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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]:29175325
[Au] Autor:Zou S; Lang T; Zhang B; Huang K; Gong L; Luo H; Xu W; He X
[Ad] Endereço:Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China; Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural
[Ti] Título:Fatty acid oxidation alleviates the energy deficiency caused by the loss of MPC1 in MPC1 mice.
[So] Source:Biochem Biophys Res Commun;495(1):1008-1013, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pyruvate is a central substrate in energy metabolism, paramount to carbohydrate, fat, and amino acid catabolic and anabolic pathways. Mitochondrial pyruvate carrier 1(MPC1) is one important component of the complex that facilitates mitochondrial pyruvate import. Complete MPC1 deficiency is a serious concern, and has been shown to result in embryonic lethality in mice. The study outlined in this paper generated one mouse line with the MPC1 protein part deficiency by using the CRISPR/Cas9 system. Clinical observations, body weight and organ/tissue weight, gas exchange, cold-stimulation, blood parameters, as well as histopathology analysis were analyzed to evaluate potential physiological abnormalities caused by MPC1 deficiency. Results indicate that MPC1 mice experienced a change in important clinical criteria such as low body weight, decreased movement, and low body shell temperature, few adipose accumulate. The mice show significant difference in some blood parameters including apo-B100, apo-A1, HDL, glucagon, insulin. However these changes alleviated while being fed with the HFD, which provided metabolites to sustain the TCA cycle and body development. The MPC1 mice may employ fatty acid oxidation to meet their bioenergetic demands. This study suggests that inhibition of MPC1 activity can boost fatty acid oxidation to provide sufficient energy to the body. This work promotes further studies regarding the interplay between carbohydrate and fat metabolism.
[Mh] Termos MeSH primário: Peso Corporal/fisiologia
Metabolismo Energético/fisiologia
Ácidos Graxos/metabolismo
Consumo de Oxigênio/fisiologia
Pró-Proteína Convertase 1/metabolismo
Ácido Pirúvico/metabolismo
[Mh] Termos MeSH secundário: Animais
Resposta ao Choque Frio/fisiologia
Ativação Enzimática
Masculino
Camundongos
Camundongos Knockout
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 8558G7RUTR (Pyruvic Acid); EC 3.4.21.93 (Pcsk1 protein, mouse); EC 3.4.21.93 (Proprotein Convertase 1)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


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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]: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]:27998058
[Au] Autor:Oliveros A; Starski P; Lindberg D; Choi S; Heppelmann CJ; Dasari S; Choi DS
[Ad] Endereço:Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic , Rochester, Minnesota 55905, United States.
[Ti] Título:Label-Free Neuroproteomics of the Hippocampal-Accumbal Circuit Reveals Deficits in Neurotransmitter and Neuropeptide Signaling in Mice Lacking Ethanol-Sensitive Adenosine Transporter.
[So] Source:J Proteome Res;16(4):1445-1459, 2017 Apr 07.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The neural circuit of the dorsal hippocampus (dHip) and nucleus accumbens (NAc) contributes to cue-induced learning and addictive behaviors, as demonstrated by the escalation of ethanol-seeking behaviors observed following deletion of the adenosine equilibrative nucleoside transporter 1 (ENT1 ) in mice. Here we perform quantitative LC-MS/MS neuroproteomics in the dHip and NAc of ENT1 mice. Using Ingenuity Pathway Analysis, we identified proteins associated with increased long-term potentiation, ARP2/3-mediated actin cytoskeleton signaling and protein expression patterns suggesting deficits in glutamate degradation, GABAergic signaling, as well as significant changes in bioenergetics and energy homeostasis (oxidative phosphorylation, TCA cycle, and glycolysis). These pathways are consistent with previously reported behavioral and biochemical phenotypes that typify mice lacking ENT1. Moreover, we validated decreased expression of the SNARE complex protein VAMP1 (synaptobrevin-1) in the dHip as well as decreased expression of pro-dynorphin (PDYN), neuroendocrine convertase (PCSK1), and Leu-Enkephalin (dynorphin-A) in the NAc. Taken together, our proteomic approach provides novel pathways indicating that ENT1-regulated signaling is essential for neurotransmitter release and neuropeptide processing, both of which underlie learning and reward-seeking behaviors.
[Mh] Termos MeSH primário: Encefalinas/genética
Transportador Equilibrativo 1 de Nucleosídeo/genética
Pró-Proteína Convertase 1/genética
Precursores de Proteínas/genética
Proteômica
Proteína 1 Associada à Membrana da Vesícula/genética
[Mh] Termos MeSH secundário: Consumo de Bebidas Alcoólicas/genética
Consumo de Bebidas Alcoólicas/patologia
Animais
Etanol/metabolismo
Hipocampo/metabolismo
Hipocampo/patologia
Potenciação de Longa Duração/genética
Camundongos
Neuropeptídeos/biossíntese
Neuropeptídeos/genética
Neurotransmissores/biossíntese
Neurotransmissores/genética
Núcleo Accumbens/metabolismo
Núcleo Accumbens/patologia
Transdução de Sinais/genética
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enkephalins); 0 (Equilibrative Nucleoside Transporter 1); 0 (Neuropeptides); 0 (Neurotransmitter Agents); 0 (Protein Precursors); 0 (SLC29A1 protein, mouse); 0 (Vesicle-Associated Membrane Protein 1); 0 (vesicle-associated membrane protein 1, mouse); 3K9958V90M (Ethanol); 93443-35-7 (preproenkephalin); EC 3.4.21.93 (Pcsk1 protein, mouse); EC 3.4.21.93 (Proprotein Convertase 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.6b00830


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[PMID]:27941249
[Au] Autor:Burnett LC; LeDuc CA; Sulsona CR; Paull D; Rausch R; Eddiry S; Carli JF; Morabito MV; Skowronski AA; Hubner G; Zimmer M; Wang L; Day R; Levy B; Fennoy I; Dubern B; Poitou C; Clement K; Butler MG; Rosenbaum M; Salles JP; Tauber M; Driscoll DJ; Egli D; Leibel RL
[Ti] Título:Deficiency in prohormone convertase PC1 impairs prohormone processing in Prader-Willi syndrome.
[So] Source:J Clin Invest;127(1):293-305, 2017 Jan 03.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prader-Willi syndrome (PWS) is caused by a loss of paternally expressed genes in an imprinted region of chromosome 15q. Among the canonical PWS phenotypes are hyperphagic obesity, central hypogonadism, and low growth hormone (GH). Rare microdeletions in PWS patients define a 91-kb minimum critical deletion region encompassing 3 genes, including the noncoding RNA gene SNORD116. Here, we found that protein and transcript levels of nescient helix loop helix 2 (NHLH2) and the prohormone convertase PC1 (encoded by PCSK1) were reduced in PWS patient induced pluripotent stem cell-derived (iPSC-derived) neurons. Moreover, Nhlh2 and Pcsk1 expression were reduced in hypothalami of fasted Snord116 paternal knockout (Snord116p-/m+) mice. Hypothalamic Agrp and Npy remained elevated following refeeding in association with relative hyperphagia in Snord116p-/m+ mice. Nhlh2-deficient mice display growth deficiencies as adolescents and hypogonadism, hyperphagia, and obesity as adults. Nhlh2 has also been shown to promote Pcsk1 expression. Humans and mice deficient in PC1 display hyperphagic obesity, hypogonadism, decreased GH, and hypoinsulinemic diabetes due to impaired prohormone processing. Here, we found that Snord116p-/m+ mice displayed in vivo functional defects in prohormone processing of proinsulin, pro-GH-releasing hormone, and proghrelin in association with reductions in islet, hypothalamic, and stomach PC1 content. Our findings suggest that the major neuroendocrine features of PWS are due to PC1 deficiency.
[Mh] Termos MeSH primário: Hormônio Liberador de Hormônio do Crescimento/metabolismo
Neurônios/metabolismo
Síndrome de Prader-Willi/metabolismo
Proinsulina/metabolismo
Pró-Proteína Convertase 1/deficiência
Precursores de Proteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Diabetes Mellitus/genética
Diabetes Mellitus/metabolismo
Diabetes Mellitus/patologia
Feminino
Hormônio Liberador de Hormônio do Crescimento/genética
Seres Humanos
Hiperfagia/genética
Hiperfagia/metabolismo
Hiperfagia/patologia
Hipogonadismo/genética
Hipogonadismo/metabolismo
Hipogonadismo/patologia
Células-Tronco Pluripotentes Induzidas/metabolismo
Células-Tronco Pluripotentes Induzidas/patologia
Masculino
Camundongos Knockout
Neurônios/patologia
Obesidade/genética
Obesidade/metabolismo
Obesidade/patologia
Síndrome de Prader-Willi/genética
Síndrome de Prader-Willi/patologia
Proinsulina/genética
Precursores de Proteínas/genética
RNA Nucleolar Pequeno/genética
RNA Nucleolar Pequeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Nhlh2 protein, mouse); 0 (Protein Precursors); 0 (RNA, Small Nucleolar); 0 (SNORD116 RNA, human); 0 (SNORD116 RNA, mouse); 125200-87-5 (pro-growth hormone releasing hormone, mouse); 148025-11-0 (NHLH2 protein, human); 9034-39-3 (Growth Hormone-Releasing Hormone); 9035-68-1 (Proinsulin); EC 3.4.21.93 (PCSK1 protein, human); EC 3.4.21.93 (Pcsk1 protein, mouse); EC 3.4.21.93 (Proprotein Convertase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


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[PMID]:27941250
[Au] Autor:Polex-Wolf J; Yeo GS; O'Rahilly S
[Ti] Título:Impaired prohormone processing: a grand unified theory for features of Prader-Willi syndrome?
[So] Source:J Clin Invest;127(1):98-99, 2017 Jan 03.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prader-Willi syndrome (PWS) is a complex disorder that manifests with an array of phenotypes, such as hypotonia and difficulties in feeding during infancy and reduced energy expenditure, hyperphagia, and developmental delays later in life. While the genetic cause has long been known, it is still not clear how mutations at this locus produce this array of phenotypes. In this issue of the JCI, Burnett and colleagues used a comprehensive approach to gain insight into how PWS-associated mutations drive disease. Using neurons derived from PWS patient induced pluripotent stem cells (iPSCs) and mouse models, the authors provide evidence that neuroendocrine PWS-associated phenotypes may be linked to reduced expression of prohormone convertase 1 (PC1). While these compelling results support a critical role for PC1 deficiency in PWS, more work needs to be done to fully understand how and to what extent loss of this prohormone processing enzyme underlies disease manifestations in PWS patients.
[Mh] Termos MeSH primário: Células-Tronco Pluripotentes Induzidas/enzimologia
Mutação
Neurônios/enzimologia
Síndrome de Prader-Willi/genética
Pró-Proteína Convertase 1/genética
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Células-Tronco Pluripotentes Induzidas/patologia
Neurônios/patologia
Síndrome de Prader-Willi/enzimologia
Síndrome de Prader-Willi/patologia
Pró-Proteína Convertase 1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.21.93 (Proprotein Convertase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


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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]:27744031
[Au] Autor:Poposki JA; Klingler AI; Stevens WW; Peters AT; Hulse KE; Grammer LC; Schleimer RP; Welch KC; Smith SS; Sidle DM; Conley DB; Tan BK; Kern RC; Kato A
[Ad] Endereço:Division of Allergy-Immunology, Department of Medicine, Northwestern University Feinberg School of Medicine, Chicago, Ill.
[Ti] Título:Proprotein convertases generate a highly functional heterodimeric form of thymic stromal lymphopoietin in humans.
[So] Source:J Allergy Clin Immunol;139(5):1559-1567.e8, 2017 May.
[Is] ISSN:1097-6825
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RATIONALE: Thymic stromal lymphopoietin (TSLP) is known to be elevated and truncated in nasal polyps (NPs) of patients with chronic rhinosinusitis and might play a significant role in type 2 inflammation in this disease. However, neither the structure nor the role of the truncated products of TSLP has been studied. OBJECTIVE: We sought to investigate the mechanisms of truncation of TSLP in NPs and the function of the truncated products. METHODS: We incubated recombinant human TSLP with NP extracts, and determined the protein sequence of the truncated forms of TSLP using Edman protein sequencing and matrix-assisted laser desorption/ionization-time of flight mass spectrometry. We investigated the functional activity of truncated TSLP using a PBMC-based bioassay. RESULTS: Edman sequencing and mass spectrometry results indicated that NP extracts generated 2 major truncated products, TSLP (residues 29-124) and TSLP (131-159). Interestingly, these 2 products remained linked with disulfide bonds and presented as a dimerized form, TSLP (29-124 + 131-159). We identified that members of the proprotein convertase were rate-limiting enzymes in the truncation of TSLP between residues 130 and 131 and generated a heterodimeric unstable metabolite TSLP (29-130 + 131-159). Carboxypeptidase N immediately digested 6 amino acids from the C terminus of the longer subunit of TSLP to generate a stable dimerized form, TSLP (29-124 + 131-159), in NPs. These truncations were homeostatic but primate-specific events. A metabolite TSLP (29-130 + 131-159) strongly activated myeloid dendritic cells and group 2 innate lymphoid cells compared with mature TSLP. CONCLUSIONS: Posttranslational modifications control the functional activity of TSLP in humans and overproduction of TSLP may be a key trigger for the amplification of type 2 inflammation in diseases.
[Mh] Termos MeSH primário: Citocinas
Pólipos Nasais/imunologia
Pró-Proteína Convertase 1
[Mh] Termos MeSH secundário: Células Cultivadas
Citocinas/farmacologia
Seres Humanos
Leucócitos Mononucleares/efeitos dos fármacos
Leucócitos Mononucleares/imunologia
Pró-Proteína Convertase 1/farmacologia
Processamento de Proteína Pós-Traducional
Proteínas Recombinantes/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Recombinant Proteins); 0 (thymic stromal lymphopoietin); EC 3.4.21.93 (PCSK1 protein, human); EC 3.4.21.93 (Proprotein Convertase 1)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161017
[St] Status:MEDLINE


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[PMID]:27491554
[Au] Autor:Righi A; Faustini-Fustini M; Morandi L; Monti V; Asioli S; Mazzatenta D; Bacci A; Foschini MP
[Ad] Endereço:Department of Pathology, Rizzoli Institute, Bologna, Italy.
[Ti] Título:The changing faces of corticotroph cell adenomas: the role of prohormone convertase 1/3.
[So] Source:Endocrine;56(2):286-297, 2017 May.
[Is] ISSN:1559-0100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spectrum of corticotroph cell adenomas is very wide. Though rarely, silent corticotroph cell adenomas (SCA) may transform into corticotroph cell adenomas associated with Cushing's disease (CD). The aim of the study was to investigate the role of prohormone convertase 1/3 (PC1/3) in the transformation of SCA into CD. We reviewed the records of 1259 consecutive endoscopic endonasal procedures for pituitary adenomas from 1998 to 2013. Of these, 132 were CD and 44 were SCA. During the follow-up, three patients with SCA showed a clear transformation from SCA into CD and underwent surgery once again to remove the recurrent tumour. The PC1/3 expression was analysed by both immunohistochemistry and quantitative real time-polymerase chain reaction (qRT-PCR) in primary and recurrent tumours. The immunohistochemical PC1/3 expression was negative or weak in the three patients in the initial phase of SCA, while a strong expression was observed in the majority of neoplastic cells in tissue specimens obtained from the same three patients at the time of recurrence as CD. The immunohistochemical PC1/3 expression showed a strict correlation with the PC1/3 levels obtained by qRT-PCR. In 14 cases of SCA with no change of phenotype during the follow-up, the immunohistochemical PC1/3 expression was low and strictly associated with the level of PC1/3 obtained by qRT-PCR both in primary (14/14 cases) and in recurrent tumours (4/4 cases). Our study provides insight into the crucial role of the PC1/3 protein in the transformation of phenotype from SCA to CD.
[Mh] Termos MeSH primário: Adenoma Hipofisário Secretor de ACT/enzimologia
Adenoma/enzimologia
Pró-Proteína Convertase 1/metabolismo
[Mh] Termos MeSH secundário: Adenoma Hipofisário Secretor de ACT/patologia
Adenoma/patologia
Adolescente
Adulto
Idoso
Feminino
Seres Humanos
Imuno-Histoquímica
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.21.93 (Proprotein Convertase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160806
[St] Status:MEDLINE
[do] DOI:10.1007/s12020-016-1028-0



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