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[Au] Autor:Mulley JF; Hargreaves AD; Hegarty MJ; Heller RS; Swain MT
[Ad] Endereço:School of Biological Sciences, Bangor University, Brambell Building, Deiniol Road, Bangor, Gwynedd LL57 2UW, United Kingdom.
[Ti] Título:Transcriptomic analysis of the lesser spotted catshark (Scyliorhinus canicula) pancreas, liver and brain reveals molecular level conservation of vertebrate pancreas function.
[So] Source:BMC Genomics;15:1074, 2014 Dec 06.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Understanding the evolution of the vertebrate pancreas is key to understanding its functions. The chondrichthyes (cartilaginous fish such as sharks and rays) have often been suggested to possess the most ancient example of a distinct pancreas with both hormonal (endocrine) and digestive (exocrine) roles. The lack of genetic, genomic and transcriptomic data for cartilaginous fish has hindered a more thorough understanding of the molecular-level functions of the chondrichthyan pancreas, particularly with respect to their "unusual" energy metabolism (where ketone bodies and amino acids are the main oxidative fuel source) and their paradoxical ability to both maintain stable blood glucose levels and tolerate extensive periods of hypoglycemia. In order to shed light on some of these processes, we carried out the first large-scale comparative transcriptomic survey of multiple cartilaginous fish tissues: the pancreas, brain and liver of the lesser spotted catshark, Scyliorhinus canicula. RESULTS: We generated a mutli-tissue assembly comprising 86,006 contigs, of which 44,794 were assigned to a particular tissue or combination of tissues based on mapping of sequencing reads. We have characterised transcripts encoding genes involved in insulin regulation, glucose sensing, transcriptional regulation, signaling and digestion, as well as many peptide hormone precursors and their receptors for the first time. Comparisons to mammalian pancreas transcriptomes reveals that mechanisms of glucose sensing and insulin regulation used to establish and maintain a stable internal environment are conserved across jawed vertebrates and likely pre-date the vertebrate radiation. Conservation of pancreatic hormones and genes encoding digestive proteins support the single, early evolution of a distinct pancreatic gland with endocrine and exocrine functions in jawed vertebrates. In addition, we demonstrate that chondrichthyes lack pancreatic polypeptide (PP) and that reports of PP in the literature are likely due cross-reaction with PYY and/or NPY in the pancreas. A three hormone islet organ is therefore the ancestral jawed vertebrate condition, later elaborated upon only in the tetrapod lineage. CONCLUSIONS: The cartilaginous fish are a great untapped resource for the reconstruction of patterns and processes of vertebrate evolution and new approaches such as those described in this paper will greatly facilitate their incorporation into the rank of "model organism".
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Cação (Peixe)/genética
Cação (Peixe)/fisiologia
Perfilação da Expressão Gênica
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Evolução Molecular
Genes Homeobox/genética
Repetições de Microssatélites/genética
Dados de Sequência Molecular
Especificidade de Órgãos
Receptores de Hormônios Pancreáticos/genética
Transdução de Sinais/genética
Fatores de Transcrição/metabolismo
[Nm] Nome de substância:
0 (Insulin); 0 (Receptors, Pancreatic Hormone); 0 (Transcription Factors); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141207
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2164-15-1074

  2 / 5 MEDLINE  
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[Au] Autor:Barth SW; Riediger T; Lutz TA; Rechkemmer G
[Ad] Endereço:Institute of Nutritional Physiology, Federal Research Centre of Nutrition, Haid und Neu Strasse 9, D-76131, Karlsruhe, Germany.
[Ti] Título:Differential effects of amylin and salmon calcitonin on neuropeptide gene expression in the lateral hypothalamic area and the arcuate nucleus of the rat.
[So] Source:Neurosci Lett;341(2):131-4, 2003 May 01.
[Is] ISSN:0304-3940
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The pancreatic peptide hormone amylin (AMY) and the AMY receptor agonist salmon calcitonin (sCT) reduce short-term food intake in rats primarily by activating neurons located in the circumventricular area postrema. In the present study we analyzed the involvement of (an)orexigenic neuropeptides expressed in the lateral hypothalamic area (LHA) and in the arcuate nucleus in mediating the AMY and sCT-induced suppression of food intake. By using semiquantitative in situ hybridization 120 min after intraperitoneal injection of AMY or sCT (50 microgram/kg), orexin mRNA levels were decreased in LHA by AMY or sCT treatment. Moreover, sCT significantly suppressed the orexigenic melanin concentrating hormone in LHA, whereas mRNA levels of neuropeptide Y, cocaine and amphetamine regulated transcript, agouti-gene-related protein and proopiomelanocortin were unaffected by either treatment. In conclusion, the anorexigenic effect of AMY/sCT might be mediated by the observed reduced expression of orexigenic neuropeptides in the LHA.
[Mh] Termos MeSH primário: Amiloide/farmacologia
Núcleo Arqueado do Hipotálamo/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Região Hipotalâmica Lateral/efeitos dos fármacos
Peptídeos e Proteínas de Sinalização Intracelular
[Mh] Termos MeSH secundário: Proteína Relacionada com Agouti
Núcleo Arqueado do Hipotálamo/metabolismo
Proteínas de Transporte/genética
Ingestão de Alimentos/efeitos dos fármacos
Região Hipotalâmica Lateral/metabolismo
Hormônios Hipotalâmicos/genética
Hibridização In Situ/métodos
Peptídeos e Proteínas de Sinalização Intercelular
Polipeptídeo Amiloide das Ilhotas Pancreáticas
Proteínas do Tecido Nervoso/metabolismo
Neuropeptídeo Y/genética
Sondas de Oligonucleotídeos
Receptores de Orexina
Fragmentos de Peptídeos/farmacologia
Hormônios Hipofisários/genética
RNA Mensageiro/biossíntese
Ratos Wistar
Receptores Acoplados a Proteínas-G
Receptores de Neuropeptídeos
Receptores de Hormônios Pancreáticos/antagonistas & inibidores
[Nm] Nome de substância:
0 (Agouti-Related Protein); 0 (Amyloid); 0 (Anti-Ulcer Agents); 0 (Carrier Proteins); 0 (Hypothalamic Hormones); 0 (Intercellular Signaling Peptides and Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Islet Amyloid Polypeptide); 0 (Melanins); 0 (Nerve Tissue Proteins); 0 (Neuropeptide Y); 0 (Neuropeptides); 0 (Oligonucleotide Probes); 0 (Orexin Receptors); 0 (Orexins); 0 (Peptide Fragments); 0 (Pituitary Hormones); 0 (Proteins); 0 (RNA, Messenger); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Neuropeptide); 0 (Receptors, Pancreatic Hormone); 0 (cocaine- and amphetamine-regulated transcript protein); 66796-54-1 (Pro-Opiomelanocortin); 67382-96-1 (melanin-concentrating hormone); 9007-12-9 (Calcitonin)
[Em] Mês de entrada:0305
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030411
[St] Status:MEDLINE

  3 / 5 MEDLINE  
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[Au] Autor:Bouchal J; Kolár Z; Mad'arová J; Hlobilková A; von Angerer E
[Ad] Endereço:Laboratory of Molecular Pathology, CMBM and Institute of Pathology, Faculty of Medicine, Palacký University, Olomouc, Czech Republic.
[Ti] Título:The effects of natural ligands of hormone receptors and their antagonists on telomerase activity in the androgen sensitive prostatic cancer cell line LNCaP.
[So] Source:Biochem Pharmacol;63(6):1177-81, 2002 Mar 15.
[Is] ISSN:0006-2952
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The effects of the 17beta-estradiol, dihydrotestosterone and hormone antagonists tamoxifen and bicalutamide on telomerase activity and expression of cell cycle related proteins in the androgen-sensitive prostatic cancer cell line LNCaP were studied. The cell line was grown in RPMI supplemented with 2.5% charcoal-stripped FBS for 72 hr. The IC(50) of tamoxifen and bicalutamide and the optimal stimulatory concentrations of 17beta-estradiol and dihydrotestosterone were determined by means of the cell-viability assay, the activity of telomerase was measured by the telomere repeat amplification protocol (TRAP) and the expression of proteins was analysed by the Western blot technique. 17beta-estradiol stimulated cell growth more effectively than dihydrotestosterone whereas hormone antagonists tamoxifen and bicalutamide caused a significant decrease in cell viability. The treatment of cells by a combination of low doses of 17 beta-estradiol and dihydrotestosterone stimulated cells stronger than treatment by a single hormone. Only 17beta-estradiol, in concentration of 10nM, increased strongly the expression of p21(Waf1/Cip1) and increased slightly telomerase activity in the LNCaP cells. 50 microM of bicalutamide down-regulated the levels of the androgen receptor, the proliferating cell nuclear antigen and telomerase activity, and up-regulated the expression of p27(Kip1). We hereby describe the first observation of the influence of bicalutamide on telomerase activity and a positive correlation between the effect of 17beta-estradiol and the induction of both the endogenous cyclin-dependent kinase inhibitor, p21(Waf1/Cip1), and telomerase activity in a prostatic cancer cell line LNCaP. These findings can shed a new light on the steroid-signaling pathway in prostate cancer cells.
[Mh] Termos MeSH primário: Di-Hidrotestosterona/farmacologia
Neoplasias da Próstata/enzimologia
Receptores de Hormônios Pancreáticos/antagonistas & inibidores
[Mh] Termos MeSH secundário: Androgênios/metabolismo
Antineoplásicos Hormonais/farmacologia
Seres Humanos
Neoplasias da Próstata/patologia
Telomerase/efeitos dos fármacos
Células Tumorais Cultivadas
[Nm] Nome de substância:
0 (Androgens); 0 (Antineoplastic Agents, Hormonal); 0 (Ligands); 0 (Receptors, Pancreatic Hormone); 08J2K08A3Y (Dihydrotestosterone); 094ZI81Y45 (Tamoxifen); 4TI98Z838E (Estradiol); EC (Telomerase)
[Em] Mês de entrada:0206
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020405
[St] Status:MEDLINE

  4 / 5 MEDLINE  
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[Au] Autor:Gehlert DR; Schober DA; Gackenheimer SL; Beavers L; Gadski R; Lundell I; Larhammar D
[Ad] Endereço:Lilly Neuroscience, Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, IN 46285, USA.
[Ti] Título:[125I]Leu31, Pro34-PYY is a high affinity radioligand for rat PP1/Y4 and Y1 receptors: evidence for heterogeneity in pancreatic polypeptide receptors.
[So] Source:Peptides;18(3):397-401, 1997.
[Is] ISSN:0196-9781
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cloned receptors for the PP-fold peptides are subdivided into Y1, Y2, PP1/Y4, Y5 and Y6. NPY and PYY have similar affinity for Y1, Y2, Y5 and Y6 receptors while PP has highest affinity for PP1. Pro34-substituted analogs of NPY and PYY have selectivity for Y1 and Y1-like receptors over Y2 receptors. In the present study, we found the putative Y1-selective radioligand, [125I]Leu31, Pro34-PYY, also binds with high affinity to the rat PP1 receptor in cell lines expressing the receptor. However, in rat brain sections, [125I]Leu31, Pro34-PYY does not appear to bind to the interpeduncular nucleus, a brain region containing a high density of [125I]-bPP binding sites. Therefore, it appears there is additional heterogeneity in receptors recognizing PP.
[Mh] Termos MeSH primário: Hormônios Gastrointestinais/metabolismo
Neuropeptídeo Y/análogos & derivados
Receptores de Neuropeptídeo Y/metabolismo
Receptores de Hormônios Pancreáticos/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Radioisótopos do Iodo
Neuropeptídeo Y/química
Neuropeptídeo Y/metabolismo
Neuropeptídeo Y/fisiologia
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/metabolismo
Receptores de Neuropeptídeo Y/química
Receptores de Hormônios Pancreáticos/química
Proteínas Recombinantes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gastrointestinal Hormones); 0 (Iodine Radioisotopes); 0 (Ligands); 0 (Neuropeptide Y); 0 (Peptide Fragments); 0 (Receptors, Neuropeptide Y); 0 (Receptors, Pancreatic Hormone); 0 (Recombinant Proteins); 0 (neuropeptide Y-Y1 receptor); 0 (peptide YY, iodo-Leu(34)-Pro(34)-); 125580-28-1 (neuropeptide Y, Leu(31)-Pro(34)-)
[Em] Mês de entrada:9707
[Cu] Atualização por classe:051117
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:970101
[St] Status:MEDLINE

  5 / 5 MEDLINE  
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[Au] Autor:Moens K; Heimberg H; Flamez D; Huypens P; Quartier E; Ling Z; Pipeleers D; Gremlich S; Thorens B; Schuit F
[Ad] Endereço:Diabetes Research Center, Vrije Universiteit Brussel, Belgium.
[Ti] Título:Expression and functional activity of glucagon, glucagon-like peptide I, and glucose-dependent insulinotropic peptide receptors in rat pancreatic islet cells.
[So] Source:Diabetes;45(2):257-61, 1996 Feb.
[Is] ISSN:0012-1797
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rat pancreatic alpha- and beta-cells are critically dependent on hormonal signals generating cyclic AMP (cAMP) as a synergistic messenger for nutrient-induced hormone release. Several peptides of the glucagon-secretin family have been proposed as physiological ligands for cAMP production in beta-cells, but their relative importance for islet function is still unknown. The present study shows expression at the RNA level in beta-cells of receptors for glucagon, glucose-dependent insulinotropic polypeptide (GIP), and glucagon-like peptide I(7-36) amide (GLP-I), while RNA from islet alpha-cells hybridized only with GIP receptor cDNA. Western blots confirmed that GLP-I receptors were expressed in beta-cells and not in alpha-cells. Receptor activity, measured as cellular cAMP production after exposing islet beta-cells for 15 min to a range of peptide concentrations, was already detected using 10 pmol/l GLP-I and 50 pmol/l GIP but required 1 nmol/l glucagon. EC50 values of GLP-I- and GIP-induced cAMP formation were comparable (0.2 nmol/l) and 45-fold lower than the EC50 of glucagon (9 nmol/l). Maximal stimulation of cAMP production was comparable for the three peptides. In purified alpha-cells, 1 nmol/l GLP-I failed to increase cAMP levels, while 10 pmol/l to 10 nmol/l GIP exerted similar stimulatory effects as in beta-cells. In conclusion, these data show that stimulation of glucagon, GLP-I, and GIP receptors in rat beta-cells causes cAMP production required for insulin release, while adenylate cyclase in alpha-cells is positively regulated by GIP.
[Mh] Termos MeSH primário: Polipeptídeo Inibidor Gástrico/metabolismo
Fragmentos de Peptídeos/metabolismo
Precursores de Proteínas/metabolismo
Receptores dos Hormônios Gastrointestinais/metabolismo
Receptores de Glucagon/metabolismo
Receptores de Hormônios Pancreáticos/metabolismo
[Mh] Termos MeSH secundário: Adenilil Ciclases/metabolismo
AMP Cíclico/metabolismo
Expressão Gênica
Peptídeo 1 Semelhante ao Glucagon
Receptor do Peptídeo Semelhante ao Glucagon 1
Ilhotas Pancreáticas/metabolismo
RNA Mensageiro/genética
Ratos Wistar
Transdução de Sinais
[Nm] Nome de substância:
0 (Glp1r protein, rat); 0 (Glucagon-Like Peptide-1 Receptor); 0 (Peptide Fragments); 0 (Protein Precursors); 0 (RNA, Messenger); 0 (Receptors, Gastrointestinal Hormone); 0 (Receptors, Glucagon); 0 (Receptors, Pancreatic Hormone); 0 (gastric inhibitory polypeptide receptor); 59392-49-3 (Gastric Inhibitory Polypeptide); 89750-14-1 (Glucagon-Like Peptide 1); 9007-92-5 (Glucagon); E0399OZS9N (Cyclic AMP); EC (Adenylyl Cyclases)
[Em] Mês de entrada:9602
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:960201
[St] Status:MEDLINE

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