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[PMID]:28453858
[Au] Autor:McCormack SE; Li D; Kim YJ; Lee JY; Kim SH; Rapaport R; Levine MA
[Ad] Endereço:Division of Endocrinology and Diabetes, Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
[Ti] Título:Digenic Inheritance of PROKR2 and WDR11 Mutations in Pituitary Stalk Interruption Syndrome.
[So] Source:J Clin Endocrinol Metab;102(7):2501-2507, 2017 Jul 01.
[Is] ISSN:1945-7197
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Context: Pituitary stalk interruption syndrome (PSIS, ORPHA95496) is a congenital defect of the pituitary gland characterized by the triad of a very thin/interrupted pituitary stalk, an ectopic (or absent) posterior pituitary gland, and hypoplasia or aplasia of the anterior pituitary gland. Complex genetic patterns of inheritance of this disorder are increasingly recognized. Objective: The objective of this study was to identify a genetic cause of PSIS in an affected child. Methods: Whole exome sequencing (WES) was performed by using standard techniques, with prioritized genetic variants confirmed via Sanger sequencing. To investigate the effects of one candidate variant on mutant WDR11 function, Western blotting and coimmunofluorescence were used to assess binding capacity, and leptomycin B exposure along with immunofluorescence was used to assess nuclear localization. Results: We describe a child who presented in infancy with combined pituitary hormone deficiencies and whose brain imaging demonstrated a small anterior pituitary, ectopic posterior pituitary, and a thin, interrupted stalk. WES demonstrated heterozygous missense mutations in two genes required for pituitary development, a known loss-of-function mutation in PROKR2 (c.253C>T;p.R85C) inherited from an unaffected mother, and a WDR11 (c.1306A>G;p.I436V) mutation inherited from an unaffected father. Mutant WDR11 loses its capacity to bind to its functional partner, EMX1, and to localize to the nucleus. Conclusions: WES in a child with PSIS and his unaffected family implicates a digenic mechanism of inheritance. In cases of hypopituitarism in which there is incomplete segregation of a monogenic genotype with the phenotype, the possibility that a second genetic locus is involved should be considered.
[Mh] Termos MeSH primário: Predisposição Genética para Doença
Hipopituitarismo/genética
Proteínas de Membrana/genética
Mutação
Hipófise/anormalidades
Proteínas Proto-Oncogênicas/genética
Receptores Acoplados a Proteínas-G/genética
Receptores de Peptídeos/genética
[Mh] Termos MeSH secundário: Exoma/genética
Genótipo
Heterozigoto
Seres Humanos
Hipopituitarismo/congênito
Hipopituitarismo/patologia
Recém-Nascido
Masculino
Linhagem
Síndrome
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (PROKR2 protein, human); 0 (Proto-Oncogene Proteins); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Peptide); 0 (WDR11 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1210/jc.2017-00332


  2 / 4107 MEDLINE  
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[PMID]:29364921
[Au] Autor:Nowak M; Boos A; Kowalewski MP
[Ad] Endereço:Institute of Veterinary Anatomy, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.
[Ti] Título:Luteal and hypophyseal expression of the canine relaxin (RLN) system during pregnancy: Implications for luteotropic function.
[So] Source:PLoS One;13(1):e0191374, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:By acting through its receptors (RXFP1, RXFP2), relaxin (RLN) exerts species-specific effects during pregnancy; possible luteotropic effects through stimulation of prolactin (PRL) release have been suggested. In the domestic dog (Canis lupus familiaris) serum PRL increases in pregnant bitches shortly after RLN appears in the circulation, and a possible functional relationship between the RLN and the PRL systems in regulating progesterone secretion has been implied. Therefore, here (Study 1) the luteal expression and localization of the RLN system was investigated by immunohistochemistry using custom-made antibodies and semi-quantitative PCR, at selected time points during gestation: pre-implantation (d. 8-12), post-implantation (d. 18-25), mid-gestation (d. 35-40) and at normal and antigestagen-induced luteolysis. Further, (Study 2) hypophyseal expression of the RLN system and its spatial association with PRL was assessed. Luteal expression of RLN, but not of its receptors, was time-dependent: it increased significantly following implantation towards mid-gestation and decreased at prepartum. Antigestagen treatment resulted in downregulation of RLN and RXFP2. Whereas RLN was localized in steroidogenic cells, RXFP1 and RXFP2 also stained strongly in macrophages and vascular endothelial cells. The RLN system was detected in the canine adenohypophysis and was co-localized with PRL in hypophyseal lactotrophs. The intraluteal RLN seems to be involved in regulating the canine corpus luteum (CL) in a time-dependent manner. The presence of RLN family members in the adenohypophysis implies their possible involvement in regulating the availability of PRL and other pituitary hormones.
[Mh] Termos MeSH primário: Corpo Lúteo/fisiologia
Hipófise/fisiologia
Relaxina/fisiologia
[Mh] Termos MeSH secundário: Animais
Manutenção do Corpo Lúteo/genética
Manutenção do Corpo Lúteo/fisiologia
Cães
Estrenos/farmacologia
Feminino
Expressão Gênica/efeitos dos fármacos
Imuno-Histoquímica
Modelos Biológicos
Gravidez
Prolactina/sangue
Prolactina/fisiologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Receptores Acoplados a Proteínas-G/genética
Receptores Acoplados a Proteínas-G/fisiologia
Receptores de Peptídeos/genética
Receptores de Peptídeos/fisiologia
Relaxina/sangue
Relaxina/genética
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Estrenes); 0 (RNA, Messenger); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Peptide); 0 (relaxin receptors); 0UT4JLE1CM (aglepristone); 9002-62-4 (Prolactin); 9002-69-1 (Relaxin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191374


  3 / 4107 MEDLINE  
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[PMID]:27771940
[Au] Autor:Agoulnik AI; Agoulnik IU; Hu X; Marugan J
[Ad] Endereço:Department of Human and Molecular Genetics, Herbert Wertheim College of Medicine, Florida International University, Miami, FL, USA.
[Ti] Título:Synthetic non-peptide low molecular weight agonists of the relaxin receptor 1.
[So] Source:Br J Pharmacol;174(10):977-989, 2017 05.
[Is] ISSN:1476-5381
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Relaxin is a small heterodimeric peptide hormone of the insulin/relaxin superfamily produced mainly in female and male reproductive organs. It has potent antifibrotic, vasodilatory and angiogenic effects and regulates the normal function of various physiological systems. Preclinical studies and recent clinical trials have shown the promise of recombinant relaxin as a therapeutic agent in the treatment of cardiovascular and fibrotic diseases. However, there are the universal drawbacks of peptide-based pharmacology that apply to relaxin: a short half-life in vivo requires its continuous delivery, and there are high costs of production, storage and treatment, as well as the possibility of immune responses. All these issues can be resolved by the development of low non-peptide MW agonists of the relaxin receptors which are stable, bioavailable, easily synthesized and specific. In this review, we describe the discovery and characterization of the first series of such compounds. The lead compound, ML290, binds to an allosteric site of the relaxin GPCR, RXFP1. ML290 shows high activity and efficacy, measured by cAMP response, in cells expressing endogenous or transfected RXFP1. Relaxin-like effects of ML290 were shown in various functional cellular assays in vitro. ML290 has excellent absorption, distribution, metabolism and excretion properties and in vivo stability. The identified series of low MW agonists does not activate rodent RXFP1 receptors and thus, the production of a RXFP1 humanized mouse model is needed for preclinical studies. The future analysis and clinical perspectives of relaxin receptor agonists are discussed. LINKED ARTICLES: This article is part of a themed section on Recent Progress in the Understanding of Relaxin Family Peptides and their Receptors. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v174.10/issuetoc.
[Mh] Termos MeSH primário: Receptores Acoplados a Proteínas-G/agonistas
Receptores de Peptídeos/agonistas
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Peso Molecular
Receptores Acoplados a Proteínas-G/metabolismo
Receptores de Peptídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Receptors, G-Protein-Coupled); 0 (Receptors, Peptide); 0 (relaxin receptors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1111/bph.13656


  4 / 4107 MEDLINE  
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[PMID]:29016690
[Au] Autor:Wu GC; Li HW; Tey WG; Lin CJ; Chang CF
[Ad] Endereço:Department of Aquaculture, National Taiwan Ocean University, Keelung, Taiwan.
[Ti] Título:Expression profile of amh/Amh during bi-directional sex change in the protogynous orange-spotted grouper Epinephelus coioides.
[So] Source:PLoS One;12(10):e0185864, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gonadal differentiation is tightly regulated by the initial sex determining gene and the downstream sex-related genes in vertebrates. However, sex change in fish can alter the sexual fate from one sex to the other. Chemical-induced maleness in the protogynous orange-spotted grouper is transient, and a reversible sex change occurs after the chemical treatment is withdrawn. We used these characteristics to study Amh signaling during bi-directional sex change in the grouper. We successfully induced the female-to-male sex change by chemical (aromatase inhibitor, AI, or methyltestosterone, MT) treatment. A dormant gonad (a low proliferation rate of early germ cells and no characteristics of both sexes) was found during the transient phase of reversible male-to-female sex change after the withdrawal of chemical administration. Our results showed that amh (anti-mullerian hormone) and its receptor amhr2 (anti-mullerian hormone receptor type 2) were significantly increased in the gonads during the process of female-to-male sex change. Amh is expressed in the Sertoli cells surrounding the type A spermatogonia in the female-to-male grouper. Male-related gene (dmrt1 and sox9) expression was immediately decreased in MT-terminated males during the reversible male-to-female sex change. However, Amh expression was found in the surrounding cells of type A spermatogonia-like cells during the transient phase of reversible male-to-female sex change. This phenomenon is correlated with the dormancy of type A spermatogonia-like cells. Thus, Amh signaling is suggested to play roles in regulating male differentiation during the female-to-male sex change and in inhibiting type-A spermatogonia-like cell proliferation/differentiation during the reversible male-to-female sex change. We suggest that Amh signaling might play dual roles during bi-directional sex change in grouper.
[Mh] Termos MeSH primário: Hormônio Antimülleriano/genética
Inibidores da Aromatase/farmacologia
Regulação da Expressão Gênica no Desenvolvimento
Metiltestosterona/farmacologia
Receptores de Peptídeos/genética
Receptores de Fatores de Crescimento Transformadores beta/genética
Diferenciação Sexual/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Hormônio Antimülleriano/metabolismo
Feminino
Masculino
Ovário/citologia
Ovário/efeitos dos fármacos
Ovário/metabolismo
Perciformes
Receptores de Peptídeos/metabolismo
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
Fatores de Transcrição SOX9/genética
Fatores de Transcrição SOX9/metabolismo
Células de Sertoli/citologia
Células de Sertoli/efeitos dos fármacos
Células de Sertoli/metabolismo
Processos de Determinação Sexual
Diferenciação Sexual/genética
Transdução de Sinais
Espermatogônias/citologia
Espermatogônias/efeitos dos fármacos
Espermatogônias/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aromatase Inhibitors); 0 (DMRT1 protein); 0 (Receptors, Peptide); 0 (Receptors, Transforming Growth Factor beta); 0 (SOX9 Transcription Factor); 0 (Transcription Factors); 0 (anti-Mullerian hormone receptor); 80497-65-0 (Anti-Mullerian Hormone); V9EFU16ZIF (Methyltestosterone)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185864


  5 / 4107 MEDLINE  
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[PMID]:28990489
[Au] Autor:Tcherkassova J; Tsurkan S; Smirnova G; Borisova J; Moro R; Treshalina H
[Ad] Endereço:1 Pharmaceutical Research Center, PharmAccess, Moscow, Russian Federation.
[Ti] Título:Binding characterization of the targeting drug AIMPILA to AFP receptors in human tumor xenografts.
[So] Source:Tumour Biol;39(10):1010428317734815, 2017 Oct.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The main objective of this study was the characterization of preclinical tumor models based on their expression of alpha-fetoprotein receptor (RECAF) for targeting cancer cells with a new non-covalent complex (AIMPILA) containing alpha-fetoprotein as the carrier and Atractyloside as an apoptosis-inducing agent. For that purpose, we measured the amount of RECAF in the homogenates of the grafted tumors T47D and SW620 and in HepG2 cell extracts. We also determined the alpha-fetoprotein binding specificity of the targeting drug AIMPILA using a solid-phase chemiluminescent assay with AIMPILA-Acrdidinium. We found that RECAF is practically absent from healthy mice tissues (100 Units/mg) where in malignant cells, the amount of alpha-fetoprotein receptors follows this order: T47D (9152 Units/mg) > HepG2 (4865 Units/mg) > SW620 (2839 Units/mg). This agrees with our findings regarding AIMPILA-induced tumor growth inhibition (T47D (T/C = 22%) > HepG2 (T/C = 51%) > SW620 (T/C = 70%), where T/C is the ratio of tumor volume in treated vs control animals). Our results demonstrate that the therapeutic response to the targeting drug AIMPILA strongly depends on the RECAF expression by human tumors and confirms the choice of the tumor models used for an AIMPILA preclinical study.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Atractilosídeo/farmacologia
Sistemas de Liberação de Medicamentos/métodos
Neoplasias Experimentais/tratamento farmacológico
Receptores de Peptídeos/metabolismo
alfa-Fetoproteínas/farmacologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Linhagem Celular Tumoral
Feminino
Seres Humanos
Medições Luminescentes
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Receptors, Peptide); 0 (alpha-Fetoproteins); 0 (alpha-fetoprotein receptor, human); 17754-44-8 (Atractyloside)
[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:171010
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317734815


  6 / 4107 MEDLINE  
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[PMID]:28957388
[Au] Autor:von Volkmann HL; Brønstad I; Gilja OH; R Tronstad R; Sangnes DA; Nortvedt R; Hausken T; Dimcevski G; Fiskerstrand T; Nylund K
[Ad] Endereço:National Centre for Ultrasound in Gastroenterology, Haukeland University Hospital, Bergen, Norway.
[Ti] Título:Prolonged intestinal transit and diarrhea in patients with an activating GUCY2C mutation.
[So] Source:PLoS One;12(9):e0185496, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Increased intestinal hydration by activation of the epithelial enzyme linked receptor guanylate cyclase C (GC-C) is a pharmacological principle for treating constipation. Activating mutations in the GUCY2C gene encoding GC-C cause Familial GUCY2C diarrhea syndrome (FGDS) which has been diagnosed with severe dysmotility. AIM: To investigate gut motility and hormones before and after a meal in FGDS patients and compare with healthy controls (HC). SUBJECTS AND METHODS: Bristol stool chart and stool frequency was assessed. Before and after a meal occlusive and non-occlusive contractions were obtained using ultrasound. A wireless motility capsule (WMC) recorded gut transit time, pH, contractions and pressure. Plasma levels of selected gut hormones were measured at different time points. RESULTS: The FGDS patients had 4 (range 1-10) loose stools/day and prolonged total gut transit time compared to HC, 55.5 h vs 28.5 h, respectively,with significantly increased colon transit time. In FGDS patients, pH in duodenum, small bowel and colon was increased and the number of contractions and the intraluminal pressure were significantly decreased, measured by WMC. Ultrasound showed in small bowel increased number of non-occlusive contractions in the FGDS patients. Serotonin (5-HT) plasma levels in the HC peaked 30 min after the meal, while the FGDS patients had no response. CONCLUSION: Despite having diarrhea, the FGDS patients have prolonged transit time through the gut compared to HC, particularly in colon. The reduced number of intestinal contractions and lack of 5-HT release after a meal in FGDS patients surprisingly resemble colonic motility disturbances seen in patients with constipation.
[Mh] Termos MeSH primário: Diarreia/genética
Diarreia/fisiopatologia
Trânsito Gastrointestinal/fisiologia
Mutação/genética
Receptores Acoplados a Guanilato Ciclase/genética
Receptores de Peptídeos/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Líquidos Corporais
Endoscopia por Cápsula
Diarreia/sangue
Diarreia/diagnóstico por imagem
Feminino
Hormônios/sangue
Seres Humanos
Concentração de Íons de Hidrogênio
Intestinos/patologia
Intestinos/fisiopatologia
Masculino
Meia-Idade
Contração Muscular
Variações Dependentes do Observador
Pressão
Receptores de Enterotoxina
Fatores de Tempo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hormones); 0 (Receptors, Peptide); EC 4.6.1.2 (GUCY2C protein, human); EC 4.6.1.2 (Receptors, Enterotoxin); EC 4.6.1.2 (Receptors, Guanylate Cyclase-Coupled)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185496


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[PMID]:28916678
[Au] Autor:Li P; Wuthrick E; Rappaport JA; Kraft C; Lin JE; Marszalowicz G; Snook AE; Zhan T; Hyslop TM; Waldman SA
[Ad] Endereço:Department of Pathology, Immunology and Laboratory Medicine, College of Medicine, The University of Florida, Gainesville, Florida.
[Ti] Título:GUCY2C Signaling Opposes the Acute Radiation-Induced GI Syndrome.
[So] Source:Cancer Res;77(18):5095-5106, 2017 Sep 15.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High doses of ionizing radiation induce acute damage to epithelial cells of the gastrointestinal (GI) tract, mediating toxicities restricting the therapeutic efficacy of radiation in cancer and morbidity and mortality in nuclear disasters. No approved prophylaxis or therapy exists for these toxicities, in part reflecting an incomplete understanding of mechanisms contributing to the acute radiation-induced GI syndrome (RIGS). Guanylate cyclase C (GUCY2C) and its hormones guanylin and uroguanylin have recently emerged as one paracrine axis defending intestinal mucosal integrity against mutational, chemical, and inflammatory injury. Here, we reveal a role for the GUCY2C paracrine axis in compensatory mechanisms opposing RIGS. Eliminating GUCY2C signaling exacerbated RIGS, amplifying radiation-induced mortality, weight loss, mucosal bleeding, debilitation, and intestinal dysfunction. Durable expression of GUCY2C, guanylin, and uroguanylin mRNA and protein by intestinal epithelial cells was preserved following lethal irradiation inducing RIGS. Oral delivery of the heat-stable enterotoxin (ST), an exogenous GUCY2C ligand, opposed RIGS, a process requiring p53 activation mediated by dissociation from MDM2. In turn, p53 activation prevented cell death by selectively limiting mitotic catastrophe, but not apoptosis. These studies reveal a role for the GUCY2C paracrine hormone axis as a novel compensatory mechanism opposing RIGS, and they highlight the potential of oral GUCY2C agonists (Linzess; Trulance) to prevent and treat RIGS in cancer therapy and nuclear disasters. .
[Mh] Termos MeSH primário: Raios gama/efeitos adversos
Trato Gastrointestinal/efeitos da radiação
Síndrome do Intestino Irritável/prevenção & controle
Lesões Experimentais por Radiação/prevenção & controle
Receptores Acoplados a Guanilato Ciclase/metabolismo
Receptores de Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos da radiação
Proliferação Celular/efeitos da radiação
Neoplasias do Colo/enzimologia
Neoplasias do Colo/patologia
Neoplasias do Colo/radioterapia
Feminino
Hormônios Gastrointestinais/metabolismo
Seres Humanos
Síndrome do Intestino Irritável/enzimologia
Síndrome do Intestino Irritável/etiologia
Linfoma/enzimologia
Linfoma/patologia
Linfoma/radioterapia
Masculino
Melanoma Experimental/enzimologia
Melanoma Experimental/patologia
Melanoma Experimental/radioterapia
Camundongos
Camundongos Endogâmicos C57BL
Peptídeos Natriuréticos/metabolismo
Comunicação Parácrina/efeitos da radiação
Lesões Experimentais por Radiação/enzimologia
Lesões Experimentais por Radiação/etiologia
Receptores de Enterotoxina
Transdução de Sinais/efeitos da radiação
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gastrointestinal Hormones); 0 (Natriuretic Peptides); 0 (Receptors, Peptide); 140653-38-9 (guanylin); 152175-68-3 (uroguanylin); EC 4.6.1.2 (GUCY2C protein, human); EC 4.6.1.2 (Gucy2c protein, mouse); EC 4.6.1.2 (Receptors, Enterotoxin); EC 4.6.1.2 (Receptors, Guanylate Cyclase-Coupled)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170917
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-17-0859


  8 / 4107 MEDLINE  
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[PMID]:28864612
[Au] Autor:Levine R; Krenning EP
[Ad] Endereço:Corporate Communications, Advanced Accelerator Applications, S.A., New York, New York; and rachel.levine@adacap.com.
[Ti] Título:Clinical History of the Theranostic Radionuclide Approach to Neuroendocrine Tumors and Other Types of Cancer: Historical Review Based on an Interview of Eric P. Krenning by Rachel Levine.
[So] Source:J Nucl Med;58(Suppl 2):3S-9S, 2017 Sep.
[Is] ISSN:1535-5667
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In nuclear medicine, the term describes the combination of therapy and diagnostic imaging. In practice, this concept dates back more than 50 years; however, among the most successful examples of theranostics are peptide receptor scintigraphy and peptide receptor radionuclide therapy of neuroendocrine tumors. The development of these modalities through the radiolabeling of somatostatin analogs with various radionuclides has led to a revolution in patient management and established a foundation for expansion of the theranostic principle into other oncology indications. This article provides a review of the evolution and development of the theranostic radionuclide approach to the management of neuroendocrine tumors, as described by the inventor of this technique, Eric P. Krenning, in an interview with Rachel Levine.
[Mh] Termos MeSH primário: Diagnóstico
Tumores Neuroendócrinos/diagnóstico
Tumores Neuroendócrinos/radioterapia
Radioisótopos/uso terapêutico
Radioterapia/história
[Mh] Termos MeSH secundário: História do Século XX
História do Século XXI
Seres Humanos
Entrevistas como Assunto
Marcação por Isótopo
Receptores de Peptídeos/metabolismo
[Pt] Tipo de publicação:HISTORICAL ARTICLE; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Radioisotopes); 0 (Receptors, Peptide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.2967/jnumed.116.186502


  9 / 4107 MEDLINE  
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[PMID]:28864606
[Au] Autor:Reubi JC; Maecke HR
[Ad] Endereço:Institute of Pathology, University of Berne, Berne, Switzerland; and.
[Ti] Título:Approaches to Multireceptor Targeting: Hybrid Radioligands, Radioligand Cocktails, and Sequential Radioligand Applications.
[So] Source:J Nucl Med;58(Suppl 2):10S-16S, 2017 Sep.
[Is] ISSN:1535-5667
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Modern drug discovery highly depends on the identification and validation of the drug targets. Using the method of in vitro quantitative receptor autoradiography, we demonstrated that-for instance, in neuroendocrine tumors-up to 3 receptors can be coexpressed at a relatively high density. In addition, nonendocrine tumors such as breast, prostate, and brain tumors concomitantly express several G protein-coupled receptors at a high density. We propose 3 strategies for exploiting these findings for multireceptor targeting in vivo: use of heterobivalent or heteromultivalent ligands, which may bind simultaneously or monovalently to their different molecular targets; coinjection of a cocktail of radioligands; and sequential injection of different radioligands. Any of these strategies may help to remedy some of the major problems in cancer targeting: heterogeneity, change in phenotype during disease progression, and resistance.
[Mh] Termos MeSH primário: Descoberta de Drogas/métodos
Neoplasias/metabolismo
Receptores de Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Diagnóstico por Imagem
Seres Humanos
Ligantes
Neoplasias/diagnóstico
Neoplasias/terapia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ligands); 0 (Receptors, Peptide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.2967/jnumed.116.186882


  10 / 4107 MEDLINE  
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[PMID]:28862756
[Au] Autor:Haßdenteufel S; Sicking M; Schorr S; Aviram N; Fecher-Trost C; Schuldiner M; Jung M; Zimmermann R; Lang S
[Ad] Endereço:Department of Medical Biochemistry and Molecular Biology, Saarland University, Homburg, Germany.
[Ti] Título:hSnd2 protein represents an alternative targeting factor to the endoplasmic reticulum in human cells.
[So] Source:FEBS Lett;591(20):3211-3224, 2017 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recently, understanding of protein targeting to the endoplasmic reticulum (ER) was expanded by the discovery of multiple pathways that function in parallel to the signal recognition particle (SRP). Guided entry of tail-anchored proteins and SRP independent (SND) are two such targeting pathways described in yeast. So far, no human SND component is functionally characterized. Here, we report hSnd2 as the first constituent of the human SND pathway able to support substrate-specific protein targeting to the ER. Similar to its yeast counterpart, hSnd2 is assumed to function as a membrane-bound receptor preferentially targeting precursors carrying C-terminal transmembrane domains. Our genetic and physical interaction studies show that hSnd2 is part of a complex network of targeting and translocation that is dynamically regulated.
[Mh] Termos MeSH primário: Retículo Endoplasmático/metabolismo
Proteínas de Membrana/genética
Proteínas Nucleares/genética
Subunidades Proteicas/genética
Receptores Citoplasmáticos e Nucleares/genética
Receptores de Peptídeos/genética
Canais de Translocação SEC/genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Regulação da Expressão Gênica
Células HeLa
Seres Humanos
Proteínas de Membrana/antagonistas & inibidores
Proteínas de Membrana/metabolismo
Proteínas Nucleares/metabolismo
Peptídeos/síntese química
Peptídeos/metabolismo
Ligação Proteica
Isoformas de Proteínas/antagonistas & inibidores
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Precursores de Proteínas/genética
Precursores de Proteínas/metabolismo
Sinais Direcionadores de Proteínas/genética
Subunidades Proteicas/metabolismo
Transporte Proteico
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Coelhos
Receptores Citoplasmáticos e Nucleares/metabolismo
Receptores de Peptídeos/metabolismo
Canais de Translocação SEC/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/antagonistas & inibidores
Proteínas de Saccharomyces cerevisiae/metabolismo
Partícula de Reconhecimento de Sinal
Transdução de Sinais
Especificidade por Substrato
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Nuclear Proteins); 0 (Peptides); 0 (Protein Isoforms); 0 (Protein Precursors); 0 (Protein Sorting Signals); 0 (Protein Subunits); 0 (RNA, Small Interfering); 0 (Receptors, Cytoplasmic and Nuclear); 0 (Receptors, Peptide); 0 (SEC Translocation Channels); 0 (Saccharomyces cerevisiae Proteins); 0 (Signal Recognition Particle); 0 (Snd2 protein, S cerevisiae); 0 (WRB protein, human); 0 (signal peptide receptor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12831



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