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  1 / 5804 MEDLINE  
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[PMID]:28455381
[Au] Autor:Blair S
[Ti] Título:Eric Lewis Blair.
[So] Source:BMJ;357:j2021, 2017 04 28.
[Is] ISSN:1756-1833
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Colecistocinina/imunologia
Gastrinas/imunologia
Fisiologia/história
Secretina/imunologia
[Mh] Termos MeSH secundário: Bioensaio/métodos
Colecistocinina/isolamento & purificação
Gastrinas/isolamento & purificação
História do Século XX
Seres Humanos
Imunoensaio/métodos
Secretina/isolamento & purificação
Reino Unido
[Pt] Tipo de publicação:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE
[Ps] Nome de pessoa como assunto:Blair EL
[Nm] Nome de substância:
0 (Gastrins); 1393-25-5 (Secretin); 9011-97-6 (Cholecystokinin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1136/bmj.j2021


  2 / 5804 MEDLINE  
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[PMID]:28693787
[Au] Autor:Trout AT; Wallihan DB; Serai S; Abu-El-Haija M
[Ad] Endereço:Department of Radiology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH. Electronic address: andrew.trout@cchmc.org.
[Ti] Título:Secretin-Enhanced Magnetic Resonance Cholangiopancreatography for Assessing Pancreatic Secretory Function in Children.
[So] Source:J Pediatr;188:186-191, 2017 Sep.
[Is] ISSN:1097-6833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To assess the accuracy and interrater reproducibility of measurements of pancreatic secretory function by magnetic resonance cholangiopancreatography in response to secretin administration and to describe our experience using the technique to noninvasively assess pancreatic secretory function in a pediatric population. STUDY DESIGN: In the accuracy study, phantoms with varying fluid volume (47-206 mL) were imaged using the clinical quantification sequence. Fluid volume was measured by image segmentation (ImageJ). Measurement accuracy was expressed in terms of error (absolute and percent) relative to known fluid volume. In the reproducibility study and clinical experience, 31 patients with suspected pancreatic disease underwent 33 secretin-enhanced magnetic resonance cholangiopancreatography exams. Two-dimensional T2-weighted, fat-saturated single shot fast spin echo sequences were acquired before and after secretin injection (0.2 µg/kg, max 16 µg). Secreted fluid volume (postsecretin minus presecretin) was independently measured by 2 blinded reviewers. Between reviewer measurement reproducibility was assessed based on correlation (Spearman) and bias (Bland-Altman analysis). RESULTS: For the accuracy study, fluid volumes were measured with mean volume errors of -0.3 to +12.5 mL (percent error -0.03% to +9.0%). For the reproducibility study, the mean secreted fluid volumes measured by reviewer 1 and reviewer 2 were 79.1 ± 54.3 mL (range 5.5-215.4) and 77.2 ± 47.1 mL (range 6.7-198.1 mL), respectively. Measured secreted fluid volumes were very strongly correlated (r = 0.922) between reviewers with a bias of only 1.9 mL (95% limits of agreement -40.5 to 44.2). CONCLUSIONS: Measurement of fluid volume by magnetic resonance imaging is highly accurate with <10% (<13 mL) error in measured volume. Measurements of pancreatic secreted fluid volume in response to secretin by magnetic resonance cholangiopancreatography are highly reproducible with a bias of <2 mL between reviewers.
[Mh] Termos MeSH primário: Colangiopancreatografia por Ressonância Magnética
Insuficiência Pancreática Exócrina/diagnóstico
Testes de Função Pancreática
Secretina/farmacocinética
[Mh] Termos MeSH secundário: Adolescente
Biomarcadores/análise
Criança
Seres Humanos
Pâncreas Exócrino/metabolismo
Pancreatite Crônica/etiologia
Imagens de Fantasmas
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 1393-25-5 (Secretin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE


  3 / 5804 MEDLINE  
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[PMID]:28671689
[Au] Autor:Sampaziotis F; Justin AW; Tysoe OC; Sawiak S; Godfrey EM; Upponi SS; Gieseck RL; de Brito MC; Berntsen NL; Gómez-Vázquez MJ; Ortmann D; Yiangou L; Ross A; Bargehr J; Bertero A; Zonneveld MCF; Pedersen MT; Pawlowski M; Valestrand L; Madrigal P; Georgakopoulos N; Pirmadjid N; Skeldon GM; Casey J; Shu W; Materek PM; Snijders KE; Brown SE; Rimland CA; Simonic I; Davies SE; Jensen KB; Zilbauer M; Gelson WTH; Alexander GJ; Sinha S; Hannan NRF; Wynn TA; Karlsen TH; Melum E; Markaki AE; Saeb-Parsy K; Vallier L
[Ad] Endereço:Wellcome Trust-Medical Research Council Stem Cell Institute, Cambridge Stem Cell Institute, Anne McLaren Laboratory, University of Cambridge, Cambridge, UK.
[Ti] Título:Reconstruction of the mouse extrahepatic biliary tree using primary human extrahepatic cholangiocyte organoids.
[So] Source:Nat Med;23(8):954-963, 2017 Aug.
[Is] ISSN:1546-170X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The treatment of common bile duct (CBD) disorders, such as biliary atresia or ischemic strictures, is restricted by the lack of biliary tissue from healthy donors suitable for surgical reconstruction. Here we report a new method for the isolation and propagation of human cholangiocytes from the extrahepatic biliary tree in the form of extrahepatic cholangiocyte organoids (ECOs) for regenerative medicine applications. The resulting ECOs closely resemble primary cholangiocytes in terms of their transcriptomic profile and functional properties. We explore the regenerative potential of these organoids in vivo and demonstrate that ECOs self-organize into bile duct-like tubes expressing biliary markers following transplantation under the kidney capsule of immunocompromised mice. In addition, when seeded on biodegradable scaffolds, ECOs form tissue-like structures retaining biliary characteristics. The resulting bioengineered tissue can reconstruct the gallbladder wall and repair the biliary epithelium following transplantation into a mouse model of injury. Furthermore, bioengineered artificial ducts can replace the native CBD, with no evidence of cholestasis or occlusion of the lumen. In conclusion, ECOs can successfully reconstruct the biliary tree, providing proof of principle for organ regeneration using human primary cholangiocytes expanded in vitro.
[Mh] Termos MeSH primário: Ductos Biliares Extra-Hepáticos/fisiologia
Células Epiteliais/citologia
Vesícula Biliar/fisiologia
Organoides/fisiologia
Regeneração/fisiologia
Engenharia Tecidual/métodos
[Mh] Termos MeSH secundário: Animais
Ductos Biliares Extra-Hepáticos/citologia
Ductos Biliares Extra-Hepáticos/lesões
Sistema Biliar/citologia
Sistema Biliar/lesões
Sistema Biliar/fisiologia
Transplante de Células
Regulador de Condutância Transmembrana em Fibrose Cística/metabolismo
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Vesícula Biliar/lesões
Seres Humanos
Técnicas In Vitro
Queratina-19/metabolismo
Queratina-7/metabolismo
Camundongos
Organoides/citologia
Organoides/efeitos dos fármacos
Organoides/metabolismo
Secretina/farmacologia
Somatostatina/farmacologia
Tecidos Suporte
gama-Glutamiltransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Keratin-19); 0 (Keratin-7); 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator); 1393-25-5 (Secretin); 51110-01-1 (Somatostatin); EC 2.3.2.2 (gamma-Glutamyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1038/nm.4360


  4 / 5804 MEDLINE  
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[PMID]:28536157
[Au] Autor:Quittot N; Nguyen PT; Nerée AT; Lussier MP; Bourgault S
[Ad] Endereço:Department of Chemistry, Pharmaqam, University of Québec in Montreal, Montreal, QC, Canada H3C 3P8.
[Ti] Título:Identification of a conformational heparin-recognition motif on the peptide hormone secretin: key role for cell surface binding.
[So] Source:Biochem J;474(13):2249-2260, 2017 Jun 26.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Secretin is a peptide hormone that exerts pleiotropic physiological functions by specifically binding to its cognate membrane-bound receptor. The membrane catalysis model of peptide-receptor interactions states that soluble peptidic ligands initially interact with the plasma membrane. This interaction increases the local concentration and structures the peptide, enhancing the rate of receptor binding. However, this model does not consider the dense network of glycosaminoglycans (GAGs) at the surface of eukaryotic cells. These sulfated polysaccharide chains are known to sequester numerous proteic signaling molecules. In the present study, we evaluated the interaction between the peptide hormone secretin and sulfated GAGs and its contribution to cell surface binding. Using GAG-deficient cells and competition experiments with soluble GAGs, we observed by confocal microscopy and flow cytometry that GAGs mediate the sequestration of secretin at the cell surface. Isothermal titration calorimetry and surface plasmon resonance revealed that secretin binds to heparin with dissociation constants ranging between 0.9 and 4 µM. By designing secretin derivatives with a restricted conformational ensemble, we observed that this interaction is mediated by the presence of a specific conformational GAG-recognition motif that decorates the surface of the peptide upon helical folding. The present study identifies secretin as a novel GAG-binding polypeptide and opens new research direction on the functional role of GAGs in the biology of secretin.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Glicosaminoglicanos/metabolismo
Heparina/metabolismo
Secretina/metabolismo
[Mh] Termos MeSH secundário: Heparina/química
Seres Humanos
Conformação Molecular
Ligação Proteica
Conformação Proteica
Secretina/química
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycosaminoglycans); 1393-25-5 (Secretin); 9005-49-6 (Heparin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170525
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170035


  5 / 5804 MEDLINE  
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[PMID]:28368447
[Au] Autor:Harikumar KG; Lau S; Sexton PM; Wootten D; Miller LJ
[Ad] Endereço:Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Scottsdale, Arizona 85259.
[Ti] Título:Coexpressed Class B G Protein-Coupled Secretin and GLP-1 Receptors Self- and Cross-Associate: Impact on Pancreatic Islets.
[So] Source:Endocrinology;158(6):1685-1700, 2017 Jun 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Class B guanine nucleotide-binding protein (G protein)-coupled receptors form symmetrical homodimeric complexes along the lipid face of transmembrane segment 4 (TM4) and can form heterodimeric complexes, although their structure is unknown. The current study demonstrates that the lipid face of TM4 is also the predominant determinant for formation of heteroreceptor complexes between two class B receptors, secretin receptor (SecR) and glucagonlike peptide-1 receptor (GLP-1R), which are expressed on pancreatic islet cells. Because these receptors use the same interface for formation of homo- and heteroreceptor complexes, competitive forces may affect expression of different complexes. Assessment of SecR and GLP-1R dimeric complexes via recombinant expression in Chinese hamster ovary cells revealed that homodimeric receptor complexes were more stable than the heterodimeric complexes, and the homodimeric SecR/SecR is more stable than the GLP-1R/GLP-1R complex. Given the greater tendency for homodimeric compared with heterodimeric complex formation, the heteroreceptor complexes lacked the expression that might have been predicted by geometry alone. Nevertheless, cells coexpressing these receptors formed heterodimeric complexes that correlated with reduced intracellular calcium responses to secretin, but no change in the cyclic adenosine monophosphate responses to each natural agonist. This functional effect was confirmed in pancreatic islets isolated from wild-type and GLP-1R knockout mice. In these cells, the increased calcium response mediated by secretin in the absence of GLP-1R was paralleled by an increased glucose-dependent insulin response, indicating that the heterodimeric receptor complexes modulate secretin responses. Furthermore, the heterodimeric receptor complexes also mediated agonist-induced cross-receptor internalization, a process that could have broad functional significance in sites of natural receptor coexpression.
[Mh] Termos MeSH primário: Receptor do Peptídeo Semelhante ao Glucagon 1/genética
Receptor do Peptídeo Semelhante ao Glucagon 1/metabolismo
Ilhotas Pancreáticas/metabolismo
Secretina/genética
Secretina/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Sinalização do Cálcio/genética
Células Cultivadas
Cricetinae
Cricetulus
Endocitose/genética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Multimerização Proteica/genética
Transporte Proteico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucagon-Like Peptide-1 Receptor); 1393-25-5 (Secretin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00023


  6 / 5804 MEDLINE  
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[PMID]:28162928
[Au] Autor:Madzak A; Olesen SS; Haldorsen IS; Drewes AM; Frøkjær JB
[Ad] Endereço:Department of Radiology, Aalborg University Hospital, Aalborg, Denmark.
[Ti] Título:Secretin-stimulated MRI characterization of pancreatic morphology and function in patients with chronic pancreatitis.
[So] Source:Pancreatology;17(2):228-236, 2017 Mar - Apr.
[Is] ISSN:1424-3911
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/OBJECTIVES: Chronic pancreatitis (CP) is characterized by abnormal pancreatic morphology and impaired endocrine and exocrine function. However, little is known about the relationship between pancreatic morphology and function, and also the association with the etiology and clinical manifestations of CP. The aim was to explore pancreatic morphology and function with advanced MRI in patients with CP and healthy controls (HC) METHODS: Eighty-two patients with CP and 22 HC were enrolled in the study. Morphological imaging parameters included pancreatic main duct diameter, gland volume, fat signal fraction and apparent diffusion coefficient (ADC) values. Functional secretin-stimulated MRI (s-MRI) parameters included pancreatic secretion (bowel fluid volume) and changes in pancreatic ADC value before and after secretin stimulation. Patients were classified according to the modified Cambridge and M-ANNHEIM classification system and fecal elastase was collected. RESULTS: All imaging parameters differentiated CP patients from HC; however, correlations between morphological and functional parameters in CP were weak. Patients with alcoholic and non-alcoholic etiology had comparable s-MRI findings. Fecal elastase was positively correlated to pancreatic gland volume (r = 0.68, P = 0.0016) and negatively correlated to Cambridge classification (r = -0.35, P < 0.001). Additionally, gland volume was negatively correlated to the duration of CP (r = -0.39, P < 0.001) and baseline ADC (r = -0.35, P = 0.027). When stratified by clinical stage (M-ANNHEIM), the pancreatic gland volume was significantly decreased in the severe stages of CP (P = 0.001). CONCLUSIONS: S-MRI provides detailed information about pancreatic morphology and function and represents a promising non-invasive imaging method to characterize pancreatic pathophysiology and may enable monitoring of disease progression in patients with CP.
[Mh] Termos MeSH primário: Imagem por Ressonância Magnética/métodos
Pâncreas/patologia
Pancreatite Crônica/diagnóstico por imagem
Pancreatite Crônica/patologia
Secretina/farmacologia
[Mh] Termos MeSH secundário: Idoso
Fezes/química
Feminino
Seres Humanos
Masculino
Meia-Idade
Elastase Pancreática/análise
Elastase Pancreática/química
Elastase Pancreática/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
1393-25-5 (Secretin); EC 3.4.21.36 (Pancreatic Elastase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170207
[St] Status:MEDLINE


  7 / 5804 MEDLINE  
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[PMID]:28138102
[Au] Autor:Vanderlinde EM; Strozen TG; Hernández SB; Cava F; Howard SP
[Ad] Endereço:Department of Microbiology and Immunology, College of Medicine, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.
[Ti] Título:Alterations in Peptidoglycan Cross-Linking Suppress the Secretin Assembly Defect Caused by Mutation of GspA in the Type II Secretion System.
[So] Source:J Bacteriol;199(8), 2017 Apr 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Gram-negative bacteria, the peptidoglycan (PG) cell wall is a significant structural barrier for outer membrane protein assembly. In , outer membrane multimerization of the type II secretion system (T2SS) secretin ExeD requires the function of the inner membrane assembly factor complex ExeAB. The putative mechanism of the complex involves the reorganization of PG and localization of ExeD, whereby ExeA functions by interacting with PG to form a site for secretin assembly and ExeB forms an interaction with ExeD. This mechanism led us to hypothesize that increasing the pore size of PG would circumvent the requirement for ExeA in the assembly of the ExeD secretin. Growth of in 270 mM Gly reduced PG cross-links by approximately 30% and led to the suppression of secretin assembly defects in strains and in those expressing ExeA mutants by enabling localization of the secretin in the outer membrane. We also established a heterologous ExeD assembly system in and showed that ExeAB and ExeC are the only proteins required for the assembly of the ExeD secretin in and that ExeAB-independent assembly of ExeD can occur upon overexpression of the d,d-carboxypeptidase PBP 5. These results support an assembly model in which, upon binding to PG, ExeA induces multimerization and pore formation in the sacculus, which enables ExeD monomers to interact with ExeB and assemble into a secretin that both is inserted in the outer membrane and crosses the PG layer to interact with the inner membrane platform of the T2SS. The PG layer imposes a strict structural impediment for the assembly of macromolecular structures that span the cell envelope and serve as virulence factors in Gram-negative species. This work revealed that by decreasing PG cross-linking by growth in Gly, the absolute requirement for the PG-binding activity of ExeA in the assembly of the ExeD secretin was alleviated in In a heterologous assembly model in , expression of the carboxypeptidase PBP 5 could relieve the requirement for ExeAB in the assembly of the ExeD secretin. These results provide some mechanistic details of the ExeAB assembly complex function, in which the PG-binding and oligomerization functions of ExeAB are used to create a pore in the PG that is required for secretin assembly.
[Mh] Termos MeSH primário: Aeromonas hydrophila/metabolismo
Proteínas de Bactérias/metabolismo
Regulação Bacteriana da Expressão Gênica/fisiologia
Proteínas de Choque Térmico/metabolismo
Peptidoglicano/metabolismo
Secretina/metabolismo
Sistemas de Secreção Tipo II/metabolismo
[Mh] Termos MeSH secundário: Aeromonas hydrophila/genética
Proteínas de Bactérias/genética
Escherichia coli/citologia
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Choque Térmico/genética
Mutação
Organismos Geneticamente Modificados
Peptidoglicano/química
Secretina/química
Sistemas de Secreção Tipo II/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Heat-Shock Proteins); 0 (Peptidoglycan); 0 (Type II Secretion Systems); 0 (global stress protein A, bacteria); 1393-25-5 (Secretin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


  8 / 5804 MEDLINE  
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[PMID]:28082350
[Au] Autor:Bai J; Chow BK
[Ad] Endereço:School of Biological Sciences, University of Hong Kong, Hong Kong, China.
[Ti] Título:Secretin is involved in sodium conservation through the renin-angiotensin-aldosterone system.
[So] Source:FASEB J;31(4):1689-1697, 2017 Apr.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secretin (SCT) and its receptor (SCTR) are important in fluid regulation at multiple levels the modulation of expression and translocation of renal aquaporin 2 and functions of central angiotensin II (ANGII). The functional interaction of SCT with peripheral ANGII, however, remains unknown. As the ANGII-aldosterone axis dominates the regulation of renal epithelial sodium channel (ENaC) function, we therefore tested whether SCT/SCTR can regulate sodium homeostasis the renin-angiotensin-aldosterone system. SCTR-knockout (SCTR ) mice showed impaired aldosterone synthase (CYP11B2) expression and, consequently, aldosterone release upon intraperitoneal injection of ANGII. Endogenous ANGII production induced by dietary sodium restriction was higher in SCTR than in C57BL/6N [wild-type (WT)] mice, but CYP11B2 and aldosterone synthesis were not elevated. Reduced accumulation of cholesteryl ester-the precursor of aldosterone-was observed in adrenal glands of SCTR mice that were fed a low-sodium diet. Absence of SCTR resulted in elevated basal transcript levels of adrenal CYP11B2 and renal ENaCs. Although transcript and protein levels of ENaCs were similar in WT and SCTR mice under sodium restriction, ENaCs in SCTR mice were less sensitive to amiloride hydrochloride. In summary, the SCT/SCTR axis is involved in aldosterone precursor uptake, and the knockout of SCTR results in defective aldosterone biosynthesis/release and altered sensitivity of ENaCs to amiloride.-Bai, J., Chow, B. K. C. Secretin is involved in sodium conservation through the renin-angiotensin-aldosterone system.
[Mh] Termos MeSH primário: Aldosterona/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
Receptores dos Hormônios Gastrointestinais/metabolismo
Sistema Renina-Angiotensina
Secretina/metabolismo
Sódio na Dieta/metabolismo
[Mh] Termos MeSH secundário: Glândulas Suprarrenais/metabolismo
Amilorida/farmacologia
Angiotensina II/metabolismo
Animais
Citocromo P-450 CYP11B2/genética
Citocromo P-450 CYP11B2/metabolismo
Bloqueadores do Canal de Sódio Epitelial/farmacologia
Canais Epiteliais de Sódio/metabolismo
Rim/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Receptores Acoplados a Proteínas-G/genética
Receptores dos Hormônios Gastrointestinais/genética
Sódio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epithelial Sodium Channel Blockers); 0 (Epithelial Sodium Channels); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Gastrointestinal Hormone); 0 (Sodium, Dietary); 0 (secretin receptor); 11128-99-7 (Angiotensin II); 1393-25-5 (Secretin); 4964P6T9RB (Aldosterone); 7DZO8EB0Z3 (Amiloride); 9NEZ333N27 (Sodium); EC 1.14.15.4 (Cytochrome P-450 CYP11B2)
[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:170114
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600911R


  9 / 5804 MEDLINE  
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[PMID]:28067918
[Au] Autor:Yan Z; Yin M; Xu D; Zhu Y; Li X
[Ad] Endereço:School of Life Sciences, Tsinghua University, Beijing, China.
[Ti] Título:Structural insights into the secretin translocation channel in the type II secretion system.
[So] Source:Nat Struct Mol Biol;24(2):177-183, 2017 Feb.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The secretin GspD of the type II secretion system (T2SS) forms a channel across the outer membrane in Gram-negative bacteria to transport substrates from the periplasm to the extracellular milieu. The lack of an atomic-resolution structure of the GspD channel hinders the investigation of substrate translocation mechanism of T2SS. Here we report cryo-EM structures of two GspD channels (∼1 MDa), from Escherichia coli K12 and Vibrio cholerae, at ∼3 Å resolution. The structures reveal a pentadecameric channel architecture, wherein three rings of GspD N domains form the periplasmic channel. The secretin domain constitutes a novel double ß-barrel channel, with at least 60 ß-strands in each barrel, and is stabilized by S domains. The outer membrane channel is sealed by ß-strand-enriched gates. On the basis of the partially open state captured, we proposed a detailed gate-opening mechanism. Our structures provide a structural basis for understanding the secretin superfamily and the mechanism of substrate translocation in T2SS.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/ultraestrutura
Porinas/ultraestrutura
Sistemas de Secreção Tipo II/ultraestrutura
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência Conservada
Microscopia Crioeletrônica
Escherichia coli/ultraestrutura
Proteínas de Escherichia coli/química
Ativação do Canal Iônico
Modelos Moleculares
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
Secretina/química
Sistemas de Secreção Tipo II/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (GspD protein, E coli); 0 (Porins); 0 (Type II Secretion Systems); 1393-25-5 (Secretin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3350


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[PMID]:27840266
[Au] Autor:Boninsegna E; Manfredi R; Negrelli R; Avesani G; Mehrabi S; Pozzi Mucelli R
[Ad] Endereço:Department of Radiology, Policlinico G.B. Rossi, University of Verona, Italy. Electronic address: boninsegnae@gmail.com.
[Ti] Título:Pancreatic duct stenosis: Differential diagnosis between malignant and benign conditions at secretin-enhanced MRCP.
[So] Source:Clin Imaging;41:137-143, 2017 Jan - Feb.
[Is] ISSN:1873-4499
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To define imaging criteria of benign and malignant nature in patients with main pancreatic duct (MPD) stenosis. MATERIALS-METHODS: S-MRCPs of 35 patients with pancreatitis and 14 with adenocarcinoma were evaluated. RESULTS: Adenocarcinoma caused higher prevalence of complete stenosis (14/14-100% vs 17/35-49%), dilated side-branches (14/14-100% vs 18/35-51%) and lower prevalence of duct-penetrating sign (0/14-0% vs 31/35-89%). The number of stenoses was higher in benign conditions (mean 1.4 Vs 1). Upstream MPD diameter was higher in cancer-induced stenoses (4.5 vs 2.9mm). CONCLUSIONS: Single complete stenosis with dilated side branches, increased MPD caliber and absent duct-penetrating sign are suggestive of malignancy.
[Mh] Termos MeSH primário: Colangiopancreatografia por Ressonância Magnética/métodos
Aumento da Imagem/métodos
Ductos Pancreáticos/diagnóstico por imagem
Neoplasias Pancreáticas/diagnóstico por imagem
[Mh] Termos MeSH secundário: Adulto
Idoso
Constrição Patológica/diagnóstico por imagem
Diagnóstico Diferencial
Feminino
Seres Humanos
Masculino
Meia-Idade
Ductos Pancreáticos/patologia
Neoplasias Pancreáticas/patologia
Reprodutibilidade dos Testes
Estudos Retrospectivos
Secretina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
1393-25-5 (Secretin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170112
[Lr] Data última revisão:
170112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161115
[St] Status:MEDLINE



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