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[PMID]: 29309431 [Au] Autor: Carmalt JL; Mortazavi S; McOnie RC; Allen AL; Unniappan S [Ad] Endereço: Department of Large Animal Clinical Sciences, Western College of Veterinary Medicine, University of Saskatchewan, Saskatoon, SK, Canada. [Ti] Título: Profiles of pro-opiomelanocortin and encoded peptides, and their processing enzymes in equine pituitary pars intermedia dysfunction. [So] Source: PLoS One;13(1):e0190796, 2018. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Equine pituitary pars intermedia dysfunction (PPID) is characterized by hyperplasia of the pars intermedia (PI) melanotrophs of the pituitary gland (PG), and increased production of proopiomelanocortin (POMC). POMC is cleaved by prohormone convertase 1 (PC1) to produce adrenocorticotropic hormone (ACTH), and further processing of ACTH by PC2 to produce alpha-melanocyte stimulating hormone (α-MSH) and corticotropin-like intermediate peptide (CLIP). High plasma ACTH concentrations in horses with PPID might be related to reduced conversion of ACTH to α-MSH by PCs. The hypothesis of this study was that PC1 and PC2 expression in the pituitary gland are altered in PPID, resulting in an abnormal relative abundance of POMC derived proteins. The objectives of this study were to identify the partial sequences of equine POMC, PC1, and PC2 mRNAs; and to determine whether the expression of POMC, PC1, and PC2 mRNAs in whole pituitary extracts, and POMC-protein in the cavernous sinus blood of horses are altered in PPID. We confirmed (RT-PCR and sequencing) that the partial sequences obtained match the corresponding regions of predicted equine POMC, PC1 and PC2 sequences. The expression (quantification by RT-qPCR) of POMC, PC1 and PC2 mRNAs were found upregulated in the pituitary of horses with PPID. Plasma (measured using RIA/ELISA) ACTH and α-MSH were elevated in PPID horses. These results indicate distinct differences in gene and protein expression of POMC and its intermediates, and processing enzymes in PPID. It provides evidence to support the notion that local, pituitary-specific inadequacies in prohormone processing likely contribute to equine PPID. [Mh] Termos MeSH primário: Peptídeos/metabolismo Adeno-Hipófise Parte Intermédia/metabolismo Pró-Opiomelanocortina/metabolismo [Mh] Termos MeSH secundário: Hormônio Adrenocorticotrópico/sangue Sequência de Aminoácidos Animais Ensaio de Imunoadsorção Enzimática Cavalos Adeno-Hipófise Parte Intermédia/enzimologia Pró-Opiomelanocortina/sangue Pró-Opiomelanocortina/química Pró-Opiomelanocortina/genética Pró-Proteína Convertase 1/genética Pró-Proteína Convertase 1/metabolismo Pró-Proteína Convertase 2/genética Pró-Proteína Convertase 2/metabolismo RNA Mensageiro/metabolismo Homologia de Sequência de Aminoácidos alfa-MSH/sangue [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Peptides); 0 (RNA, Messenger); 581-05-5 (alpha-MSH); 66796-54-1 (Pro-Opiomelanocortin); 9002-60-2 (Adrenocorticotropic Hormone); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1803 [Cu] Atualização por classe: 180309 [Lr] Data última revisão: 180309 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 180109 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0190796

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[PMID]: 28355309 [Au] Autor: Gluckman TL; Mundy NI [Ad] Endereço: Department of Zoology, University of Cambridge, Downing Street, Cambridge, United Kingdom. [Ti] Título: The differential expression of MC1R regulators in dorsal and ventral quail plumages during embryogenesis: Implications for plumage pattern formation. [So] Source: PLoS One;12(3):e0174714, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Melanin pigmentation patterns are ubiquitous in animals and function in crypsis, physical protection, thermoregulation and signalling. In vertebrates, pigmentation patterns formed over large body regions as well as within appendages (hair/feathers) may be due to the differential distribution of pigment producing cells (melanocytes) and/or regulation of the melanin synthesis pathway. We took advantage of the pigmentation patterns of Japanese quail embryos (pale ventrum and patterned feathers dorsally) to explore the role of genes and their transcripts in regulating the function of the melanocortin-1-receptor (MC1R) via 1. activation: pro-opiomelanocortin (POMC), endoproteases prohormone convertase 1 (PC1) and 2 (PC2), and 2. inhibition-agouti signaling and agouti-related protein (ASIP and AGRP, respectively). Melanocytes are present in all feather follicles at both 8 and 12 days post-fertilisation (E8/E12), so differential deposition of melanocytes is not responsible for pigmentation patterns in embryonic quail. POMC transcripts expressed were a subset of those found in chicken and POMC expression within feather follicles was strong. PC1 was not expressed in feather follicles. PC2 was strongly expressed in all feather follicles at E12. ASIP transcript expression was variable and we report four novel ASIP transcripts. ASIP is strongly expressed in ventral feather follicles, but not dorsally. AGRP expression within feather follicles was weak. These results demonstrate that the pale-bellied quail phenotype probably involves inhibition of MC1R, as found previously. However, quail may require MC1R activation for eumelanogenesis in dorsal feathers which may have important implications for an understanding of colour pattern formation in vertebrates. [Mh] Termos MeSH primário: Proteínas Aviárias/genética Coturnix/genética Plumas/metabolismo Regulação da Expressão Gênica no Desenvolvimento Receptor Tipo 1 de Melanocortina/genética [Mh] Termos MeSH secundário: Proteína Agouti Sinalizadora/genética Proteína Relacionada com Agouti/genética Animais Sequência de Bases Padronização Corporal/genética Coturnix/embriologia Plumas/embriologia Perfilação da Expressão Gênica/métodos Hibridização In Situ Melaninas/metabolismo Melanócitos/metabolismo Pigmentação/genética Pró-Opiomelanocortina/genética Pró-Proteína Convertase 1/genética Pró-Proteína Convertase 2/genética Reação em Cadeia da Polimerase Via Transcriptase Reversa Homologia de Sequência do Ácido Nucleico Fatores de Tempo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Agouti Signaling Protein); 0 (Agouti-Related Protein); 0 (Avian Proteins); 0 (Melanins); 0 (Receptor, Melanocortin, Type 1); 66796-54-1 (Pro-Opiomelanocortin); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170906 [Lr] Data última revisão: 170906 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170330 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0174714

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[PMID]: 28353232 [Au] Autor: Guest PC [Ad] Endereço: Laboratory of Neuroproteomics, Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas (UNICAMP), Rua Monteiro Lobato 255 F/01, Cidade Universitária Zeferino Vaz, 13083-862, Campinas, Brazil. paulcguest@yahoo.com. [Ti] Título: Sequential Immunoprecipitation of Secretory Vesicle Proteins from Biosynthetically Labelled Cells. [So] Source: Adv Exp Med Biol;974:157-165, 2017. [Is] ISSN: 0065-2598 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Pulse radiolabelling of cells with radioactive amino acids is a common method for studying the biosynthesis of proteins. The labelled proteins can then be immunoprecipitated and analysed by electrophoresis and imaging techniques. This chapter presents a protocol for the biosynthetic labelling and immunoprecipitation of pancreatic islet proteins which are known to be affected in psychiatric disorders such as schizophrenia. [Mh] Termos MeSH primário: Imunoprecipitação/métodos Insulina/análise Ilhotas Pancreáticas/química Pró-Proteína Convertase 2/análise Vesículas Secretórias/química [Mh] Termos MeSH secundário: Especificidade de Anticorpos Cromatografia em Agarose/métodos Eletroforese/métodos Glucose/farmacologia Seres Humanos Concentração de Íons de Hidrogênio Imunoprecipitação/instrumentação Imunoadsorventes Insulina/biossíntese Ilhotas Pancreáticas/efeitos dos fármacos Ilhotas Pancreáticas/metabolismo Marcação por Isótopo/métodos Metionina/análise Pró-Proteína Convertase 2/biossíntese Vesículas Secretórias/enzimologia Radioisótopos de Enxofre/análise Ureia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Immunosorbents); 0 (Insulin); 0 (Sulfur Radioisotopes); 8W8T17847W (Urea); AE28F7PNPL (Methionine); EC 3.4.21.94 (PCSK2 protein, human); EC 3.4.21.94 (Proprotein Convertase 2); IY9XDZ35W2 (Glucose) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170928 [Lr] Data última revisão: 170928 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170330 [St] Status: MEDLINE [do] DOI: 10.1007/978-3-319-52479-5_11

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[PMID]: 27999871 [Au] Autor: Courtade JA; Wang EY; Yen P; Dai DL; Soukhatcheva G; Orban PC; Verchere CB [Ad] Endereço: Research Institute, BC Children's Hospital, 950 West 28th Avenue, Vancouver, BC, V5Z 4H4, Canada. [Ti] Título: Loss of prohormone convertase 2 promotes beta cell dysfunction in a rodent transplant model expressing human pro-islet amyloid polypeptide. [So] Source: Diabetologia;60(3):453-463, 2017 Mar. [Is] ISSN: 1432-0428 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: AIMS/HYPOTHESIS: A contributor to beta cell failure in type 2 diabetes and islet transplants is amyloid formation by aggregation of the beta cell peptide, islet amyloid polypeptide (IAPP). Similar to the proinsulin processing pathway that generates insulin, IAPP is derived from a prohormone precursor, proIAPP, which requires cleavage by prohormone convertase (PC) 1/3 and PC2 in rodent pancreatic beta cells. We hypothesised that loss of PC2 would promote beta cell death and dysfunction in a rodent model of human beta cell proIAPP overexpression. METHODS: We generated an islet transplant model wherein immune-deficient mouse models of diabetes received islets expressing amyloidogenic human proIAPP and lacking PC2, leading to restoration of normoglycaemia accompanied by increased secretion of human proIAPP. Blood glucose levels were analysed for up to 16 weeks in transplant recipients and grafts were assessed for islet amyloid and beta cell number and death. RESULTS: Hyperglycaemia (blood glucose >16.9 mmol/l) returned in 94% of recipients of islets expressing human proIAPP and lacking PC2, whereas recipients of islets that express human proIAPP and normal PC2 levels remained normoglycaemic for at least 16 weeks. Islet graft failure was accompanied by a ∼20% reduction in insulin-positive cells, yet the degree of amyloid deposition and beta cell apoptosis was similar to those of controls expressing human proIAPP with functional PC2 levels. CONCLUSIONS/INTERPRETATION: PC2 deficiency in transplanted mouse islets expressing human proIAPP promotes beta cell loss and graft failure. Our data suggest that impaired NH -terminal processing and increased secretion of human proIAPP promote beta cell failure. [Mh] Termos MeSH primário: Amiloide/metabolismo Células Secretoras de Insulina/metabolismo Pró-Proteína Convertase 2/metabolismo [Mh] Termos MeSH secundário: Amiloide/genética Animais Glicemia/metabolismo Western Blotting Seres Humanos Polipeptídeo Amiloide das Ilhotas Pancreáticas/metabolismo Transplante das Ilhotas Pancreáticas Camundongos Camundongos Endogâmicos C57BL Camundongos Knockout Camundongos SCID Proinsulina/metabolismo Pró-Proteína Convertase 1/genética Pró-Proteína Convertase 1/metabolismo Pró-Proteína Convertase 2/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amyloid); 0 (Blood Glucose); 0 (Islet Amyloid Polypeptide); 0 (pro-islet amyloid polypeptide); 9035-68-1 (Proinsulin); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170919 [Lr] Data última revisão: 170919 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161222 [St] Status: MEDLINE [do] DOI: 10.1007/s00125-016-4174-2

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[PMID]: 27837406 [Au] Autor: Maddila SC; Busch-Dienstfertig M; Stein C [Ad] Endereço: Klinik für Anästhesiologie und operative Intensivmedizin, Freie Universität Berlin, Charité Campus Benjamin Franklin, Hindenburgdamm 30, 12200, Berlin, Germany. [Ti] Título: B Lymphocytes Express Pomc mRNA, Processing Enzymes and ß-Endorphin in Painful Inflammation. [So] Source: J Neuroimmune Pharmacol;12(1):180-186, 2017 Mar. [Is] ISSN: 1557-1904 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Immune cell-derived beta-endorphin (END) and other opioid peptides elicit potent and clinically relevant inhibition of pain (analgesia) in inflamed tissue by activation of peripheral opioid receptors. Pro-opiomelanocortin (POMC) is the polypeptide precursor of END and is processed by prohormone convertases (PCs). This study aims to decipher the processing of POMC in lymphocyte subsets in a rat model of unilateral painful hindpaw inflammation. Lymphocytes, isolated from popliteal lymph nodes, were separated into B-cells, T-cells, T-helper cells and cytotoxic T-cells using magnetic cell sorting, and were examined by polymerase chain reaction, immunofluorescence and radioimmunoassay. At 2 h of inflammation, POMC exon 2-3 mRNA was mostly expressed in B- but not in T-cells. Prohormone convertase 1 (PC1) mRNA and protein were upregulated in B-cells and T-helper cells. Prohormone convertase 2 (PC2) was expressed in T- and B-cells, both in inflamed and non-inflamed lymph nodes. END was expressed in B- but not in T-cells. We conclude that POMC, its processing enzymes and END are predominantly expressed in B-lymphocytes at 2 h of paw inflammation. [Mh] Termos MeSH primário: Linfócitos B/metabolismo Dor/metabolismo Pró-Opiomelanocortina/biossíntese RNA Mensageiro/biossíntese Serina Endopeptidases/biossíntese beta-Endorfina/biossíntese [Mh] Termos MeSH secundário: Animais Linfócitos B/enzimologia Expressão Gênica Inflamação/genética Inflamação/metabolismo Masculino Dor/genética Pró-Opiomelanocortina/genética Pró-Proteína Convertase 1/biossíntese Pró-Proteína Convertase 1/genética Pró-Proteína Convertase 2/biossíntese Pró-Proteína Convertase 2/genética RNA Mensageiro/genética Ratos Ratos Wistar Serina Endopeptidases/genética beta-Endorfina/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (RNA, Messenger); 60617-12-1 (beta-Endorphin); 66796-54-1 (Pro-Opiomelanocortin); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171104 [Lr] Data última revisão: 171104 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161113 [St] Status: MEDLINE [do] DOI: 10.1007/s11481-016-9715-4

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[PMID]: 27396958 [Au] Autor: Lam WY; Becker AM; Kennerly KM; Wong R; Curtis JD; Llufrio EM; McCommis KS; Fahrmann J; Pizzato HA; Nunley RM; Lee J; Wolfgang MJ; Patti GJ; Finck BN; Pearce EL; Bhattacharya D [Ad] Endereço: Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63110, USA. [Ti] Título: Mitochondrial Pyruvate Import Promotes Long-Term Survival of Antibody-Secreting Plasma Cells. [So] Source: Immunity;45(1):60-73, 2016 07 19. [Is] ISSN: 1097-4180 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Durable antibody production after vaccination or infection is mediated by long-lived plasma cells (LLPCs). Pathways that specifically allow LLPCs to persist remain unknown. Through bioenergetic profiling, we found that human and mouse LLPCs could robustly engage pyruvate-dependent respiration, whereas their short-lived counterparts could not. LLPCs took up more glucose than did short-lived plasma cells (SLPCs) in vivo, and this glucose was essential for the generation of pyruvate. Glucose was primarily used to glycosylate antibodies, but glycolysis could be promoted by stimuli such as low ATP levels and the resultant pyruvate used for respiration by LLPCs. Deletion of Mpc2, which encodes an essential component of the mitochondrial pyruvate carrier, led to a progressive loss of LLPCs and of vaccine-specific antibodies in vivo. Thus, glucose uptake and mitochondrial pyruvate import prevent bioenergetic crises and allow LLPCs to persist. Immunizations that maximize these plasma cell metabolic properties might thus provide enduring antibody-mediated immunity. [Mh] Termos MeSH primário: Células Produtoras de Anticorpos/imunologia Glucose/metabolismo Mitocôndrias/metabolismo Plasmócitos/imunologia Ácido Pirúvico/metabolismo [Mh] Termos MeSH secundário: Animais Transporte Biológico Ativo Respiração Celular Células Cultivadas Glicosilação Seres Humanos Imunoglobulinas/biossíntese Camundongos Camundongos Endogâmicos C57BL Camundongos Knockout Pró-Proteína Convertase 2/genética Pró-Proteína Convertase 2/metabolismo Estresse Fisiológico/imunologia [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL [Nm] Nome de substância: 0 (Immunoglobulins); 8558G7RUTR (Pyruvic Acid); EC 3.4.21.94 (Pcsk2 protein, mouse); EC 3.4.21.94 (Proprotein Convertase 2); IY9XDZ35W2 (Glucose) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 171121 [Lr] Data última revisão: 171121 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160712 [St] Status: MEDLINE

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[PMID]: 27318130 [Au] Autor: Steinmetz AB; Johnson SA; Iannitelli DE; Pollonini G; Alberini CM [Ad] Endereço: Center for Neural Science, New York University, New York, NY, USA. [Ti] Título: Insulin-like growth factor 2 rescues aging-related memory loss in rats. [So] Source: Neurobiol Aging;44:9-21, 2016 Aug. [Is] ISSN: 1558-1497 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Aging is accompanied by declines in memory performance, and particularly affects memories that rely on hippocampal-cortical systems, such as episodic and explicit. With aged populations significantly increasing, the need for preventing or rescuing memory deficits is pressing. However, effective treatments are lacking. Here, we show that the level of the mature form of insulin-like growth factor 2 (IGF-2), a peptide regulated in the hippocampus by learning, required for memory consolidation and a promoter of memory enhancement in young adult rodents, is significantly reduced in hippocampal synapses of aged rats. By contrast, the hippocampal level of the immature form proIGF-2 is increased, suggesting an aging-related deficit in IGF-2 processing. In agreement, aged compared to young adult rats are deficient in the activity of proprotein convertase 2, an enzyme that likely mediates IGF-2 posttranslational processing. Hippocampal administration of the recombinant, mature form of IGF-2 rescues hippocampal-dependent memory deficits and working memory impairment in aged rats. Thus, IGF-2 may represent a novel therapeutic avenue for preventing or reversing aging-related cognitive impairments. [Mh] Termos MeSH primário: Envelhecimento/psicologia Fator de Crescimento Insulin-Like II/administração & dosagem Fator de Crescimento Insulin-Like II/fisiologia Transtornos da Memória/etiologia Transtornos da Memória/prevenção & controle Memória [Mh] Termos MeSH secundário: Animais Hipocampo/metabolismo Fator de Crescimento Insulin-Like II/deficiência Fator de Crescimento Insulin-Like II/metabolismo Masculino Memória de Curto Prazo Terapia de Alvo Molecular Pró-Proteína Convertase 2/metabolismo Processamento de Proteína Pós-Traducional Ratos Ratos Endogâmicos F344 Proteínas Recombinantes/administração & dosagem [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Recombinant Proteins); 67763-97-7 (Insulin-Like Growth Factor II); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170928 [Lr] Data última revisão: 170928 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160619 [St] Status: MEDLINE

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[PMID]: 27268986 [Au] Autor: Shimoyama S; Inoue T; Kashima M; Agata K [Ad] Endereço: Department of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan. [Ti] Título: Multiple Neuropeptide-Coding Genes Involved in Planarian Pharynx Extension. [So] Source: Zoolog Sci;33(3):311-9, 2016 Jun. [Is] ISSN: 0289-0003 [Cp] País de publicação: Japan [La] Idioma: eng [Ab] Resumo: Planarian feeding behavior involves three steps: moving toward food, extending the pharynx from their planarian's ventral side after arriving at the food, and ingesting the food through the pharynx. Although pharynx extension is a remarkable behavior, it remains unknown what neuronal cell types are involved in its regulation. To identify neurons involved in regulating pharynx extension, we quantitatively analyzed pharynx extension and sought to identify these neurons by RNA interference (RNAi) and in situ hybridization. This assay, when performed using planarians with amputation of various body parts, clearly showed that the head portion is indispensable for inducing pharynx extension. We thus tested the effects of knockdown of brain neurons such as serotonergic, GABAergic, and dopaminergic neurons by RNAi, but did not observe any effects on pharynx extension behavior. However, animals with RNAi of the Prohormone Convertase 2 (PC2, a neuropeptide processing enzyme) gene did not perform the pharynx extension behavior, suggesting the possible involvement of neuropeptide(s in the regulation of pharynx extension. We screened 24 neuropeptide-coding genes, analyzed their functions by RNAi using the pharynx extension assay system, and identified at least five neuropeptide genes involved in pharynx extension. These was expressed in different cells or neurons, and some of them were expressed in the brain, suggesting complex regulation of planarian feeding behavior by the nervous system. [Mh] Termos MeSH primário: Comportamento Alimentar/fisiologia Neuropeptídeos/genética Planárias/fisiologia [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Perfilação da Expressão Gênica Regulação da Expressão Gênica Hibridização In Situ Neurônios/fisiologia Neuropeptídeos/química Faringe/metabolismo Planárias/genética Pró-Proteína Convertase 2/genética Interferência de RNA [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Neuropeptides); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1612 [Cu] Atualização por classe: 161230 [Lr] Data última revisão: 161230 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160609 [St] Status: MEDLINE [do] DOI: 10.2108/zs150170

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[PMID]: 27208618 [Au] Autor: Lutfy K; Parikh D; Lee DL; Liu Y; Ferrini MG; Hamid A; Friedman TC [Ad] Endereço: Department of Pharmaceutical Sciences, College of Pharmacy, Western University of Health Sciences, Pomona, CA 91766, USA; Division of Endocrinology, Diabetes and Metabolism, Department of Internal Medicine, Charles R. Drew University of Medicine and Sciences, Los Angeles, CA 90059, USA. Electronic a [Ti] Título: Prohormone convertase 2 (PC2) null mice have increased mu opioid receptor levels accompanied by altered morphine-induced antinociception, tolerance and dependence. [So] Source: Neuroscience;329:318-25, 2016 Aug 04. [Is] ISSN: 1873-7544 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Chronic morphine treatment increases the levels of prohormone convertase 2 (PC2) in brain regions involved in nociception, tolerance and dependence. Thus, we tested if PC2 null mice exhibit altered morphine-induced antinociception, tolerance and dependence. PC2 null mice and their wild-type controls were tested for baseline hot plate latency, injected with morphine (1.25-10mg/kg) and tested for antinociception 30min later. For tolerance studies, mice were tested in the hot plate test before and 30min following morphine (5mg/kg) on day 1. Mice then received an additional dose so that the final dose of morphine was 10mg/kg on this day. On days 2-4, mice received additional doses of morphine (20, 40 and 80mg/kg on days 1, 2, 3, and 4, respectively). On day 5, mice were tested in the hot plate test before and 30min following morphine (5mg/kg). For withdrawal studies, mice were treated with the escalating doses of morphine (10, 20, 40 and 80mg/kg) for 4days, implanted with a morphine pellet on day 5 and 3 days later injected with naloxone (1mg/kg) and signs of withdrawal were recorded. Morphine dose-dependently induced antinociception and the magnitude of this response was greater in PC2 null mice. Tolerance to morphine was observed in wild-type mice and this phenomenon was blunted in PC2 null mice. Withdrawal signs were also reduced in PC2 null mice. Immunohistochemical studies showed up-regulation of the mu opioid receptor (MOP) protein expression in the periaqueductal gray area, ventral tegmental area, lateral hypothalamus, medial hypothalamus, nucleus accumbens, and somatosensory cortex in PC2 null mice. Likewise, naloxone specific binding was increased in the brains of these mice compared to their wild-type controls. The results suggest that the PC2-derived peptides may play a functional role in morphine-induced antinociception, tolerance and dependence. Alternatively, lack of opioid peptides led to up-regulation of the MOP and altered morphine-induced antinociception, tolerance and dependence. [Mh] Termos MeSH primário: Analgésicos Opioides/farmacologia Dependência de Morfina/metabolismo Morfina/farmacologia Dor Nociceptiva/tratamento farmacológico Pró-Proteína Convertase 2/deficiência Receptores Opioides mu/metabolismo [Mh] Termos MeSH secundário: Animais Encéfalo/efeitos dos fármacos Encéfalo/metabolismo Encéfalo/patologia Relação Dose-Resposta a Droga Tolerância a Medicamentos/fisiologia Masculino Camundongos da Linhagem 129 Camundongos Endogâmicos C57BL Camundongos Knockout Dependência de Morfina/patologia Naloxona/farmacologia Antagonistas de Entorpecentes/farmacologia Dor Nociceptiva/metabolismo Pró-Proteína Convertase 2/genética Síndrome de Abstinência a Substâncias/metabolismo Síndrome de Abstinência a Substâncias/patologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Analgesics, Opioid); 0 (Narcotic Antagonists); 0 (Receptors, Opioid, mu); 36B82AMQ7N (Naloxone); 76I7G6D29C (Morphine); EC 3.4.21.94 (Pcsk2 protein, mouse); EC 3.4.21.94 (Proprotein Convertase 2) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170804 [Lr] Data última revisão: 170804 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160522 [St] Status: MEDLINE

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[PMID]: 26757816 [Au] Autor: Kumar DP; Asgharpour A; Mirshahi F; Park SH; Liu S; Imai Y; Nadler JL; Grider JR; Murthy KS; Sanyal AJ [Ad] Endereço: Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, Virginia 23298 and. [Ti] Título: Activation of Transmembrane Bile Acid Receptor TGR5 Modulates Pancreatic Islet α Cells to Promote Glucose Homeostasis. [So] Source: J Biol Chem;291(13):6626-40, 2016 Mar 25. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The physiological role of the TGR5 receptor in the pancreas is not fully understood. We previously showed that activation of TGR5 in pancreatic ß cells by bile acids induces insulin secretion. Glucagon released from pancreatic α cells and glucagon-like peptide 1 (GLP-1) released from intestinal L cells regulate insulin secretion. Both glucagon and GLP-1 are derived from alternate splicing of a common precursor, proglucagon by PC2 and PC1, respectively. We investigated whether TGR5 activation in pancreatic α cells enhances hyperglycemia-induced PC1 expression thereby releasing GLP-1, which in turn increases ß cell mass and function in a paracrine manner. TGR5 activation augmented a hyperglycemia-induced switch from glucagon to GLP-1 synthesis in human and mouse islet α cells by GS/cAMP/PKA/cAMP-response element-binding protein-dependent activation of PC1. Furthermore, TGR5-induced GLP-1 release from α cells was via an Epac-mediated PKA-independent mechanism. Administration of the TGR5 agonist, INT-777, to db/db mice attenuated the increase in body weight and improved glucose tolerance and insulin sensitivity. INT-777 augmented PC1 expression in α cells and stimulated GLP-1 release from islets of db/db mice compared with control. INT-777 also increased pancreatic ß cell proliferation and insulin synthesis. The effect of TGR5-mediated GLP-1 from α cells on insulin release from islets could be blocked by GLP-1 receptor antagonist. These results suggest that TGR5 activation mediates cross-talk between α and ß cells by switching from glucagon to GLP-1 to restore ß cell mass and function under hyperglycemic conditions. Thus, INT-777-mediated TGR5 activation could be leveraged as a novel way to treat type 2 diabetes mellitus. [Mh] Termos MeSH primário: Ácidos Cólicos/farmacologia Diabetes Mellitus Experimental/genética Peptídeo 1 Semelhante ao Glucagon/secreção Glucose/metabolismo Comunicação Parácrina/genética Receptores Acoplados a Proteínas-G/agonistas [Mh] Termos MeSH secundário: Animais Derivados de Benzeno/farmacologia Benzenossulfonatos/farmacologia Linhagem Celular Proteínas Quinases Dependentes de AMP Cíclico/genética Proteínas Quinases Dependentes de AMP Cíclico/metabolismo Diabetes Mellitus Experimental/tratamento farmacológico Diabetes Mellitus Experimental/metabolismo Diabetes Mellitus Experimental/patologia Diabetes Mellitus Tipo 2/genética Diabetes Mellitus Tipo 2/metabolismo Diabetes Mellitus Tipo 2/patologia Estrenos/farmacologia Regulação da Expressão Gênica Peptídeo 1 Semelhante ao Glucagon/biossíntese Peptídeo 1 Semelhante ao Glucagon/genética Células Secretoras de Glucagon/efeitos dos fármacos Células Secretoras de Glucagon/metabolismo Células Secretoras de Glucagon/patologia Homeostase/efeitos dos fármacos Seres Humanos Resistência à Insulina Células Secretoras de Insulina/efeitos dos fármacos Células Secretoras de Insulina/metabolismo Células Secretoras de Insulina/patologia Masculino Camundongos Camundongos Endogâmicos C57BL Camundongos Transgênicos Pró-Proteína Convertase 1/genética Pró-Proteína Convertase 1/metabolismo Pró-Proteína Convertase 2/genética Pró-Proteína Convertase 2/metabolismo Pirrolidinonas/farmacologia Receptores Acoplados a Proteínas-G/genética Receptores Acoplados a Proteínas-G/metabolismo Transdução de Sinais Sulfonas/farmacologia [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL [Nm] Nome de substância: 0 (4,4,',4'',4'''-(carbonylbis(imino-5,1,3-benzenetriylbis(carbonylimino)))tetrakis(benzene-1,3-disulfonate)); 0 (6alpha-ethyl-23(S)-methylcholic acid); 0 (Benzene Derivatives); 0 (Benzenesulfonates); 0 (Cholic Acids); 0 (ESI-05); 0 (Estrenes); 0 (Gpbar1 protein, mouse); 0 (Pyrrolidinones); 0 (Receptors, G-Protein-Coupled); 0 (Sulfones); 112648-68-7 (1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dione); 89750-14-1 (Glucagon-Like Peptide 1); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 3.4.21.93 (Proprotein Convertase 1); EC 3.4.21.94 (Proprotein Convertase 2); IY9XDZ35W2 (Glucose) [Em] Mês de entrada: 1608 [Cu] Atualização por classe: 170403 [Lr] Data última revisão: 170403 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160114 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M115.699504

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