UNIPROT:P01189 - FACTA Search

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Query: UNIPROT:P01189 (beta-endorphin)
21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The presence of glucocorticoid receptor (GR) in the anterior lobe of the pituitary gland has previously been demonstrated, but the exact cell types expressing GR have not yet been characterized. In this study, we demonstrate the colocalization of GR and pituitary hormones in the rat pituitary gland by using an immunocytochemical double-labelling method. The majority of anterior lobe corticotropin-immunoreactive and growth hormone-immunoreactive cells contained GR-like immunoreactivity. Cells of the intermediate lobe showed intensive ACTH-like immunoreactivity but did not express GR. The glycoprotein hormones thyroid-stimulating hormone, follicle-stimulating hormone and luteinizing hormone were colocalized with GR to a lesser degree; approximately one-half of the cells exhibited immunoreactivity to these hormones contained GR. By contrast, only a minority of the prolactin-immunoreactive cells expressed GR. Our results suggest that glucocorticoids may differentially regulate the secretion and/or synthesis of these pituitary hormones by directly affecting the hormone-producing cells of the anterior pituitary.
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PMID:Glucocorticoid receptor colocalization with pituitary hormones in the rat pituitary gland. 831 36

Asn-linked oligosaccharides terminating with the sequence SO4-4GalNAc beta 1,4GlcNAc beta 1,2Man alpha (S4GGnM) are present on the glycoprotein hormones lutropin and thyrotropin, pro-opiomelanocortin, and tissue factor pathway inhibitor. The peptide motif ProXaaArg/Lys (PXR/K), which is recognized by a PXR/K-specific GalNAc-transferase, is present in each of these glycoproteins 6-9 residues NH2-terminal to an Asn glycosylation site. Both the PXR/K-specific GalNAc-transferase and a GalNAc beta 1,4GlcNAc beta 1,2Man alpha (GGnM)-4-sulfotransferase are required for synthesis of the S4GGnM sequence. Glycoproteins which do not contain the PXR/K motif but bear Asn-linked oligosaccharides terminating with GGnM or sialic acid alpha 2,3/6GGnM have also been described, suggesting a distinct GalNAc-transferase may be responsible for their synthesis. We have examined a number of tissues and cultured cell lines for the transfer of sulfate to the trisaccharide acceptor GGnM and transfer of GalNAc to oligosaccharide acceptors on protein which do, human chorionic gonadotropin (hCG), and do not, transferrin (Trf), contain the PXR/K motif. The PXR/K-specific GalNAc-transferase and the GGnM-4-sulfo-transferase are expressed in salivary gland, pituitary, lacrimal gland, kidney, and brain, and in the cell lines AtT-20, 293, SHSY5Y, and alpha T3. In contrast Bowes, EL-4, and B16L6 cell extracts transferred GalNAc to oligosaccharides acceptors on Trf but not on hCG. A number of tissues and cell lines displayed transfer of GalNAc to both hCG and to Trf suggesting that two distinct GalNAc-transferases were present. The GGnM-4-sulfotransferase was expressed in tissues and cell lines which expressed the PXR/K-specific GalNAc-transferase but not in cell lines expressing exclusively the Trf-specific GalNAc-transferase. Thus, the PXR/K-specific GalNAc-transferase and the GGnM-4-sulfotransferase are coordinately expressed in a number of tissues other than pituitary. The Trf-specific GalNAc-transferase may account for the presence of beta 1,4-linked GalNAc on glycoproteins which do not contain the PXR/K motif.
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PMID:Co-ordinate and restricted expression of the ProXaaArg/Lys-specific GalNAc-transferase and the GalNAc beta 1,4GlcNAc beta 1,2Man alpha-4-sulfotransferase. 834 98

A panel of long-term murine T lymphocyte clones specific for the glycoprotein of vesicular stomatitis virus (VSV) in association with either H-2I-Ad or I-E(d) was tested for the production of cytokines in both resting and poststimulation states using both in situ hybridization and bioassay. All but one of the clones showed antigen-specific cytolytic activity in a 4-hr 51Cr release assay. Unexpectedly, the clones did not appear to be typical Th1 cells. Five of these T cell clones produced both IL-2 and IFN-gamma but not IL-4 after stimulation with either phorbol 12-myristate 13-acetate (PMA) or concanavalin A (Con A). Some clones constitutively expressed mRNA for IL-2 and INF-gamma. The proliferation of these clones was factor independent, suggesting an autocrine growth mechanism. Three clones produced variable levels of IL-4 mRNA and some, to significant quantities, of IL-2 mRNA. One cytolytic clone produced neither IL-2 nor IL-4 mRNA to detectable levels, although mRNA for IFN-gamma was observed. A noncytolytic, Ag-specific clone produced IL-6, tumor necrosis factor (TNF), and lymphotoxin (LT), but no IL-2, IL-4, or IFN-gamma mRNA. There was a strong quantitative correlation between the expression of IL-2-, INF-gamma-, and LT-specific mRNAs by the clones. All the T cell clones tested which secreted INF-gamma and LT expressed no measurable IL-4 mRNA. We examined expression of several other genes in the panel of clones. These included TNF, met-enkephalin (met-enk), IL-1, and IL-6. IL-1 m-RNA synthesis was not observed in any of the T cell clones. Almost all clones produced TNF mRNA. Parallel bioassays showed that secreted IL-2/IL-4 activity levels and mRNA levels correlated well for all clones. Thus, we observed a great degree of heterogeneity among CD4+ cytolytic T lymphocyte clones.
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PMID:Lymphokine expression profile of resting and stimulated CD4+ CTL clones specific for the glycoprotein of vesicular stomatitis virus. 838 Oct 52

Yeast cells express an alternate enzyme encoded by the YAP3 gene which can process pro-alpha-mating factor when this pheromone is overexpressed in KEX2-deficient mutants. The YAP3 gene product is an aspartic protease (YAP3) that cleaves at paired basic residues (Egel-Mittani, M., Flygenring, H.P., and Hansen, M. T. (1990) Yeast 6, 127-137). In this study, the YAP3 gene was overexpressed in the BJ 3501 strain of Saccharomyces cerevisiae. YAP3 was purified to apparent homogeneity using concanavalin A and pepstatin A affinity chromatography. The enzyme was characterized as an M(r) 68,000 glycoprotein with a pH optimum of 4.0-4.5. It was inhibited by pepstatin A and activated by 5 mM Ca2+. YAP3 cleaved at paired basic residues of mouse pro-opiomelanocortin (POMC) to yield adrenocorticotropin (ACTH) and beta-lipotropin (LPH); human beta-LPH to yield beta-endorphin-(1-31), beta-endorphin-(1-29), beta-endorphin-(1-28), gamma-LPH, and beta-melanocyte-stimulating hormone; and bovine N-POMC1-77 to yield gamma 3-melanocyte-stimulating hormone. It also cleaved the tetrabasic residues of ACTH1-39 to yield primarily ACTH1-15 and Lys-Arg-corticotropin-like intermediate lobe peptide. The physical properties, pH optimum, and specificity of YAP3 indicate that it is a homologue of the mammalian POMC-converting enzyme (EC 3.4.23.17), a paired basic residue-specific aspartic protease from bovine pituitary intermediate lobe secretory granules (Loh, Y. P., Parish, D.C., and Tuteja, R. (1985) J. Biol. Chem. 260, 7194-7205).
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PMID:Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme. 838 68

Corticotropin-induced secreted protein (CISP) is a trimeric glycoprotein secreted by primary cultures of bovine adrenortical cells in response to adrenocorticotropic hormone (ACTH). This protein was recently purified in our laboratory, and its N-terminal amino-acid sequence revealed a significant similarity with thrombospondin-2 (TSP2). We report here the nucleotide sequence of a 386 bp RT-PCR fragment specific for CISP. The deduced protein sequence shares 84% identity with the N-terminal portion of mature human TSP2, suggesting that CISP is its bovine counterpart. Northern analysis of adrenocortical cell RNA using the above cDNA fragment as a probe revealed a 6.0 kb CISP/TSP2 mRNA whose abundance was increased nearly fivefold following a 24 h cell treatment with 10(-7) M ACTH. Under the same conditions, the expression of TSP1 mRNA was reduced by tenfold. The protein levels of TSP1 and CISP/TSP2 varied accordingly with their respective mRNA levels, as shown by immunoprecipitation and immunofluorescence experiments. Taken together, these data show that ACTH induces a dramatic shift in the pattern of adrenocortical cell thrombospondin expression from TSP1 to CISP/TSP2. This observation suggests that these two members of the thrombospondin family exert distinct biological functions in the adrenal cortex. This hypothesis is further supported by the observation that anti-CISP antibodies inhibit the maintenance of the morphological changes of bovine adrenocortical cells induced by ACTH, whereas anti-TSP1 antibodies do not.
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PMID:Opposite regulation of thrombospondin-1 and corticotropin-induced secreted protein/thrombospondin-2 expression by adrenocorticotropic hormone in adrenocortical cells. 869 34

Pituitary adenomas that are characterized by the absence of a particular clinical syndrome and the absence of excessive hormone secretion have been classified as nonfunctioning adenomas. Recent development of immunohistochemical analysis and hormonal assay have suggested that many of these tumors have function to secret the gonadotropin subunits. A novel procedure biotin amplification in immunohistochemistry, catalyzed signal amplification (CSA) has been reported recently. In this study, the authors applied this new method to tissues from 50 cases of clinically nonfunctioning adenomas. These cases had no evidence of endocrinological signs by hormone secretion. When the CSA system was applied in normal pituitary gland, each of subunits was positive even when the antibody was diluted 1:1,000,000, which is 1,000 folds of standard indirect immunoperoxidase method. Immunohistochemical staining by indirect immunohistochemical method revealed that all 50 adenomas were negative for all the anterior hormones, including growth hormone (GH), prolactin (PRL), adrenocorticotropic hormone (ACTH), beta-subunit of luteinizing hormone (LH beta), follicle-stimulating hormone (FSH beta), thyroid stimulating hormone (TSH beta), and a-subunit of glycoprotein (alpha SU). Using avidin-biotin complex (ABC) method, two cases were positive for FSH beta and four cases were positive for alpha SU, respectively, and the immunopositivities were observed weakly in scattered cells. By CSA system, 26 cases of 50 nonfunctioning adenoma were positive for FSH beta, 16 cases were positive for LH beta, and 29 cases were positive for alpha SU, respectively. The immunoreactivities were clearly observed in cytoplasm of many adenoma cells. This amplification procedure provides a means of greatly increasing the sensitivity of the immunohistochemistry including subunits of glycoproteins that are difficult to detect by previous indirect immunoperoxidase method or ABC method. This amplification procedure provides a great increase in the sensitivity of the immunohistochemistry for the detection of gonadotropin subunits and suggest that significant proportion of the nonfunctioning adenomas are gonadotropin subunit producing adenomas.
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PMID:Application of catalyzed signal amplification in immunodetection of gonadotropin subunits in clinically nonfunctioning pituitary adenomas. 870 26

Specific cells of the hypophyseal pars tuberalis (PT) have been associated with the transmission of photoperiodic stimuli to the endocrine system. However, their principal secretory products have not been identified yet. Therefore we studied the expression of several adenohypophyseal hormones and their subunits (TSH, FSH, LH, common alpha-chain, GH, ACTH, PRL, alpha- and gamma-MSH, beta-lipotropin) by immunocytochemistry, Northern blot analysis and in situ hybridization in the sheep pituitary. Only the common alpha-chain of glycoprotein hormones could be detected in ovine PT-specific cells by immunocytochemistry while antibodies directed against the beta-chains of LH, FSH, TSH and beta-lipotropin labeled single cells in the PT but failed to detect these antigens in PT-specific cells. In situ hybridization and Northern blot analysis with antisense oligonucleotides against the common alpha-chain, beta-LH, beta-FSH, beta-TSH, PRL and POMC revealed the expression of these subunits in the ovine PT. The mRNA of the common alpha-chain, beta-TSH and, to a far lower extent, PRL and POMC were found throughout the entire pars tuberalis while beta-FSH and beta-LH could only be detected in cells of the caudal PT. Hence, GH-mRNA and GH immunoreactivity were exclusively found in the pituitary pars distalis. Compared to these results--obtained under the short photoperiod (winter)--we found clear ultrastructural signs of altered secretory activity in PT-specific cells of animals exposed to the long photoperiod (summer); the common alpha-chain immunoreactivity was nearly absent in PT-specific cells of summer animals. However, no seasonal influence on gene transcription or translation for other adenohypophyseal hormone was observed. These findings suggest that ovine PT-specific cells, which are only immunopositive for the common alpha-chain, are capable to express different mRNAs of adenohypophyseal hormones. Although it remains elusive how gene transcription and translation are related in this cell type, the presence of an mRNA pool for hormone subunits leads to the speculation that--at least in the sheep--hormone synthesis is mainly regulated at the translational level and that secretion of hormones may be primarily constitutive.
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PMID:Evidence for gene transcription of adenohypophyseal hormones in the ovine pars tuberalis. 883 51

Somatotroph adenomas often secrete prolactin (PRL) besides growth hormone (GH) and are sometimes immunostained for other anterior pituitary hormones or their subunits, such as thyroid-stimulating hormone (TSH) beta-subunit and glycoprotein hormone alpha-subunit (alpha SU). However, somatotroph adenomas showing hypersecretion of adrenocorticotropic hormone (ACTH) are extremely rare. There have been, to our knowledge, only five published reports on somatotroph adenomas accompanied by excessive ACTH secretion. Here we report a case of intracavernously invading somatotroph macro-adenoma with high serum GH, PRL, and ACTH levels. We examined the case using immunohistochemistry (IHC), in situ hybridization (ISH), and cell culture, and confirmed GH, PRL, and ACTH, as well as alpha SU, production, and the expression of Pit-1 protein by the adenoma, which is known as a transcriptional factor for GH, PRL, and TSH, not for ACTH. Therefore, the presence of unknown transcriptional factor other than Pit-1, common to GH, PRL, and ACTH, may be speculated to be expressed in this adenoma. In our previous study, we had found plurihormonal mRNA expression, especially for ACTH, the beta-subunit of follicle-stimulating hormone and luteinizing hormone in some somatotroph adenomas, using non-radio-isotopic ISH, and suggested that these adenomas might be derived from plurihormonal primordial stem cells. Our present case is significant from the viewpoint of histogenesis of pituitary adenomas, because it further supports the cell origin of somatotroph adenomas from plurihormonal primordial stem cells, and moreover it suggests the presence of unknown transcriptional factor other than Pit-1, common to GH, PRL, and ACTH.
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PMID:A case of pituitary somatotroph adenoma with concomitant secretion of growth hormone, prolactin, and adrenocorticotropic hormone--an adenoma derived from primordial stem cell, studied by immunohistochemistry, in situ hybridization, and cell culture. 889 Sep 99

Sulfated glycoprotein-2 (SGP-2 or clusterin) is a complex multifunctional molecule that has been recently been implicated in neuronal degeneration and remodeling. We have shown that estradiol treatment results in a selective destruction of beta-endorphin neurons in the hypothalamic arcuate nucleus. We have used immunocytochemistry to determine the distribution of SGP-2 immunoreactivity in the rat hypothalamus and to assess the effects of the estradiol-induced destruction of beta-endorphin neurons on SGP-2 expression. We have found that SGP-2-immunopositive neurons normally occur in the medial preoptic area (MPOA), supraoptic nucleus (SON), paraventricular nucleus (PVN), dorsomedial nucleus (DM), and the lateral hypothalamic area (LHA) in both males and females. The neuropil appears free of label. Treatment with estradiol valerate results in the appearance of immunopositive punctate deposits in the neuropil in the MPOA, PVN and DM. The number and distribution of SGP-2-positive neurons are unaffected by estradiol treatment except in the MPOA, where there are twice as many SGP-2-positive neurons as in controls. These effects are precluded by treatment with vitamin E, with blocks the cytotoxic action of estradiol on beta-endorphin neurons. Thus, we interpret these changes as responses to the loss of beta-endorphin afferents.
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PMID:The effect of estradiol-induced hypothalamic pathology on sulfated glycoprotein-2 (clusterin) expression in the hypothalamus. 903 92

In domestic ruminants such as the sheep, birth is effected through sequential maturation of the foetal hypothalamic-pituitary-adrenal (HPA) axis, leading to the increased output of cortisol. Factors regulating foetal pituitary adrenocorticotrophin (ACTH) secretion have been delineated, and these include corticotrophin releasing hormone (CRH), arginine vasopressin, prostaglandin (PG) E2 and endogenous opioids. The pre-partum increase in foetal plasma ACTH is associated with a rise in pro-opiomelanocortin (POMC) mRNA in the foetal pars distalis, and with an altered pattern of POMC post-translational processing. Foetal adrenal activation results from an increase in ACTH receptors and enhanced coupling through the Gs protein to adenylate cyclase, and increased expression of key steroidogenic enzymes including P450c17. Cortisol modulates the mechanism by which ACTH activates foetal adrenal function, through specific glucocorticoid receptors (GR) in the foetal adrenal cortex. Although the numbers of GR change with gestation, the relative abundance of GR mRNA does not, pointing to post-translational regulatory mechanisms. Cortisol also stimulates an increase in the concentration of its own high affinity binding protein (corticosteroid binding globulin; CBG) in the foetal circulation, apparently by increasing CBG gene expression in the foetal liver, and by altering the extent of foetal CBG glycosylation in a manner that would be expected to decrease the metabolic clearance of this glycoprotein. Clear evidence for placental CRH and ACTH production is lacking in sheep, but PGE2, produced in increasing amounts by the placenta during late pregnancy, may augment the drive to HPA maturation. Aspects of the maturational pathway of cortisol biosynthesis have been described in other species, including the horse, and some comparison is made with the more detailed information currently available from species such as the sheep.
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PMID:Foetal endocrine maturation. 907 35

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