Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The actions of DL-threo-beta-fluoroasparagine (DL-beta-F-Asn) on the glycosylation of proteins were examined in AtT-20/D16v cells which synthesize several forms of the glycoprotein prohormone, pro-opiomelanocortin (POMC). Treatment with threo-beta-F-Asn(5-10 mM) resulted in: 1) a reduction in the amount of the more highly glycosylated form of POMC (Mr = 32,000) relative to the less glycosylated form (Mr = 29,000) and 2) the appearance of a new species of POMC (Mr = 27,000). 35S]Methionine-labeled tryptic peptides prepared from 27,000 POMC were identical to those from 29,000 and 32,000 POMC; however, 27,000 POMC was found to contain 10% as much [3H]glucosamine relative to [35S]methionine as the 32,000 molecule. Furthermore, 27,000 POMC comigrated with a previously characterized unglycosylated form of this prohormone produced by treatment of cells with tunicamycin. These findings indicate that treatment of cells with threo-beta-F-Asn results in the production of a species of POMC which contains little or no carbohydrate. The effects of beta-F-Asn were specific for the threo diastereomer, were reversible by equimolar concentrations of Asn, but not Asp, and were dose-dependent. Evidence that threo-beta-F-Asn can replace Asn in proteins was obtained by showing that an identified Asn-containing tryptic peptide from threo-beta-F-Asn-treated cells displayed an altered mobility during electrophoresis consistent with threo-beta-F-Asn substitution within this peptide. We conclude that threo-beta-F-Asn can inhibit the glycosylation of proteins in intact cells and that this effect is due to its ability to replace Asn at glycosylation sites.
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PMID:Inhibition of asparagine-linked glycosylation of pro-opiomelanocortin in mouse pituitary cells by DL-threo-beta-fluoroasparagine. 686 47

In the sea turtle Caretta caretta the dorsal wall of the pituitary anlage and the apex of the hypophyseal angle are derived from stomodeal epithelium adherent to the neural epithelium of the diencephalon; a substantial part of the ventral wall of the anlage is derived from epithelium of mixed origin (stomodeum and foregut). Distribution of immunoreactive cells in the embryonic gland suggests that pituitary peptide hormones (adrenocorticotropin, ACTH; melanotropin, MSH; prolactin, PRL; growth hormone, GH) are synthesized in cells from the dorsal wall, while cells producing glycoprotein hormones (luteinizing hormone, LH; thyrotropin, TSH) trace their lineage to ventral and ventrolateral areas of the anlage that include some endoderm. Mesenchymal movements mold the epithelial anlage in two steps, delineating first the posterior and subsequently the anterior area of the gland. During the former process the lateral lobes are defined, and material immunoreactive with antiserum to ACTH appears in epithelial cells of presumptive pars distalis (PD) and pars intermedia (PI). Delineation of the anterior end of the pituitary gland occurs as the hypophyseal stalk forms, approximately one-fourth through ontogenesis. Shortly thereafter, immunoreactions demonstrate synthetic activity of distinctively distributed cells containing ACTH, PRL, GH, LH and TSH. In Caretta the lateral lobes of the pituitary anlage give rise to a distinct layer of tissue around the PD (pars tuberalis interna, PTint) and a thick layer on the floor of the hypothalamus (juxtaneural pars tuberalis, juxPT). In the pituitaries of late embryos, juxPT tissue proximal to the PD contains many cells immunoreactive with LH antiserum; whereas cells in distal areas of the juxPT do not react with any antisera tested. LH-cells also occur in large numbers in the PTint and in the posterior PD where tissues of the partes tuberalis and distalis are continuous. Cells reactive with antiserum to TSH are found in small numbers in the PTint, and in larger numbers along with the LH-cells in the posterior PD. PRL-cells occur in the anterior PD, GH-cells in the posterior. ACTH-cells are found primarily in the anterior two-thirds of the PD.
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PMID:Ontogeny and immunocytochemical differentiation of the pituitary gland in a sea turtle, Caretta caretta. 688 41

Research from a number of laboratories using of systems has shown that cells from the anterior and intermediate lobes of the pituitary gland, from hypothalamic neurons and from the placenta produce a glycoprotein with the full sequences of corticotropin, beta-lipotropin and gamma-melanotropin. These peptides in turn contain the sequences of alpha- and beta-melanotropin, CLIP, gamma-lipotropin, alpha-, beta- and gamma-endorphins and methionine-enkephalin. The precursor molecule, here called protropin, is processed by the four types of cell to give rise to different ratios of corticotropin, CLIP, beta- and gamma-lipotropin, alpha-, beta- and gamma-endorphins and alpha-, beta- and gamma-melanotropins. The physiological roles of these peptides in neurotransmission, pre- and postnatal endocrinology, mental disorders and neoplasia are only now being established.
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PMID:The intermediate lobe of the pituitary gland: introduction and background. 691 97

In the intermediate pituitary gland of Xenopus laevis, the expression levels of the prohormone pro-opiomelanocortin (POMC) can be readily manipulated. When the animal is placed on a black background, the gene for POMC is actively transcribed, whereas on a white background the gene is virtually inactive. In this study, we characterized two genes whose transcript levels in the intermediate pituitary are regulated in coordination with that for POMC. One of these codes for a protein homologous to translocon-associated protein TRAP delta, a subunit of a transmembrane protein complex located at the site where nascent secretory proteins enter the endoplasmic reticulum (ER). Both Xenopus and mice were found to express an alternatively spliced transcript that gives rise to a previously unknown version of the TRAP delta protein. The product of the second gene is a novel and highly conserved protein with structural similarity to glycoprotein gp25L, a constituent of another translocon-associated protein complex. A database search revealed the existence of a novel family of gp25L-related proteins whose members occur throughout the animal kingdom. Together, our data imply that (i) the group of ER proteins surrounding translocating polypeptide chains may be far more complex than previously expected, and (ii) a number of the accessory components of the translocon participate in early steps of prohormone biosynthesis.
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PMID:Translocon-associated protein TRAP delta and a novel TRAP-like protein are coordinately expressed with pro-opiomelanocortin in Xenopus intermediate pituitary. 749 14

We used a nonisotopic in situ hybridization (ISH) method to investigate the expression of pituitary hormone, including glycoprotein hormone mRNAs in 17 somatotrophic and four lactotrophic adenomas. Our ISH studies of lactotrophic adenomas showed that their hormonal gene expression was confined to prolactin, whereas those of somatotrophic adenomas showed that some of them expressed plurihormonal genes. In some somatotrophic adenomas that were immunohistochemically negative for pituitary hormones, positive reactions, mainly for adrenocorticotropic hormone (ACTH), follicle-stimulating hormone beta subunit (FSH beta), and luteinizing hormone beta subunit (LH beta) mRNAs, were observed in our ISH studies. These results suggest that some somatotrophic adenomas may originate from plurihormonal primordial stem cells, which we have presumed serve as precursors for various hormone-expressing cells. It is unclear why some somatotrophic adenomas derived from plurihormonal primordial stem cells manifest clinically only as the acromegalic hyperfunction syndrome or gigantism. Additional translational factors or some other somatic mutations may play important roles in the clinical manifestations of such adenomas. In conclusion, some somatotrophic adenomas appear to be derived from plurihormonal primordial stem cells, whereas lactotrophic adenomas are well differentiated tumors that originate from lactotrophic cells, which represent the final stage of acidophilic cell line differentiation.
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PMID:Expression of plurihormonal mRNAs in somatotrophic adenomas detected using a nonisotopic in situ hybridization method: comparison with lactotrophic adenomas. 789 Feb 77

Differential expression of glycosyltransferases has the potential to generate functionally distinct glycoforms of otherwise identical proteins. We have previously demonstrated the presence of unique oligosaccharides terminating with GalNAc-4-SO4 on the pituitary glycoproteins lutropin (LH), thyroid stimulating hormone (TSH), and pro-opiomelanocortin (POMC). A glycoprotein hormone:GalNAc-transferase and a GalNAc-4-sulfotransferase are present in the pituitary and can account for the synthesis of these unique oligosaccharides on specific glycoproteins. Both transferases are coordinately expressed in a number of tissues in addition to pituitary, including submaxillary gland, lacrimal gland, and kidney, suggesting that additional glycoproteins bearing oligosaccharides terminating with GalNAc-4-SO4 are synthesized in these tissues. In this study we show that while the glycoprotein hormone:GalNAc-transferase and the GalNAc-4-sulfotransferase are coordinately expressed in bovine submaxillary gland, the GalNAc-transferase is expressed in the parotid gland in the absence of the GalNAc-4-sulfotransferase. The relative expression of these two transferases in submaxillary and parotid glands correlates with the presence of unique Asn-linked oligosaccharides on carbonic anhydrase VI (CA VI) synthesized in each of these tissues. The majority of Asn-linked oligosaccharides on CA VI synthesized in submaxillary gland terminate with GalNAc-4-SO4. In contrast, CA VI which is synthesized in bovine parotid gland bears oligosaccharides which terminate predominantly with beta 1,4-linked GalNAc which is not sulfated. The presence of different terminal residues on the Asn-linked oligosaccharides of submaxillary and parotid CA VI thus correlates with the complement of transferases in these glands and suggests differing biological roles for submaxillary and parotid CA VI.
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PMID:Differential expression of GalNAc-4-sulfotransferase and GalNAc-transferase results in distinct glycoforms of carbonic anhydrase VI in parotid and submaxillary glands. 789 Jul 28

We used 35S-labeled oligonucleotides and cRNAs (riboprobes) to detect the temporal order and spatial pattern of anterior pituitary hormone gene expression in (B6CBF1 x B6CBF1)F2 fetal mice from embryonic Day 9.5 (E9.5) to postnatal Day 1 (P1). Pro-opiomelanocortin (POMC) mRNA was expressed in the basal diencephalon on Day E10.5, in the ventromedial zone of the pars distalis on Day E12.5, and in the pars intermedia on Day E14.5. The common alpha-glycoprotein subunit (alpha-GSU) mRNA first appeared in the anterior wall of Rathke's pouch on Day E11.5 and extended to the pars tuberalis and ventromedial zone of the pars distalis on Day E12.5. Thyroid-stimulating hormone-beta (TSH beta) subunit mRNA was expressed initially in both the pas tuberalis and ventromedial pars distalis on Day E14.5, with an identical spatial distribution to alpha-GSU at the time. In contrast, luteinizing hormone-beta (LH beta) subunit and follicle-stimulating hormone beta (FSH beta) subunit mRNAs were detected initially only in the ventromedial pars distalis on Days E16.5 and E17.5, respectively, in an identical distribution to each other. POMC-, alpha-GSU-, TSH beta, LH beta-, and FSH beta-positive cells within the pars distalis all increased in number and autoradiographic signal with differing degrees of spatial expansion posteriorly, laterally, and dorsally up to Day P1. POMC expression was typically the most intense and extended circumferentially to include the entire lateral and dorsal surfaces of the pars distalis. The expression of both growth hormone (GH) and prolactin (PRL) started coincidentally on Day E15.5. However PRL cells localized in the ventromedial area similarly to POMC and the glycoprotein hormone subunits, whereas GH cells were found initially in a more lateral and central distribution within the lobes of the pars distalis. Somatotrophs increased dramatically in number and autoradiographic signal, extending throughout the pars distalis except for the most peripheral layer of cells on Day E17.5. Mammotrophs also increased in number but less abundantly than somatotrophs, and PRL expression remained more confined to central-medial and ventrolateral areas of the pars distalis up to Day P1. These data demonstrate distinctive patterns of expression for each of the major anterior pituitary hormone genes during development of the mouse pituitary gland and suggest that different groups of committed cells are the immediate precursors to the terminally differentiated hormone-secreting cell types.
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PMID:In situ hybridization analysis of anterior pituitary hormone gene expression during fetal mouse development. 802 30

Twenty-five pituitary adenomas were analyzed for expression of various chromogranin/secretogranin (Cg/Sg) messenger RNA (mRNA) transcripts by in situ hybridization (ISH). An additional five adenomas were also analyzed by Northern hybridization. Immunohistochemical staining for CgA and for SgIV (with monoclonal antibody HISL-19) was also performed. Most prolactin and adrenocorticotropin adenomas did not express CgA mRNA or protein, whereas growth hormone (GH) tumors had low to moderate amounts of CgA mRNA by Northern and in situ hybridization analyses and were focally positive for CgA protein. CgB, SgII, SgIII, and SgV mRNA transcripts were present in most adenomas, and SgIV protein was detected in all groups of tumors. A GH and a null cell adenoma cultured for 7 days also expressed CgA/Sg mRNA transcripts and protein. Paraffin sections of some adenomas that were negative for CgA protein had detectable CgA mRNA by in situ hybridization analysis. These results indicate that CgA mRNA and protein are more commonly expressed in glycoprotein hormone-producing tumors compared with other types of pituitary adenomas and that ISH for CgA may detect the mRNA transcripts for CgA even when CgA protein is not detected by immunohistochemistry.
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PMID:Analysis of chromogranin/secretogranin messenger RNAs in human pituitary adenomas. 816 54

The rdw rat (gene symbol: rdw) with hereditary dwarfism has been shown immunohistochemically to have subnormal numbers not only of GH- but also of prolactin- and thyrotrophin-positive cells. To characterize the dwarfism of this strain, the expression of pituitary hormone mRNAs was examined by Northern hybridization. The pituitary gland in the rdw rat expressed 30-100 times less GH and prolactin mRNAs than normal controls, whereas mRNAs for pro-opiomelanocortin and the alpha subunit of rat glycoprotein hormone revealed a significant increase. There was a non-significant difference in rat LH-beta subunit and FSH-beta subunit between normal and rdw rats. The suppressed expression of a pituitary-specific transcription factor, Pit-1, is considered to cause hereditary dwarfism in mouse strains Snell and Jackson, whose phenotypes resemble those of the rdw rat. In this study, however, no difference in mRNA expression for Pit-1 was found between rdw rats and controls. This work indicates that the rdw rat may not have the same genotype as the phenotypically similar dwarf mice, Snell, Jackson and Ames.
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PMID:Expression of mRNA coding for pituitary hormones and pituitary-specific transcription factor in the pituitary gland of the rdw rat with hereditary dwarfism. 822 39

A rat brain opioid receptor protein was isolated by binding [epsilon-biotinyl-Lys32] beta-endorphin to membranes, solubilizing the receptor-ligand (R.L) complex with deoxycholate-lysophosphatidylcholine and purifying on immobilized streptavidin and wheat germ agglutinin. The purified glycoprotein had a molecular mass of 60-70 kDa. Recovery of this protein was blocked by the nonselective opioid antagonist naloxone and the highly mu-selective agonist [D-Ala2,N-methyl-Phe4,Glyol5]-enkephalin but not by the highly delta-selective agonist [D-Pen2,4'-Cl-Phe4,D-Pen5]enkephalin when these compounds were added as competitors at the binding step. The 60-70-kDa receptor protein co-purified through the streptavidin column with 40-kDa protein recognized by anti-Gi alpha antibodies. GTP and Na+ influenced dissociation of the solubilized R.125I-L complex and elution of the receptor and G protein from streptavidin in fashions consistent with the pharmacology of mu-opioid receptors. A 23-amino acid residue sequence from the purified receptor differs at 4 positions from a similar sequence in the murine delta-opioid receptor and is encoded within a novel rat brain cDNA isolated by polymerase chain reaction with oligonucleotide primers related to the murine delta-opioid receptor gene.
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PMID:Purification and partial amino acid sequence of a mu opioid receptor from rat brain. 825 72


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