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  • 1
    Electronic Resource
    Electronic Resource
    Structural and Functional Organization of the Gene Encoding the Human Thyrotropin-Releasing Hormone Receptor (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 72 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : The thyrotropin-releasing hormone (TRH) receptor (TRHR)is widely distributed throughout the central and peripheral nervous systems.In addition to its role in controlling the synthesis and secretion ofthyroid-stimulating hormone and prolactin from the anterior pituitary, TRH isbelieved to act as a neurotransmitter as well as a neuromodulator. We haveisolated genomic λ and P1-derived artificial chromosome clones encodingthe human TRHR. The gene was found to be 35 kb with three exons and twointrons. A 541-bp intron 1 (-629 to -89 relative to the translation startsite) is conserved between human and mouse. A large intron 2 of 31 kb disruptsthe open reading frame (starting in position +790) in the sequence encodingthe supposed junction between the third intracellular loop and the putativesixth transmembrane domain. A similar intron was found in chimpanzee and sheepbut not in rat and mouse. Promoter analysis of upstream regions demonstratedcell type-specific reporter activation, and sequencing of 2.5 kb of thepromoter revealed putative cis-acting regulatory elements for severaltranscription factors that may contribute to the regulation of theTRHR gene expression. Functional analysis of potential responseelements for the anterior pituitary-specific transcription factor Pit-1revealed cell type-specific binding that was competed out with a Pit-1response element from the GH gene promoter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0720040.x
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  • 2
    Electronic Resource
    Electronic Resource
    A cortical neuropeptide with neuronal depressant and sleep-modulating properties (1996)
    [s.l.] : Nature Publishing Group
    Nature 381 (1996), S. 242-245 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] While characterizing region-specific brain messenger RNAs, we isolated a complementary DNA clone whose sequence suggested that it corresponded to an mRNA that encoded a new protein of 112 amino-acid residues which we called preprocortistatin. Alignment of preprocortistatin with the 116-residue ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/381242a0
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  • 3
    Electronic Resource
    Electronic Resource
    The mechanisms by which vasoactive intestinal peptide (VIP) and thyrotropin releasing hormone (TRH) stimulate prolactin release from pituitary cells (1990)
    Springer
    Bioscience reports 10 (1990), S. 189-199 
    Details
    ISSN: 1573-4935
    Keywords: vasoactive intestinal peptide (VIP) ; thyrotropin releasing hormone (TRH) ; prolactin (PRL) ; lactotrophs ; anterior pituitary ; second messengers ; hormone secretion ; adenylate cyclase ; calcium ; inositol trisphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The effect of vasoactive intestinal peptide (VIP) on prolactin (PRL) secretion from pituitary cells is reviewed and compared to the effect of thyrotropin releasing hormone (TRH). These two peptides induced different secretion profiles from parafused lactotrophs in culture. TRH was found to increase PRL secretion within 4 s and induced a biphasic secretion pattern, while VIP induced a monophasic secretion pattern after a lag time of 45–60 s. The secretion profiles are compared to changes in adenylate cyclase activity, production of inositol polyphosphates, changes in intracellular calcium concentrations and changes in electrophysiological properties of the cell membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01116578
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  • 4
    Electronic Resource
    Electronic Resource
    Bone turnover in rats treated with 1,25-dihydroxyvitamin D3, 25-hydroxyvitamin D3 or 24,25-dihydroxyvitamin D3 (1993)
    Springer
    Bioscience reports 13 (1993), S. 27-39 
    Details
    ISSN: 1573-4935
    Keywords: Bone turnover ; cholecalciferols ; parathyroid hormone ; calcitonin ; prolactin ; growth hormone ; alkaline phosphatase ; cAMP ; hydroxyproline
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Female rats were given 1,25-dihydroxyvitamin D3 (1,25(OH)2D3), 0.25 μg per 100 g body weight (bw), 25-hydroxyvitamin D3 (25(OH)D3), 1.7 μg/100 g bw or 24,25-dihydroxyvitamin D3 (24,25(OH)2D3) 1.7 μg/100 g bw, subcutaneously three times a week for 12 weeks. Traditional variables pertaining to calcium homeostasis and growth, i.e. blood and urine calcium (Ca) and phosphate (P), serum levels of vitamin D3 metabolites parathyroid hormone, (PTH), calcitonin (CT), prolactin (PRL) and growth hormone (GH) were measured every four weeks. This data pool was correlated with bone matrix turnover parameters, i.e. serum levels of alkaline phosphatase (ALP) and urinary hydroxyproline (u-HYP) excretion. After 12 weeks of treatment, 1,25(OH)2D3 significantly enhanced serum total and ionized Ca, urine Ca and urine P, and also diminished urine cAMP due to reduced renal function (creatinine clearance). However, 25(OH)D3 administration had no such impact. 24,25(OH)2D3 opposed the effect of 1,25(OH)2D3 after 12 weeks by significantly augmenting serum P and diminishing serum levels of total Ca and ionized Ca. Cross sectional group analyses showed that criculating levels of ALP were directly related with serum 1,25(OH)2D3 and inversely related to serum 24,25(OH)2D3 and CT. Total u-HYP and per cent non-dialysable HYP (ndHYP) were reciprocally and positively correlated with serum PRL, respectively. However, no such relations were observed with serum GH. It appears that rats with elevated circulating levels of 1,25(OH)2D3 exhibit increased bone resorption, while augmented 24,25(OH)2D3 is associated with the opposite. Apparently, high bone turnover (i.e. reduced total urinary HYP and enhanced ndHYP) is associated with high serum PRL.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01138176
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  • 5
    Electronic Resource
    Electronic Resource
    On the involvement of cyclic AMP and extracellular Ca2+ in the regulation of hormone release from rat pituitary tumour (GH3) cells in culture (1987)
    Springer
    Bioscience reports 7 (1987), S. 93-105 
    Details
    ISSN: 1573-4935
    Keywords: GH3 cells ; hormone release ; cyclic AMP ; Ca2+ ; calmodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Thyroliberin (TRH), dibutyryl cyclic AMP (db-cAMP), and 3-isobutyl-l-methylxanthine (MIX) had a stimulatory effect on prolactin (PRL) and growth hormone (GH) release from GH 3 cells. Half-maximal and maximal effects were observed for TRH at 2.5 nM and 10 nM; for db-cAMP at 0.6 mM and 5 mM, respectively. MIX (0.1 mM–1 mM) induced a dose-dependent accumulation of cellular cyclic AMP, while the hormone release was already maximally stimulated at 0.1 mM MIX. The maximal effects on hormone release of TRH and db-cAMP, but not of TRH and MIX, were additive. The Ca2+ channel blockers Co2+ (5 mM) and verapamil (100 μM) and the Ca2+ chelator EGTA (4 mM) abolished the stimulatory effect of TRH (1 μM) on hormone release. Co2+ and verapamil, but not EGTA, inhibited the stimulatory effect of db-cAMP (5 mM) on hormone release. The inhibitory effects of Co2+ and verapamil on GH release were counteracted by the combination of TRH and db-cAMP. For PRL release Co2+, but not verapamil, was able to inhibit the combined action of TRH and db-cAMP. Co2+, verapamil, and EGTA eliminated the stimulatory effect of MIX (1 mM) on PRL release while only Co2+ and EGTA affected the GH release. Hormone release in the presence of MIX plus verapamil or EGTA, but not Co2+, was increased by TRH. The calmodulin antagonist trifluoperazine (TFP) at 30 μM inhibited basal hormone release and hormone release stimulated by TRH (1 μM), db-cAMP (5 mM), and MIX (1 mM). The Ca2+ ionophore A23187 (5 μM) had a stimulatory effect on basal hormone release which was abolished by 30 μM TFP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01121872
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  • 6
    Electronic Resource
    Electronic Resource
    Thrombin and H64A subtilisin cleavage of fusion proteins for preparation of human recombinant parathyroid hormone (1991)
    Springer
    The protein journal 10 (1991), S. 517-526 
    Details
    ISSN: 1573-4943
    Keywords: Enzymatic cleavage ; fusion protein ; parathyroid hormone ; thrombin ; H64A subtilisin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Human parathyroid hormone, hPTH, an 84 amino acid polypeptide, was produced intracellularly inEscherichia coli as a fusion protein, linked to the C-terminus of a 15 kD IgG-binding protein. Approximately 100 mg fusion protein was obtained per liter fermentation medium. To test the efficiency of two alternative enzymatic cleavage methods, two fusion proteins differing only in the linker region were constructed. Cleavage of a Phe-Phe-Pro-Arg linker was obtained with bovine thrombin and cleavage of a Phe-Ala-His-Tyr linker with recombinant H64A subtilisin. Both enzmes yielded the correct N-terminus and cleaved their respective linkers quantitatively, although additional internal cleavage sites in hPTH were detected and characterized. The linker cleavage conditions were optimized and hPTH was purified to homogeneity. Thrombin cleavage resulted in a final yield of 5 mg hPTH/L, while H64A subtilisin cleavage was more specific and gave 8 mg/L. The purified recombinant product was identical to native hPTH and exhibited full biological activity in an adenylate cyclase assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025480
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  • 7
    Electronic Resource
    Electronic Resource
    Variations in prolactin and growth hormone production during cellular growth in clonal strains of rat pituitary cells (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 91 (1977), S. 15-29 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A permanent, clonal strain of rat pituitary tumor cells (GH3-cells) spontaneously synthesizes and secretes prolactin (rPRL) and growth hormone (rGH) into the culture medium. The rates of hormone production (μg extracellular hormone/mg cell protein/24 hours) and synthesis (vida infra) as well as the rate of [3H]thymidine incorporation into DNA (DNA synthesis) have been studied.During logarithmic growth rPRL and rGH production increased to 160 and 250% of the value at day 2 after plating, while during the plateau phase of cell growth hormone production decreased to initial values. The fluctuations in rPRL production could be fully explained by variations in the rate of rPRL synthesis: [3H]leucine incorporated into rPRL as measured with immunoprecipitation and polyacryl-amide gel electrophoresis. Also the rates of synthesis and production of rGH showed parallel changes during exponential and plateau phase of growth, but this hormone was probably degraded intracellularly. The relative reduction in the rate of synthesis of rPRL and rGH during the plateau phase of growth corresponded closely to the fall in the rate of DNA synthesis. The reduction in rPRL synthesis could not be explained through an inhibition by extra-cellular rPRL accumulation or by cell to cell interaction occurring in dense cultures.The intracellular concentrations of both hormones were unaltered during logarithmic growth, but rose to 500% for rPRL and 200% for rGH during the plateau phase.In spite of the marked variations in basal rPRL and rGH production, the GH3 cultures of different ages were equally able to increase rPRL and decrease rGH production in response to thyrotropin releasing hormone (3 X 10-7 M) and 17β-estradiol (10-8 M).
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040910103
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  • 8
    Electronic Resource
    Electronic Resource
    Effects of colchicine and 2-Br-α-Ergocryptine-methane-sulfonate (CB 154) on the release of prolactin and growth hormone by functional pituitary tumor cells in culture (1973)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 82 (1973), S. 401-409 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of colchicine and 2-Br-α-ergocryptine-methane-sulfonate (CB 154) on the release of prolactin and growth hormone have been studied in a clonal strain of rat pituitary tumor cells (GH3) in monolayer culture. These cultures produce both prolactin and growth hormone and release both proteins spontaneously into the medium without storing them in large amounts. Immunological methods were used to measure both intracellular and extracellular concentrations of the hormones. Colchicine (5 × 10-6 M for 3 hours) caused a 2- to 3-fold increase in intracellular concentrations of prolactin and growth hormone but, under basal conditions, had little or no measurable effect on the amounts of hormone accumulated in the medium during the course of the standard three hour treatment period. This latter finding evidently is due to a lag in the onset of drug action. Colchicine had little or no effect on accumulation of extracellular prolactin during the first two hours of treatment whereas such accumulation was depressed by over 60% during the third hour of treatment. Previous studies have shown that treatment of GH3 cells with thyrotropin releasing hormone (TRH) and hydrocortisone (HC) increases both intra and extracellular levels of prolactin and growth hormone, respectively. In cultures treated with TRH (5 × 10-8 M), colchicine (5 × 10-6 M for 3 hours) increased intracellular prolactin by about 70% and decreased extracellular hormone by 10%. In cultures treated with HC (3 × 1O-6 M), colchicine increased intracellular growth hormone by more than 100% and decreased medium concentrations of the hormone by 15%. Colchicine did not significantly alter total hormone (intracellular + extracellular) accumulation, cellular uptake of 3H-amino acids, or total cell protein synthesis. The synthetic ergot alkaloid, CB 154, (3.3 × 10-6 M for 3 hours) caused an 80% increase in intracellular, and a nearly 50% decrease in extracellular, prolactin without affecting the accumulation of growth hormone, the uptake of 3H-labeled amino acids, or overall protein synthesis in the cultures. Elevation of medium potassium concentration from a basal value of 5.3 mM to 3-5 × 10-2 M (by addition of KCl) decreased intracellular levels of prolactin by 85% and growth hormone by 55%. These effects of high potassium were blocked by colchicine and by CB 154. We conclude that colchicine, after a lag period of two hours, acts to inhibit the release of prolactin and growth hormone from GH3 cells. By the end of three hours of treatment, this inhibition is over 60% complete in the case of prolactin. The qualitatively different effects of colchicine and CB 154 on prolactin and growth hormone release suggest that these two secretory blocking agents probably act on GH3 cells by different mechanisms.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040820310
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  • 9
    Electronic Resource
    Electronic Resource
    Nucleotidase activity in regenerating liver and in clonal strains of hepatoma and pituitary cells in culture (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 88 (1976), S. 13-22 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A nucleotidase of the combined 3′- and 5′-type (nucleotide phosphohydrolase, E.C.3.1.3.31) was present in the cytosol of regenerating rat liver cells, and of rat hepatoma and pituitary cells in culture. The enzyme activity per milligram of cell protein was very similar in regenerating liver and in three of the different cell types. The hepatoma cell strain which showed the slowest growth rate had a three-fold higher basal enzyme activity. After the first days of regenerative growth in rat liver and during early plateau phase of cell growth, there was a 50-120% increase in specific enzyme activity. In the hepatoma cells, the enzyme activities were also compared to the cellular content and synthesis of RNA and DNA. The increase in enzyme activity occurred concomitantly with a reduced incorporation of 3H-thymidine into DNA. The possible physiological role of this nucleotidase in nucleic acid and nucleotide metabolism is discussed.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040880103
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  • 10
    Electronic Resource
    Electronic Resource
    Human parathyroid hormone as a secretory peptide in milk of transgenic mice (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 59 (1995), S. 168-176 
    Details
    ISSN: 0730-2312
    Keywords: human parathyroid hormone ; transgenic mice ; mammary gland ; secretory peptide ; osteoporosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: In a transgenic mouse model we have targeted the expression of recombinant human parathyroid hormone (hPTH) to the mammary gland yielding hPTH as a secretory, soluble peptide in milk. A 2.5 kb upstream regulatory sequence of the murine whey acidic protein (WAP) directed the expression of the hPTH cDNA in a fusion gene construct (WAPPTHSV2) containing the SV40 small t-antigen intron and polyadenylation site in the 3′ end. Established lines of transgenic mice secreted hPTH to milk in concentrations up to 415 ng/ml. Recombinant hPTH recovered from the milk was purified by HPLC and shown to be identical to hPTH standard as analyzed by SDS-PAGE followed by immunoblotting. Expression of the WAPPTHSV2 was limited to the mammary gland as analyzed by polymerase chain reaction (PCR) and Southern blot of reversed transcribed mRNA from different tissues. hPTH is an important bone anabolic hormone and may be a potentially important pharmaceutical for treatment of demineralization disorders such as osteoporosis. We present the transgenic animal as a possible production system for hPTH. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240590206
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