Base de dados : MEDLINE
Pesquisa : A11.382.944 [Categoria DeCS]
Referências encontradas : 477 [refinar]
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[PMID]:29203758
[Au] Autor:Stefanski M; Brulinski K; Stefanska M
[Ad] Endereço:Oddzial Chirurgii Klatki Piersiowej, Centrum Pulmonologii I Torakochirurgii, Bystra, Polska.
[Ti] Título:[Diffuse idiopathic pulmonary neuroendocrine cell hyperplasia (dipnech) - an overview of the cases diagnosed at the department of thoracic surgery in the years 2010-2014].
[So] Source:Wiad Lek;70(5):1005-1012, 2017.
[Is] ISSN:0043-5147
[Cp] País de publicação:Poland
[La] Idioma:pol
[Ab] Resumo:INTRODUCTION: Pulmonary neuroendocrine cells (PNEC) are present in the normal lungs with the incidence of 1 in 2500 epithelial cells. They usually proliferate in the presence of reactive processes related to inflammation and fibrosis of the lung parenchyma. The division of pulmonary neuroendocrine cell hyperplasia proposed by Travis et al. additionally distinguished diffuse idiopathic pulmonary neuroendocrine cell hyperplasia (DIPNECH) or proliferation that occurs in people without reactive hyperplasia risk factors. The confirmation of the DIPNECH diagnosis requires staining of biopsy specimens using the immunohistochemical technique for neuroendocrine markers. AIM: The aim of this study is to overview the cases of 5 patients in whom the histopathological DIPNECH diagnosis was made in the process of invasive diagnostics performed at the Department of Thoracic Surgery. The aim of the study is to evaluate typical clinical, functional, radiological and histopathological features of this rare disease syndrome. MATERIAL AND METHODS: In the period from April 2010 to June 2014, five patients with lesions in the lungs were subjected to invasive diagnostics. Histopathological and immunohistochemical examinations of the collected specimens were used to make the DIPNECH diagnosis in these patients. The natural history of the disease was traced based on a 5-year follow-up in one of the patients. In addition, we analyzed the literature with regard to the described cases. CONCLUSIONS: Thanks to the early diagnosis of non-specific lesions in the lungs, typical carcinoid which develops on the basis of discussed DIPNECH, was found in the resected material in two out of five operated patients. The accurate diagnosis of DIPNECH allows for the implementation of appropriate treatment and channels further management of the patient into the right direction.
[Mh] Termos MeSH primário: Hiperplasia/diagnóstico por imagem
Hiperplasia/patologia
Pneumopatias/diagnóstico por imagem
Pneumopatias/patologia
Células Neuroendócrinas/patologia
[Mh] Termos MeSH secundário: Idoso
Proliferação Celular
Feminino
Seres Humanos
Imuno-Histoquímica
Masculino
Meia-Idade
Testes de Função Respiratória
Tomografia Computadorizada por Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


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[PMID]:28920920
[Au] Autor:Shi G; Somlo DRM; Kim GH; Prescianotto-Baschong C; Sun S; Beuret N; Long Q; Rutishauser J; Arvan P; Spiess M; Qi L
[Ad] Endereço:Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan, USA.
[Ti] Título:ER-associated degradation is required for vasopressin prohormone processing and systemic water homeostasis.
[So] Source:J Clin Invest;127(10):3897-3912, 2017 10 02.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peptide hormones are crucial regulators of many aspects of human physiology. Mutations that alter these signaling peptides are associated with physiological imbalances that underlie diseases. However, the conformational maturation of peptide hormone precursors (prohormones) in the ER remains largely unexplored. Here, we report that conformational maturation of proAVP, the precursor for the antidiuretic hormone arginine-vasopressin, within the ER requires the ER-associated degradation (ERAD) activity of the Sel1L-Hrd1 protein complex. Serum hyperosmolality induces expression of both ERAD components and proAVP in AVP-producing neurons. Mice with global or AVP neuron-specific ablation of Se1L-Hrd1 ERAD progressively developed polyuria and polydipsia, characteristics of diabetes insipidus. Mechanistically, we found that ERAD deficiency causes marked ER retention and aggregation of a large proportion of all proAVP protein. Further, we show that proAVP is an endogenous substrate of Sel1L-Hrd1 ERAD. The inability to clear misfolded proAVP with highly reactive cysteine thiols in the absence of Sel1L-Hrd1 ERAD causes proAVP to accumulate and participate in inappropriate intermolecular disulfide-bonded aggregates, promoted by the enzymatic activity of protein disulfide isomerase (PDI). This study highlights a pathway linking ERAD to prohormone conformational maturation in neuroendocrine cells, expanding the role of ERAD in providing a conducive ER environment for nascent proteins to reach proper conformation.
[Mh] Termos MeSH primário: Degradação Associada com o Retículo Endoplasmático
Retículo Endoplasmático/metabolismo
Células Neuroendócrinas/metabolismo
Proteólise
Vasopressinas/metabolismo
Equilíbrio Hidroeletrolítico
[Mh] Termos MeSH secundário: Animais
Retículo Endoplasmático/genética
Camundongos
Camundongos Transgênicos
Células Neuroendócrinas/patologia
Neurônios/metabolismo
Neurônios/patologia
Polidipsia/genética
Polidipsia/metabolismo
Polidipsia/patologia
Isomerases de Dissulfetos de Proteínas/genética
Isomerases de Dissulfetos de Proteínas/metabolismo
Proteínas/genética
Proteínas/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
Vasopressinas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins); 0 (Sel1h protein, mouse); 0 (proAVP hormone); 11000-17-2 (Vasopressins); EC 2.3.2.27 (Syvn1 protein, mouse); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 5.3.4.1 (Protein Disulfide-Isomerases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


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[PMID]:28734980
[Au] Autor:Maina PK; Shao P; Jia X; Liu Q; Umesalma S; Marin M; Long D; Concepción-Román S; Qi HH
[Ad] Endereço:Department of Anatomy and Cell Biology, Carver College of Medicine, University of Iowa, Iowa City, IA 52242-1109, USA.
[Ti] Título:Histone demethylase PHF8 regulates hypoxia signaling through HIF1α and H3K4me3.
[So] Source:Biochim Biophys Acta;1860(9):1002-1012, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hypoxia through transcription factor HIF1α plays a critical role in cancer development. In prostate cancer, HIF1α interplays with androgen receptor (AR) to contribute to the progression of this disease to its lethal form-castration-resistant prostate cancer (CRPC). Hypoxia upregulates several epigenetic factors including histone demethylase KDM3A which is a critical co-factor of HIF1α. However, how histone demethylases regulate hypoxia signaling is not fully understood. Here, we report that histone demethylase PHF8 plays an essential role in hypoxia signaling. Knockdown or knockout of PHF8 by RNAi or CRISPR-Cas9 system reduced the activation of HIF1α and the induction of HIF1α target genes including KDM3A. Mechanistically, PHF8 regulates hypoxia inducible genes mainly through sustaining the level of trimethylated histone 3 lysine 4 (H3K4me3), an active mark in transcriptional regulation. The positive role of PHF8 in hypoxia signaling extended to hypoxia-induced neuroendocrine differentiation (NED), wherein PHF8 cooperates with KDM3A to regulate the expression of NED genes. Moreover, we discovered that the role of PHF8 in hypoxia signaling is associated with the presence of full-length AR in CRPC cells. Collectively, our study identified PHF8 as a novel epigenetic factor in hypoxia signaling, and the underlying regulatory mechanisms likely apply to general cancer development involving HIF1α. Therefore, targeting PHF8 can potentially be a novel therapeutic strategy in cancer therapy.
[Mh] Termos MeSH primário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Histona Desmetilases/metabolismo
Histonas/metabolismo
Hipóxia/metabolismo
Transdução de Sinais/fisiologia
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sistemas CRISPR-Cas/fisiologia
Linhagem Celular
Proliferação Celular/fisiologia
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas/fisiologia
Regulação da Expressão Gênica/fisiologia
Células HEK293
Seres Humanos
Histona Desmetilases com o Domínio Jumonji/metabolismo
Lisina/metabolismo
Células Neuroendócrinas/metabolismo
RNA Longo não Codificante/metabolismo
Receptores Androgênicos/metabolismo
Transcrição Genética/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Histones); 0 (RNA, Long Noncoding); 0 (Receptors, Androgen); 0 (Transcription Factors); 0 (endothelial PAS domain-containing protein 1); 0 (long noncoding RNA CASC9, human); EC 1.14.11.- (Histone Demethylases); EC 1.14.11.- (Jumonji Domain-Containing Histone Demethylases); EC 1.14.11.- (PHF8 protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170724
[St] Status:MEDLINE


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[PMID]:28675567
[Au] Autor:Rohde K; Bering T; Furukawa T; Rath MF
[Ad] Endereço:Department of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
[Ti] Título:A modulatory role of the Rax homeobox gene in mature pineal gland function: Investigating the photoneuroendocrine circadian system of a Rax conditional knockout mouse.
[So] Source:J Neurochem;143(1):100-111, 2017 Oct.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The retinal and anterior neural fold homeobox gene (Rax) controls development of the eye and the forebrain. Postnatal expression of Rax in the brain is restricted to the pineal gland, a forebrain structure devoted to melatonin synthesis. The role of Rax in pineal function is unknown. In order to investigate the role of Rax in pineal function while circumventing forebrain abnormalities of the global Rax knockout, we generated an eye and pineal-specific Rax conditional knockout mouse. Deletion of Rax in the pineal gland did not affect morphology of the gland, suggesting that Rax is not essential for pineal gland development. In contrast, deletion of Rax in the eye generated an anophthalmic phenotype. In addition to the loss of central visual pathways, the suprachiasmatic nucleus of the hypothalamus housing the circadian clock was absent, indicating that the retinohypothalamic tract is required for the nucleus to develop. Telemetric analyses confirmed the lack of a functional circadian clock. Arylalkylamine N-acetyltransferase (Aanat) transcripts, encoding the melatonin rhythm-generating enzyme, were undetectable in the pineal gland of the Rax conditional knockout under normal conditions, whereas the paired box 6 homeobox gene, known to regulate pineal development, was up-regulated. By injecting isoproterenol, which mimics a nocturnal situation in the pineal gland, we were able to induce pineal expression of Aanat in the Rax conditional knockout mouse, but Aanat transcript levels were significantly lower than those of Rax-proficient mice. Our data suggest that Rax controls pineal gene expression and via Aanat may modulate melatonin synthesis.
[Mh] Termos MeSH primário: Ritmo Circadiano/fisiologia
Proteínas do Olho/fisiologia
Genes Homeobox/fisiologia
Proteínas de Homeodomínio/fisiologia
Glândula Pineal/metabolismo
Núcleo Supraquiasmático/metabolismo
Fatores de Transcrição/fisiologia
Vias Visuais/metabolismo
[Mh] Termos MeSH secundário: Animais
Arilalquilamina N-Acetiltransferase/biossíntese
Arilalquilamina N-Acetiltransferase/genética
Proteínas do Olho/genética
Feminino
Perfilação da Expressão Gênica/métodos
Proteínas de Homeodomínio/genética
Masculino
Camundongos
Camundongos da Linhagem 129
Camundongos Knockout
Células Neuroendócrinas/metabolismo
Retina/metabolismo
Fatores de Transcrição/deficiência
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (Homeodomain Proteins); 0 (Rax protein, mouse); 0 (Transcription Factors); EC 2.3.1.87 (AANAT protein, human); EC 2.3.1.87 (Arylalkylamine N-Acetyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.14120


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[PMID]:28626000
[Au] Autor:Zhang X; Jiang S; Mitok KA; Li L; Attie AD; Martin TFJ
[Ad] Endereço:Department of Biochemistry, University of Wisconsin, Madison, WI.
[Ti] Título:BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-core vesicles in neuroendocrine cells.
[So] Source:J Cell Biol;216(7):2151-2166, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dense-core vesicle (DCV) exocytosis is a SNARE (soluble -ethylmaleimide-sensitive fusion attachment protein receptor)-dependent anterograde trafficking pathway that requires multiple proteins for regulation. Several C2 domain-containing proteins are known to regulate Ca -dependent DCV exocytosis in neuroendocrine cells. In this study, we identified others by screening all (∼139) human C2 domain-containing proteins by RNA interference in neuroendocrine cells. 40 genes were identified, including several encoding proteins with known roles (CAPS [calcium-dependent activator protein for secretion 1], Munc13-2, RIM1, and SYT10) and many with unknown roles. One of the latter, BAIAP3, is a secretory cell-specific Munc13-4 paralog of unknown function. BAIAP3 knockdown caused accumulation of fusion-incompetent DCVs in BON neuroendocrine cells and lysosomal degradation (crinophagy) of insulin-containing DCVs in INS-1 ß cells. BAIAP3 localized to endosomes was required for Golgi trans-Golgi network 46 (TGN46) recycling, exhibited Ca -stimulated interactions with TGN SNAREs, and underwent Ca -stimulated TGN recruitment. Thus, unlike other Munc13 proteins, BAIAP3 functions indirectly in DCV exocytosis by affecting DCV maturation through its role in DCV protein recycling. Ca rises that stimulate DCV exocytosis may stimulate BAIAP3-dependent retrograde trafficking to maintain DCV protein homeostasis and DCV function.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Exocitose
Proteínas do Tecido Nervoso/metabolismo
Células Neuroendócrinas/metabolismo
Vesículas Secretórias/metabolismo
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Proteínas de Transporte/genética
Linhagem Celular Tumoral
Células HEK293
Seres Humanos
Insulina/metabolismo
Insulina/secreção
Células Secretoras de Insulina/metabolismo
Células Secretoras de Insulina/secreção
Proteínas do Tecido Nervoso/genética
Células Neuroendócrinas/secreção
Domínios Proteicos
Transporte Proteico
Interferência de RNA
Ratos
Vesículas Secretórias/secreção
Transfecção
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BAIAP3 protein, human); 0 (BAIAP3 protein, rat); 0 (Carrier Proteins); 0 (Insulin); 0 (Nerve Tissue Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702099


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[PMID]:28579251
[Au] Autor:Mucio-Ramírez S; Sánchez-Islas E; Sánchez-Jaramillo E; Currás-Collazo M; Juárez-González VR; Álvarez-González MY; Orser LE; Hou B; Pellicer F; Kodavanti PRS; León-Olea M
[Ad] Endereço:Departamento de Neuromorfología Funcional, Dirección de Investigaciones en Neurociencias, Instituto Nacional de Psiquiatría Ramón de la Fuente Muñiz, Calz. México Xochimilco No. 101, Col. San Lorenzo Huipulco, México D.F. C.P. 14370, México. Electronic address: mucios@imp.edu.mx.
[Ti] Título:Perinatal exposure to organohalogen pollutants decreases vasopressin content and its mRNA expression in magnocellular neuroendocrine cells activated by osmotic stress in adult rats.
[So] Source:Toxicol Appl Pharmacol;329:173-189, 2017 Aug 15.
[Is] ISSN:1096-0333
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polychlorinated biphenyls (PCBs) and polybrominated diphenyl ethers (PBDEs) are environmental pollutants that produce neurotoxicity and neuroendocrine disruption. They affect the vasopressinergic system but their disruptive mechanisms are not well understood. Our group reported that rats perinatally exposed to Aroclor-1254 (A1254) and DE-71 (commercial mixtures of PCBs and PBDEs) decrease somatodendritic vasopressin (AVP) release while increasing plasma AVP responses to osmotic activation, potentially emptying AVP reserves required for body-water balance. The aim of this research was to evaluate the effects of perinatal exposure to A1254 or DE-71 (30mgkg/day) on AVP transcription and protein content in the paraventricular and supraoptic hypothalamic nuclei, of male and female rats, by in situ hybridization and immunohistochemistry. cFOS mRNA expression was evaluated in order to determine neuroendocrine cells activation due to osmotic stimulation. Animal groups were: vehicle (control); exposed to either A1254 or DE-71; both, control and exposed, subjected to osmotic challenge. The results confirmed a physiological increase in AVP-immunoreactivity (AVP-IR) and gene expression in response to osmotic challenge as reported elsewhere. In contrast, the exposed groups did not show this response to osmotic activation, they showed significant reduction in AVP-IR neurons, and AVP mRNA expression as compared to the hyperosmotic controls. cFOS mRNA expression increased in A1254 dehydrated groups, suggesting that the AVP-IR decrease was not due to a lack of the response to the osmotic activation. Therefore, A1254 may interfere with the activation of AVP mRNA transcript levels and protein, causing a central dysfunction of vasopressinergic system.
[Mh] Termos MeSH primário: Arginina Vasopressina/metabolismo
/toxicidade
Poluentes Ambientais/toxicidade
Éteres Difenil Halogenados/toxicidade
Células Neuroendócrinas/efeitos dos fármacos
Pressão Osmótica
Núcleo Hipotalâmico Paraventricular/efeitos dos fármacos
Efeitos Tardios da Exposição Pré-Natal
RNA Mensageiro/metabolismo
Núcleo Supraóptico/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Arginina Vasopressina/genética
Regulação para Baixo
Feminino
Masculino
Exposição Materna/efeitos adversos
Células Neuroendócrinas/metabolismo
Células Neuroendócrinas/patologia
Núcleo Hipotalâmico Paraventricular/metabolismo
Núcleo Hipotalâmico Paraventricular/patologia
Gravidez
Proteínas Proto-Oncogênicas c-fos/genética
Proteínas Proto-Oncogênicas c-fos/metabolismo
RNA Mensageiro/genética
Ratos Sprague-Dawley
Ratos Wistar
Cloreto de Sódio/administração & dosagem
Núcleo Supraóptico/metabolismo
Núcleo Supraóptico/patologia
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Environmental Pollutants); 0 (Halogenated Diphenyl Ethers); 0 (Proto-Oncogene Proteins c-fos); 0 (RNA, Messenger); 11097-69-1 (Chlorodiphenyl (54% Chlorine)); 113-79-1 (Arginine Vasopressin); 451W47IQ8X (Sodium Chloride); 7REL09ZX35 (pentabromodiphenyl ether)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE


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[PMID]:28566470
[Au] Autor:Barrios J; Patel KR; Aven L; Achey R; Minns MS; Lee Y; Trinkaus-Randall VE; Ai X
[Ad] Endereço:The Pulmonary Center, Department of Medicine, Boston University School of Medicine, Boston, Massachusetts, USA.
[Ti] Título:Early life allergen-induced mucus overproduction requires augmented neural stimulation of pulmonary neuroendocrine cell secretion.
[So] Source:FASEB J;31(9):4117-4128, 2017 Sep.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pulmonary neuroendocrine cells (PNECs) are the only innervated airway epithelial cells. To what extent neural innervation regulates PNEC secretion and function is unknown. Here, we discover that neurotrophin 4 (NT4) plays an essential role in mucus overproduction after early life allergen exposure by orchestrating PNEC innervation and secretion of GABA. We found that PNECs were the only cellular source of GABA in airways. In addition, PNECs expressed NT4 as a target-derived mechanism underlying PNEC innervation during development. Early life allergen exposure elevated the level of NT4 and caused PNEC hyperinnervation and nodose neuron hyperactivity. Associated with aberrant PNEC innervation, the authors discovered that GABA hypersecretion was required for the induction of mucin Muc5ac expression. In contrast, mice were protected from allergen-induced mucus overproduction and changes along the nerve-PNEC axis without any defects in inflammation. Last, GABA installation restored mucus overproduction in mice after early life allergen exposure. Together, our findings provide the first evidence for NT4-dependent neural regulation of PNEC secretion of GABA in a neonatal disease model. Targeting the nerve-PNEC axis may be a valid treatment strategy for mucus overproduction in airway diseases, such as childhood asthma.-Barrios, J., Patel, K. R., Aven, L., Achey, R., Minns, M. S., Lee, Y., Trinkaus-Randall, V. E., Ai, X. Early life allergen-induced mucus overproduction requires augmented neural stimulation of pulmonary neuroendocrine cell secretion.
[Mh] Termos MeSH primário: Alérgenos/imunologia
Regulação da Expressão Gênica/imunologia
Hipersensibilidade/metabolismo
Muco/metabolismo
Células Neuroendócrinas/metabolismo
Ovalbumina/imunologia
[Mh] Termos MeSH secundário: Animais
Cálcio
Camundongos Endogâmicos C57BL
Ácido gama-Aminobutírico/genética
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 56-12-2 (gamma-Aminobutyric Acid); 9006-59-1 (Ovalbumin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700115R


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[PMID]:28557996
[Au] Autor:Minnerly J; Zhang J; Parker T; Kaul T; Jia K
[Ad] Endereço:Department of Biological Sciences, Florida Atlantic University, Jupiter, FL, United States of America.
[Ti] Título:The cell non-autonomous function of ATG-18 is essential for neuroendocrine regulation of Caenorhabditis elegans lifespan.
[So] Source:PLoS Genet;13(5):e1006764, 2017 May.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dietary restriction (DR) and reduced insulin growth factor (IGF) signaling extend lifespan in Caenorhabditis elegans and other eukaryotic organisms. Autophagy, an evolutionarily conserved lysosomal degradation pathway, has emerged as a central pathway regulated by various longevity signals including DR and IGF signaling in promoting longevity in a variety of eukaryotic organisms. However, the mechanism remains unclear. Here we show that the autophagy protein ATG-18 acts cell non-autonomously in neuronal and intestinal tissues to maintain C. elegans wildtype lifespan and to respond to DR and IGF-mediated longevity signaling. Moreover, ATG-18 activity in chemosensory neurons that are involved in food detection sufficiently mediates the effect of these longevity pathways. Additionally, ATG-18-mediated cell non-autonomous signaling depends on the release of neurotransmitters and neuropeptides. Interestingly, our data suggest that neuronal and intestinal ATG-18 acts in parallel and converges on unidentified neurons that secrete neuropeptides to regulate C. elegans lifespan through the transcription factor DAF-16/FOXO in response to reduced IGF signaling.
[Mh] Termos MeSH primário: Proteínas Relacionadas à Autofagia/metabolismo
Caenorhabditis elegans/metabolismo
Longevidade
Neuropeptídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas Relacionadas à Autofagia/genética
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Restrição Calórica
Fatores de Transcrição Forkhead/genética
Fatores de Transcrição Forkhead/metabolismo
Fator de Crescimento Insulin-Like I/metabolismo
Intestinos/metabolismo
Células Neuroendócrinas/metabolismo
Neurotransmissores/metabolismo
Células Receptoras Sensoriais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autophagy-Related Proteins); 0 (Caenorhabditis elegans Proteins); 0 (Forkhead Transcription Factors); 0 (Neuropeptides); 0 (Neurotransmitter Agents); 0 (daf-16 protein, C elegans); 67763-96-6 (Insulin-Like Growth Factor I)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006764


  9 / 477 MEDLINE  
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[PMID]:28546426
[Au] Autor:Emery AC; Xu W; Eiden MV; Eiden LE
[Ad] Endereço:From the Section on Molecular Neuroscience and.
[Ti] Título:Guanine nucleotide exchange factor Epac2-dependent activation of the GTP-binding protein Rap2A mediates cAMP-dependent growth arrest in neuroendocrine cells.
[So] Source:J Biol Chem;292(29):12220-12231, 2017 Jul 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:First messenger-dependent activation of MAP kinases in neuronal and endocrine cells is critical for cell differentiation and function and requires guanine nucleotide exchange factor (GEF)-mediated activation of downstream Ras family small GTPases, which ultimately lead to ERK, JNK, and p38 phosphorylation. Because there are numerous GEFs and also a host of Ras family small GTPases, it is important to know which specific GEF-small GTPase dyad functions in a given cellular process. Here we investigated the upstream activators and downstream effectors of signaling via the GEF Epac2 in the neuroendocrine NS-1 cell line. Three cAMP sensors, Epac2, PKA, and neuritogenic cAMP sensor-Rapgef2, mediate distinct cellular outputs: p38-dependent growth arrest, cAMP response element-binding protein-dependent cell survival, and ERK-dependent neuritogenesis, respectively, in these cells. Previously, we found that cAMP-induced growth arrest of PC12 and NS-1 cells requires Epac2-dependent activation of p38 MAP kinase, which posed the important question of how Epac2 engages p38 without simultaneously activating other MAP kinases in neuronal and endocrine cells. We now show that the small GTP-binding protein Rap2A is the obligate effector for, and GEF substrate of, Epac2 in mediating growth arrest through p38 activation in NS-1 cells. This new pathway is distinctly parcellated from the G protein-coupled receptor → G → adenylate cyclase → cAMP → PKA → cAMP response element-binding protein pathway mediating cell survival and the G protein-coupled receptor → G → adenylate cyclase → cAMP → neuritogenic cAMP sensor-Rapgef2 → B-Raf → MEK → ERK pathway mediating neuritogenesis in NS-1 cells.
[Mh] Termos MeSH primário: AMP Cíclico/metabolismo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Sistema de Sinalização das MAP Quinases
Células Neuroendócrinas/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas rap de Ligação ao GTP/agonistas
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Ativação Enzimática
Proteínas de Ligação ao GTP/química
Proteínas de Ligação ao GTP/genética
Proteínas de Ligação ao GTP/metabolismo
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Ligantes
Proteínas Monoméricas de Ligação ao GTP/antagonistas & inibidores
Proteínas Monoméricas de Ligação ao GTP/genética
Proteínas Monoméricas de Ligação ao GTP/metabolismo
Proteínas do Tecido Nervoso/agonistas
Proteínas do Tecido Nervoso/antagonistas & inibidores
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Neuritos/metabolismo
Células Neuroendócrinas/citologia
Neurogênese
Fosforilação
Prenilação de Proteína
Interferência de RNA
Ratos
Proteínas Recombinantes/metabolismo
Proteínas rap de Ligação ao GTP/antagonistas & inibidores
Proteínas rap de Ligação ao GTP/genética
Proteínas rap de Ligação ao GTP/metabolismo
Proteínas ras/antagonistas & inibidores
Proteínas ras/genética
Proteínas ras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epac-2 protein, rat); 0 (Guanine Nucleotide Exchange Factors); 0 (Ligands); 0 (Nerve Tissue Proteins); 0 (Rap2a protein, rat); 0 (Recombinant Proteins); 147336-22-9 (Green Fluorescent Proteins); E0399OZS9N (Cyclic AMP); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.5.2 (Monomeric GTP-Binding Proteins); EC 3.6.5.2 (Rit1 protein, rat); EC 3.6.5.2 (rap GTP-Binding Proteins); EC 3.6.5.2 (ras Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.790329


  10 / 477 MEDLINE  
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[PMID]:28542590
[Au] Autor:Aristizabal Prada ET; Orth M; Nölting S; Spöttl G; Maurer J; Auernhammer C
[Ad] Endereço:Department of Internal Medicine II, Campus Grosshadern, Interdisciplinary Center of Neuroendocrine Tumours of the GastroEnteroPancreatic System (GEPNET-KUM), University-Hospital, Ludwig-Maximilians-University of Munich, Bavaria, Germany.
[Ti] Título:The MTH1 inhibitor TH588 demonstrates anti-tumoral effects alone and in combination with everolimus, 5-FU and gamma-irradiation in neuroendocrine tumor cells.
[So] Source:PLoS One;12(5):e0178375, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Modulation of the redox system in cancer cells has been considered a promising target for anti-cancer therapy. The novel MTH1 inhibitor TH588 proved tremendous potential in terms of cancer cell eradication, yet its specificity has been questioned by recent reports, indicating that TH588 may also induce cancer cell death by alternative mechanisms than MTH1 inhibition. Here we used a panel of heterogeneous neuroendocrine tumor cells in order to assess cellular mechanisms and molecular signaling pathways implicated in the effects of TH588 alone as well as dual-targeting approaches combining TH588 with everolimus, cytotoxic 5-fluorouracil or γ-irradiation. Our results reflect that TH588 alone efficiently decreased the survival of neuroendocrine cancer cells by PI3K-Akt-mTOR axis downregulation, increased apoptosis and oxidative stress. However, in the dual-targeting approaches cell survival was further decreased due to an even stronger downregulation of the PI3K-Akt-mTOR axis and augmentation of apoptosis but not oxidative stress. Furthermore, we could attribute TH588 chemo- and radio-sensitizing properties. Collectively our data not only provide insights into how TH588 exactly kills cancer cells but also depict novel perspectives for combinatorial treatment approaches encompassing TH588.
[Mh] Termos MeSH primário: Protocolos de Quimioterapia Combinada Antineoplásica/farmacologia
Enzimas Reparadoras do DNA/antagonistas & inibidores
Everolimo/farmacologia
Fluoruracila/farmacologia
Tumores Neuroendócrinos/tratamento farmacológico
Tumores Neuroendócrinos/radioterapia
Monoéster Fosfórico Hidrolases/antagonistas & inibidores
Pirimidinas/farmacologia
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Apoptose/efeitos da radiação
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/efeitos da radiação
Regulação para Baixo/efeitos dos fármacos
Regulação para Baixo/efeitos da radiação
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Resistência a Medicamentos Antineoplásicos/efeitos da radiação
Raios gama/uso terapêutico
Seres Humanos
Células Neuroendócrinas/efeitos dos fármacos
Células Neuroendócrinas/efeitos da radiação
Tumores Neuroendócrinos/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Estresse Oxidativo/efeitos da radiação
Fosfatidilinositol 3-Quinases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Radioterapia Adjuvante
Transdução de Sinais/efeitos dos fármacos
Serina-Treonina Quinases TOR/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyrimidines); 0 (TH588 compound); 9HW64Q8G6G (Everolimus); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.1 (MTOR protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.6.1.55 (8-oxodGTPase); EC 6.5.1.- (DNA Repair Enzymes); U3P01618RT (Fluorouracil)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178375



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