovine FSH-beta gene contains approximately 4000 nucleotides and consists of three exons separated by two intervening sequences. The transcription initiation site of the gene was mapped by nuclease protection experiments. Analysis of RNA species present in pituitary mRNA demonstrated the presence of a 4.0-kb RNA containing FSH-beta sequences, which is the appropriate size for the primary transcript of the gene. Comparison of nucleotide sequence of the 5'-flanking sequence of the FSH-beta gene to the 5'-flanking regions of other pituitary glycoprotein hormone genes reveals little sequence similarity.

Amino Acid Sequence↗
PubMed2004

Processing of O-linked glycosylation in the chimera consisting of alpha-subunit and carboxyl-terminal peptide of the human chorionic gonadotropin beta-subunit is affected by dimer formation with follicle-stimulating hormone beta-subunit.

hCG, LH, FSH, and TSH are a family of heterodimeric glycoprotein hormones that contain a common alpha-subunit, but differ in their hormone-specific beta-subunits. hCGbeta is unique among beta-subunits due to a carboxyl-terminal peptide (CTP) bearing four O-linked oligosaccharides. We previously reported that there were differences in O-glycosylation between two chimeras consisting of alpha-subunit and CTP, i.e. a variant with CTP at the N-terminal region (Calpha) and another analog with CTP at the C-terminus (alphaC) of the alpha-subunit. To address whether O-glycosylation is influenced by the heterodimer formation, Calpha and alphaC were expressed alone or with FSHbeta-subunit in Chinese hamster ovary cells. The O-linked glycosylation was assessed by continuous labeling with [(35)S]methionine/cysteine, immunoprecipitation with anti-alpha or anti-FSH serum, serial digestion with endoglycosidase-F and neuraminidase, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The decrease in molecular weight of dimeric chimeras digested with endoglycosidase-F was greater in Calpha than that in alphaC after treatment with neuraminidase, revealing that both chimeras have different numbers of sialic acids on O-linked carbohydrates. By treating with endoglycosidase-F, the dimeric alphaC migrated faster than its free form, whereas the mobility difference between assembled and unassembled forms of Calpha was very little. These data indicate that processing of O-glycosylation is affected by the backbone polypeptide chain(s).

Animals↗
PubMed1999

Multiple binding sites for nuclear proteins of the anterior pituitary are located in the 5'-flanking region of the porcine follicle-stimulating hormone (FSH) beta-subunit gene.

Gonadotropins, follicle-stimulating hormone (FSH), and luteinizing hormone (LH), are synthesized specifically in the gonadotropes of the anterior pituitary. The aim of this study was to investigate nuclear factors that bind specifically to the porcine FSH beta-subunit gene. We examined nuclear protein binding to 2.75 kilobase pairs (kbp) of DNA adjacent to the porcine FSH beta-subunit gene: about 2.32 kbp of upstream DNA and 0.43 kbp of downstream DNA. The upstream region contains only TATA box, CACCC element, and some imperfect sequences of cAMP-responsive element, activator protein-1 binding site, and activator protein-2 binding site. Gel mobility shift assay using nuclear proteins extracted from the porcine anterior pituitary revealed that the proteins bound to a limited region of DNA, 107 bp long (designated as Fd2), located about -800 bp upstream from the transcription initiation site. Competitive binding assays demonstrated that the protein binding was sequence specific; the addition of excess amounts of several putative regulatory sequences and plasmid (non-homologous) DNA fragments did not reduce the binding. Furthermore, all five subfragments of Fd2 were also bound by the pituitary nuclear proteins, showing that the entire region of Fd2 is involved in this interaction. Southwestern blotting demonstrated that at least seven protein species of 110, 98, 78, 63, 52, 42, and 35 kDa recognize Fd2. Nuclear proteins from several other porcine tissues were also able to bind to the Fd2 fragment but the gel shift patterns were different and the bindings were weak, although only the cerebellum showed a pattern of binding that was similar to that of the anterior pituitary. These data suggest that multiple proteins of the anterior pituitary recognize a specific region of the porcine FSH beta-subunit gene.

5' Untranslated Regions↗
PubMed1976

Amino acid sequence of the beta subunit of follicle-stimulating hormone from human pituitary glands.

The beta subunit of follicle-stimulating hormone (FSH-beta) from human pituitary glands was reduced and S-aminoethylated prior to thermolytic, tryptic, and chymotryptic digestions. Each digest was gel-filtered on Sephadex G-50 to seperate the glycopeptides. The glycopeptides and the peptides were isolated by high voltage paper electrophoresis at pH 6, 3.5, and 2.0. The purity of the isolated peptides was confirmed by amino acid analyses. The amino acid sequences of peptides were determined by Edman degradation followed by subtractive amino acid analysis and, in certain cases, confirmed by dansylation. COOH-terminal sequences of the peptides were determined by digestion with carboxypeptidases A and B and by hydrazinolysis. The tryptophan content of human follicle-stimulating hormone, of the beta subunit of human follicle-stimulating hormone, and of the glycopeptides obtained from the enzymic digests was determined by fluorescence spectra, titration against N-bromosuccinimide, colorimetric estimation with p-dimethyl aminobenzaldehyde, hydrolysis with methane sulfonic acid containing 0.2% tryptamine followed by amino acid analysis, microbiological assay, and sequence analysis. The presence of 1 tryptophan residue in the beta subunit was indicated.

Amino Acid Sequence↗
PubMed1991

Localization of the beta-subunit of follicle stimulating hormone in cattle and sheep by in situ hybridization.

The locus for the beta-subunit of the follicle stimulating hormone gene (FSHB) has been determined in both cattle and sheep by in situ hybridization of a bovine and an ovine cDNA probe, respectively, to metaphase chromosomes. Our results show that the FSHB locus is on cattle chromosome 15 in the region of bands q24-qter and in sheep on the cytogenetically homologous chromosome 15, also in the region q24-qter. The mapping of the FSHB gene in cattle together with the location of other genes (CAT, HBB and PTH) previously found to be syntenic in cattle and on human chromosome 11p, defines an evolutionarily conserved synteny. The localization of the FSHB gene to a cytogenetically homologous region in cattle and sheep is consistent with the hypothesis of extensively conserved chromosome structure in these two species.

Animals↗
PubMed1987

DNA sequence and regional assignment of the human follicle-stimulating hormone beta-subunit gene to the short arm of human chromosome 11.

A human genomic DNA fragment in phage lambda containing FSHB, the gene for the beta-subunit of human follicle-stimulating hormone (FSH-beta), was analyzed and the nucleotide sequence of the region of the clone encoding FSH-beta was determined. A subclone of the lambda phage containing 67% of FSH-beta coding sequence was used as hybridization probe to determine the human chromosomal location of FSHB. A panel of mouse-human somatic cell hybrids containing reduced numbers of human chromosomes was screened with the FSHB probe; complete cosegregation of FSHB with human chromosome 11 was observed in all 26 cell hybrids tested. Analysis of a set of cell hybrids containing translocated derivatives of chromosome 11 further localized FSHB to the human chromosome region 11p11.2----11pter. A Hind III restriction fragment length polymorphism (RFLP) detected by another subclone of the lambda phage containing FSHB now provides a genetic marker for this region of the human genome.

Amino Acid Sequence↗
PubMed1988

Cloning and DNA sequence analysis of the cDNA for the precursor of porcine follicle stimulating hormone (FSH) beta subunit.

A cDNA library of porcine anterior pituitary was constructed in an expression vector lambda gt11. The cDNAs encoding the porcine follicle stimulating hormone (pFSH) beta subunit were obtained using anti-human FSH beta antiserum or synthetic oligonucleotide. The nucleotide sequence of the pFSH beta subunit cDNA clone (929 base) has been determined. The cDNA contained a part of the signal sequence (six amino acids) and the whole amino acid sequence of the mature molecule (109 amino acids). The predicted protein sequence was different from that of the amino acid sequence analysis in ten residues and had an extended carboxyl terminus. Northern analysis showed that the length of the pFSH greater than subunit mRNA was about 1.8 kb.

Amino Acid Sequence↗
PubMed2004

Mapping of a discontinuous and highly conformational binding site on follicle stimulating hormone subunit-beta (FSH-beta) using domain Scan and Matrix Scan technology.

This paper describes the application of two novel screening technologies, i.e. Domain Scan (24- and 30-mer peptides) and Matrix Scan (24-mer peptides) technology, in the mapping of a discontinuous epitope on FSH-beta for a series of 20 monoclonal antibodies. 11 out of 20 mAb's, mapping of which was not successful by conventional Pepscan technology (12-mer peptides), showed selective binding to peptide-constructs corresponding to the beta3-loop of FSH in the Domain and/or Matrix Scan. Systematic replacement analysis studies with peptide-construct 57VYETVRVPGCAC-SAc-ADSLYTYPVATQ81 revealed that for most mAb's the amino acids R62, A70, D71, and L73 form the core of the epitope. A Domain Scan performed in the C-O format showed highly selective binding for mAb's 1 and 2 with only three beta1-beta3 peptide-constructs covering the residues 60TVRVPGCAHHADSLY74 in combination with 10IAIEKEECRFAI21, while for mAb 10 binding was observed with peptide-constructs containing the C-terminal residues 97RGLGPSYCSFGEMKE114 in combination with the residues 10IAIEKEECRFAI21. A Matrix Scan of mAb 17 showed that peptides from four different regions on FSH (1st strand beta3-loop, alpha 1-loop, long alpha2-loop, det. loop) showed enhanced binding in combination with several 70ADSL73-containing peptides. BIACORE measurements with mAb's 1, 2, 13, and 17 using a set of 21 different peptide(-construct)s partially confirmed the Domain and Matrix Scan screening results. Only 24- and 33-mer peptides covering both the 1st and 2nd strand of the beta3-loop showed measurable binding. Cyclic beta3-loop peptide mimics were found to bind significantly stronger (Kd approximately 5 microM) than the lineair analogues, in agreement with the fact that the discontinuous epitope is part of a loop structure. Coupling of the lineair beta1-peptide 1oIAIEKEECRFAI21 to the linear beta3-peptide *52TFKELVYETVRVPGCAHHADSLYTYPVATQAH83# via disulfide bond formation showed a 2-3 fold increase in Kd, thus conforming participation of the beta 1-loop in antibody binding for these mAb's.

Amino Acid Sequence↗
PubMed2006

Sequence analysis of cDNA encoding rabbit follicle-stimulating hormone beta-subunit precursor protein.

To understand the molecular basis of the rabbit's efficient superovulation, we determined the cDNA sequence of the follicle-stimulating hormone (FSH) beta-subunit precursor protein using a combination of 5'- and 3'-rapid amplification of cDNA ends (RACE) with pituitary cDNA libraries of the Japanese White rabbit and compared it with those of other mammals. RACE experiments detected at least three transcripts for the FSHbeta precursor protein in the libraries. The transcripts had lengths of 457, 1,621, and 1,767 bp, from the 5'-end to the poly(A) site. The shortest and mid-length transcripts had the putative polyadenylation signal sequence AATAAA at nucleotides 436 and 1,601, respectively, whereas the longest form had an ATTAAA sequence at nucleotide 1,745 of the cDNA sequence. These transcripts are likely to be polyadenylation variants of one large transcript because they share the same coding sequence for the precursor protein (130 amino acid residues in length). However, only a few shortest variants seem to be formed because the shortest variants were not detected by Northern blot analysis. Phylogenetic analysis of the deduced amino acid sequence indicates that the rabbit is phylogenetically closer to humans than to the other mammals, suggesting that an FSH preparation from human sources would be superior as a follicle stimulant for the induction of superovulation.

Amino Acid Sequence↗
PubMed2004

Gonadotroph heterogeneity, density and distribution, and gonadotroph-lactotroph associations in the pars distalis of the male equine pituitary gland.

The intrapituitary mechanisms regulating gonadotrophin secretion in the horse remain unclear. Here, we examined seasonal and gonadal effects on the gonadotroph and lactotroph populations of male horses with the aim of defining a possible morphological basis for the differential release of gonadotrophins. Pituitaries were collected from: (i) gonadal-intact horses in the breeding season (GBS); (ii) orchidectomized horses in the breeding season (OBS); and (iii) orchidectomized horses in the nonbreeding season (ONBS). Immunohistochemistry was performed using antibodies to the luteinizing hormone (LH) beta subunit, follicle-stimulating hormone (FSH) beta subunit and prolactin. In all groups, gonadotrophs were distributed throughout the pars distalis, with dense populations detected near the borders with the pars tuberalis and pars intermedia. The numbers of LH-monohormonal, FSH-monohormonal and bihormonal cells/field were greater in GBS than in OBS and ONBS horses. Similarly, the proportion of gonadotrophs in relation to all pituitary cells was larger in gonadal-intact than orchidectomized horses. In the absence of the gonads, no effects of season were observed on these variables. Interestingly, the relative proportions of gonadotroph subtypes and the LH/FSH gonadotroph ratio were similar among groups. Furthermore, while specific gonadotroph-lactotroph associations were identified in all groups, significant gonadal effects within the breeding season and direct effects of season within orchidectomized horses were detected for the number of lactotrophs. This study reveals a gonadal-independent effect of season on the lactotroph, but not the gonadotroph population of the equine pituitary, and a clear gonadal stimulation of both cell types within the breeding season. We suggest that alterations in intercellular arrangements, rather than changes in the incidence of gonadotroph subtypes, may contribute to the differential release of gonadotrophins and, accordingly, to the intrapituitary control of fertility throughout the male equine annual reproductive cycle.

Animals↗
PubMed1985

Chemical synthesis of peptide fragments of the hormone-specific beta-subunit of human follicle-stimulating hormone.

In order to determine the specific antigenic determinants of human follicle-stimulating hormone (hFSH), hFSH-beta peptides with amino acid residues 33-49 (V2), 95-118 (V3), 76-118 (V3 + 1/2 C2), 1-33 (V1 + C1), 22-33 (1/2C1), and 95-107 (V3 + 1/4C2) according to the nomenclature of Stewart and Stewart [Stewart, M., & Stewart, F. (1977) J. Mol. Biol. 116, 175] as well as additional peptides with the residues 93-107, 91-107, 89-107, 87-107, and 85-107 were chemically synthesized. The peptides were examined in radioimmunoassay systems of FSH, luteinizing hormone (LH), or human chorionic gonadotropin (hCG). V3 + 1/2C2 and V1 + C1 showed immunological activity, whereas the other peptides did not. Antibodies were raised in rabbits against these peptides and examined for specific binding with hFSH, LH, thyroid-stimulating hormone (TSH), and hCG. V3 + 1/2C2 as well as V1 + C1 produced antisera, which specifically bound hFSH, hLH, and hTSH, indicating that the amino acid sequences contained in hFSH-beta peptides V3 + 1/2C2 and V1 + C1 share common antigenic sites with hLH and hTSH. Antisera were produced in rabbits against hFSH-beta, against reduced and S-aminoethylated hFSH-beta (AE-FSH-beta), and against AE-FSH-beta coupled to hemocyanin. Reduced and S-aminoethylated beta-subunit of FSH-beta coupled with hemocyanin produced antisera in rabbits that specifically bound only hFSH and not hLH, hTSH, or hCG.

Amino Acid Sequence↗
PubMed1998

Cloning of complementary deoxyribonucleic acid for the follicle-stimulating hormone-beta subunit in the Japanese quail.

Complementary DNA clones encoding the luteinizing hormone-beta and common alpha subunits have been isolated not only in mammals but also in some nonmammalian tetrapod vertebrates. However, cloning of cDNA encoding the follicle-stimulating hormone (FSH)-beta subunit is limited to mammals, and no clone for the FSH-beta subunit has been isolated for nonmammalian vertebrates. We report here the isolation and characterization of cDNA encoding the FSH-beta subunit precursor molecule in the Japanese quail from a cDNA library of the pituitary gland of this bird. As the hybridization probe for the screening, we used a cDNA clone prepared by the polymerase chain reaction (PCR) with primers designed from known nucleotide sequence data of cDNA for FSH-beta subunit precursors of mammals. The FSH-beta subunit precursor cDNA we isolated was longer than any other FSH-beta subunit precursor cDNAs previously reported. This is due to the extraordinarily long 3'-untranslated region (2135 bp). This region is extremely rich in consensus sequences reported to cause instability of mRNA, suggesting that mRNA for the FSH-beta subunit, especially that of the Japanese quail, is unstable. Northern blot analysis of mRNA for the FSH-beta subunit revealed that the pituitary content of mRNA in the nonbreeding season was about 1/5 to 1/10 that in the breeding season in male Japanese quail kept in an outdoor cage. The profile of the seasonal change in FSH-beta subunit mRNA in the quail pituitary gland was similar to that of the seasonal change in the concentration of FSH in plasma reported previously. The deduced amino acid sequence of the mature protein region showed that the quail FSH-beta subunit is more similar to the opossum FSH-beta subunit than to the other mammalian FSH-beta subunits.

Amino Acid Sequence↗
PubMed1997

The follicle-stimulating hormone beta-subunit gene of the common brushtail possum (Trichosurus vulpecula): analysis of cDNA sequence and expression.

Reverse transcription-PCR has been used to obtain a cDNA sequence from the follicle-stimulating hormone (FSH) beta-subunit gene of the Australian brushtail possum (Trichosurus vulpecula). Comparisons of the possum FSHbeta-mRNA coding region nucleotide sequence with that of six eutherian mammal homologues reveals a mean percent identity of 77.3% and 76.8% at the nucleotide and predicted amino acid-sequence levels respectively. Furthermore, the predicted amino acid sequence of the possum FSHbeta mature protein shows evolutionary conservation of twelve cysteine residues and two potential N-linked glycosylation sites. The protein lacks the CAGY motif present in most reported glycoprotein beta-subunit sequences. The translation termination codon and consensus polyadenylation sequence overlap, a feature observed in other mammalian FSHbeta genes. Northern hybridization of total RNA from adult female possum pituitary revealed three hybridizing transcripts of approximately 2.8, 1.2 and 0.5 kb which may arise from utilizing alternative polyadenylation signals. In situ hybridization localized the FSHbeta transcripts to a sub-population of anterior pituitary cells interpreted as being gonadotropes. In summary the results indicate considerable evolutionary conservation of the structure of the FSH beta-subunit gene between the marsupial and eutherian mammalian lineages.

Adult↗
PubMed1998

Enzyme immunoassay method for total urinary follicle-stimulating hormone (FSH) beta subunit and its application for measurement of total urinary FSH.

OBJECTIVE: To develop and validate an enzyme-linked immunosorbent assay (ELISA) for total urinary follicle-stimulating hormone (FSH) that can be used to evaluate frozen-thawed urine samples. DESIGN: A method was developed for dissociating urinary FSH into subunits by boiling. An ELISA for the free beta subunit of FSH was used to measure total FSH in urine samples collected from male and female volunteers. The urinary FSH values were compared with serum FSH concentrations in paired samples. SETTING: A clinical research laboratory. PATIENT(S): Serum and urine samples from normal male and female volunteers and from men with infertility were used to develop and validate an assay for total urinary FSH. INTERVENTION(S): None. RESULT(S): Urinary FSH concentrations in frozen-thawed urine were highly correlated to matched serum FSH concentrations. CONCLUSION(S): A microtiter plate ELISA for FSH beta subunit provides an economical method for evaluating FSH secretion in men and women. This method has practical applications for population-based epidemiologic studies in which urine samples are collected in the field and stored frozen before analysis.

Adult↗
PubMed1990

Gonadotropin subunit messenger RNA concentrations after blockade of gonadotropin-releasing hormone action: testosterone selectively increases follicle-stimulating hormone beta-subunit messenger RNA by posttranscriptional mechanisms.

Regulation of gonadotropin gene expression by sex steroids may occur via direct effects on the pituitary and/or indirect effects of steroids mediated through hypothalamic GnRH. We aimed to define the effects of testosterone (T) on alpha, LH beta, and FSH beta mRNA expression in the male rat after blockade of GnRH action on the gonadotrope. A water-soluble GnRH antagonist was administered iv to castrate male rats (increased endogenous GnRH secretion) and to castrate T-replaced rats in which gonadotropin subunit mRNAs had been increased by prior treatment with exogenous GnRH pulses. In castrate male rats, GnRH antagonist resulted in a fall in all three subunit mRNAs. Alpha and LH beta declined at slower rates (half-disappearance after 50 and 65 h, respectively), and neither fell to values present in intact rats over 84 h. In contrast, FSH beta mRNA declined more rapidly, with a half-disappearance after 20 h. In castrate T-replaced rats, alpha mRNA declined at a rate similar to that in castrates (half-disappearance after 50 h). LH beta declined more slowly, and the rate of FSH beta decline was markedly prolonged in the presence of T (half-disappearance time increased from 20 to 50 h). These results suggest that T exerts direct effects on FSH beta transcription or mRNA stability which are independent of GnRH action. To assess these possibilities, a long-acting GnRH antagonist (Detirelix) was administered to castrate male rats, which also received T or sham implants 4 days after castration. FSH beta mRNA levels fell during the 4 days of Detirelix alone, but the addition of T on day 4 resulted in a 2-fold rise in FSH beta mRNA, restoring FSH beta mRNA to levels present in intact rats. Serum FSH closely paralleled FSH beta mRNA concentrations. Alpha mRNA was reduced by 25%, and LH beta mRNA concentrations were unchanged in the presence of T. The rate of alpha mRNA transcription was markedly reduced and that of LH beta tended to fall in T-treated rats, but T had no significant effect on the FSH beta transcription rate. Thus, the action of T to increase concentrations of cytosolic FSH beta mRNA appears to be exerted at a posttranscriptional level, possibly via effects of T on FSH beta mRNA stability. This may represent a mechanism by which T can effect differential regulation of gonadotropin subunit mRNA concentrations.

Amino Acid Sequence↗