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[PMID]:28711627
[Au] Autor:Bednarska O; Walter SA; Casado-Bedmar M; Ström M; Salvo-Romero E; Vicario M; Mayer EA; Keita ÅV
[Ad] Endereço:Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden; Department of Gastroenterology, Linköping University, Linköping, Sweden.
[Ti] Título:Vasoactive Intestinal Polypeptide and Mast Cells Regulate Increased Passage of Colonic Bacteria in Patients With Irritable Bowel Syndrome.
[So] Source:Gastroenterology;153(4):948-960.e3, 2017 Oct.
[Is] ISSN:1528-0012
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND & AIMS: Irritable bowel syndrome (IBS) is associated with intestinal dysbiosis and symptoms of IBS develop following gastroenteritis. We aimed to study the passage of live bacteria through the colonic epithelium, and determine the role of mast cells (MCs) and vasoactive intestinal polypeptide (VIP) in barrier regulation in IBS and healthy individuals. METHODS: Colon biopsies from 32 women with IBS and 15 age-matched healthy women (controls) were mounted in Ussing chambers; we measured numbers of fluorescently labeled Escherichia coli HS and Salmonella typhimurium that passed through from the mucosal side to the serosal side of the tissue. Some biopsies were exposed to agents that block the VIP receptors (VPAC1 and VPAC2) or MCs. Levels of VIP and tryptase were measured in plasma and biopsy lysates. Number of MCs and MCs that express VIP or VIP receptors were quantified by immunofluorescence. Biopsies from an additional 5 patients with IBS and 4 controls were mounted in chambers and Salmonella were added; we studied passage routes through the epithelium by transmission electron microscopy and expression of tight junctions by confocal microscopy. RESULTS: In colon biopsies from patients with IBS, larger numbers of E coli HS and S typhimurium passed through the epithelium than in biopsies from controls (P < .0005). In transmission electron microscopy analyses, bacteria were found to cross the epithelium via only the transcellular route. Bacterial passage was reduced in biopsies from patients with IBS and controls after addition of antibodies against VPACs or ketotifen, which inhibits MCs. Plasma samples from patients with IBS had higher levels of VIP than plasma samples from controls. Biopsies from patients with IBS had higher levels of tryptase, larger numbers of MCs, and a higher percentage of MCs that express VPAC1 than biopsies from controls. In biopsies from patients with IBS, addition of Salmonella significantly reduced levels of occludin; subsequent addition of ketotifen significantly reversed this effect. CONCLUSIONS: We found that colonic epithelium tissues from patients with IBS have increased translocation of commensal and pathogenic live bacteria compared with controls. The mechanisms of increased translocation include MCs and VIP.
[Mh] Termos MeSH primário: Translocação Bacteriana
Colo/microbiologia
Escherichia coli/fisiologia
Mucosa Intestinal/microbiologia
Síndrome do Intestino Irritável/microbiologia
Mastócitos/microbiologia
Salmonella typhimurium/fisiologia
Peptídeo Intestinal Vasoativo/metabolismo
[Mh] Termos MeSH secundário: Adulto
Biópsia
Estudos de Casos e Controles
Colo/ultraestrutura
Disbiose
Impedância Elétrica
Escherichia coli/patogenicidade
Feminino
Imunofluorescência
Microbioma Gastrointestinal
Seres Humanos
Mucosa Intestinal/ultraestrutura
Síndrome do Intestino Irritável/diagnóstico
Síndrome do Intestino Irritável/metabolismo
Mastócitos/metabolismo
Mastócitos/ultraestrutura
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Meia-Idade
Receptores Tipo II de Peptídeo Intestinal Vasoativo/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
Salmonella typhimurium/patogenicidade
Simbiose
Junções Íntimas/microbiologia
Junções Íntimas/ultraestrutura
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptors, Vasoactive Intestinal Peptide, Type II); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); 37221-79-7 (Vasoactive Intestinal Peptide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170717
[St] Status:MEDLINE


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[PMID]:28490016
[Au] Autor:Ivic I; Fulop BD; Juhasz T; Reglodi D; Toth G; Hashimoto H; Tamas A; Koller A
[Ad] Endereço:Institute for Translational Medicine, University of Pecs, Pecs, Hungary.
[Ti] Título:Backup Mechanisms Maintain PACAP/VIP-Induced Arterial Relaxations in Pituitary Adenylate Cyclase-Activating Polypeptide-Deficient Mice.
[So] Source:J Vasc Res;54(3):180-192, 2017.
[Is] ISSN:1423-0135
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pituitary adenylate cyclase-activating polypeptide (PACAP) is a multifunctional neuropeptide in the VIP/secretin/glucagon peptide superfamily. Two active forms, PACAP1-38 and PACAP1-27, act through G protein-coupled receptors, the PAC1 and VPAC1/2 receptors. Effects of PACAP include potent vasomotor activity. Vasomotor activity and organ-specific vasomotor effects of PACAP-deficient mice have not yet been investigated; thus, the assessment of its physiological importance in vasomotor functions is still missing. We hypothesized that backup mechanisms exist to maintain PACAP pathway activity in PACAP knockout (KO) mice. Thus, we investigated the vasomotor effects of exogenous vasoactive intestinal peptide (VIP) and PACAP polypeptides in PACAP wild-type (WT) and PACAP-deficient (KO) male mice. METHODS: Carotid and femoral arteries were isolated from 8- to 12-week-old male WT and PACAP-KO mice. Vasomotor responses were measured with isometric myography. RESULTS: In the arteries of WT mice the peptides induced relaxations, which were significantly greater to PACAP1-38 than to PACAP1-27 and VIP. In KO mice, PACAP1-38 did not elicit relaxation, whereas PACAP1-27 and VIP elicited significantly greater relaxation in KO mice than in WT mice. The specific PAC1R and VPAC1R antagonist completely blocked the PACAP-induced relaxations. CONCLUSION: Our data suggest that in PACAP deficiency, backup mechanisms maintain arterial relaxations to polypeptides, indicating an important physiological role for the PACAP pathway in the regulation of vascular tone.
[Mh] Termos MeSH primário: Artéria Carótida Primitiva/efeitos dos fármacos
Artéria Femoral/efeitos dos fármacos
Fragmentos de Peptídeos/farmacologia
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/deficiência
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/farmacologia
Peptídeo Intestinal Vasoativo/farmacologia
Vasodilatação/efeitos dos fármacos
Vasodilatadores/farmacologia
[Mh] Termos MeSH secundário: Animais
Artéria Carótida Primitiva/enzimologia
Relação Dose-Resposta a Droga
Artéria Femoral/enzimologia
Genótipo
Técnicas In Vitro
Masculino
Camundongos Knockout
Fenótipo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/agonistas
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/agonistas
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adcyap1 protein, mouse); 0 (Peptide Fragments); 0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); 0 (Vasodilator Agents); 37221-79-7 (Vasoactive Intestinal Peptide)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170511
[St] Status:MEDLINE
[do] DOI:10.1159/000457798


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[PMID]:28385693
[Au] Autor:Jayawardena D; Guzman G; Gill RK; Alrefai WA; Onyuksel H; Dudeja PK
[Ad] Endereço:Department of Biopharmaceutical Sciences, University of Illinois at Chicago, Chicago, Illinois.
[Ti] Título:Expression and localization of VPAC1, the major receptor of vasoactive intestinal peptide along the length of the intestine.
[So] Source:Am J Physiol Gastrointest Liver Physiol;313(1):G16-G25, 2017 Jul 01.
[Is] ISSN:1522-1547
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vasoactive intestinal peptide (VIP) is an endogenous neuropeptide with a broad array of physiological functions in many organs including the intestine. Its actions are mediated via G protein-coupled receptors, and vasoactive intestinal peptide receptor 1 (VPAC1) is the key receptor responsible for majority of VIP's biological activity. The distribution of VPAC1 along the length of the gastrointestinal tract and its subcellular localization in intestinal epithelial cells have not been fully characterized. The current studies were undertaken to determine VPAC1 distribution and localization so that VIP-based therapies can be targeted to specific regions of the intestine. The results indicated that the mRNA levels of VPAC1 showed an abundance pattern of colon > ileum > jejunum in the mouse intestine. In parallel, the VPAC1 protein levels were higher in the mouse colon, followed by the ileum and jejunum. Immunofluorescence studies in mouse colon demonstrated that the receptor was specifically localized to the luminal surface, as was evident by colocalization with the apical marker villin but not with the basolateral marker Na /K -ATPase. In the human intestine, VPAC1 mRNA expression exhibited a distribution similar to that in mouse intestine and was highest in the sigmoid colon. Furthermore, in the human colon, VPAC1 also showed predominantly apical localization. The physiological relevance of the expression and apical localization of VPAC1 remains elusive. We speculate that apical VPAC1 in intestinal epithelial cells may have relevance in recognizing secreted peptides in the intestinal lumen and therefore supports the feasibility of potential therapeutic and targeting use of VIP formulations via oral route to treat gastrointestinal diseases. These studies for the first time present comprehensive data on the relative characterization of vasoactive intestinal peptide (VIP) receptors in the intestinal mucosa. Vasoactive intestinal peptide receptor 1 (VPAC1) was identified as the predominant receptor with higher levels in the colon compared with the small intestine and was mainly localized to the apical membrane. In addition, the findings in the human tissues were consistent with VPAC1 expression in the mouse intestine and open possibilities to target colonic tissues with VIP for treating diseases such as inflammatory bowel disease.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/fisiologia
Intestinos/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
Peptídeo Intestinal Vasoativo/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/genética
Peptídeo Intestinal Vasoativo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (RNA, Messenger); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); 37221-79-7 (Vasoactive Intestinal Peptide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.1152/ajpgi.00081.2017


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[PMID]:28356352
[Au] Autor:Yin Y; de Waal PW; He Y; Zhao LH; Yang D; Cai X; Jiang Y; Melcher K; Wang MW; Xu HE
[Ad] Endereço:From the Van Andel Research Institute - Shanghai Institute of Materia Medica (VARI-SIMM) Center, Center for Structure and Function of Drug Targets, The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai 201203, China.
[Ti] Título:Rearrangement of a polar core provides a conserved mechanism for constitutive activation of class B G protein-coupled receptors.
[So] Source:J Biol Chem;292(24):9865-9881, 2017 Jun 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The glucagon receptor (GCGR) belongs to the secretin-like (class B) family of G protein-coupled receptors (GPCRs) and is activated by the peptide hormone glucagon. The structures of an activated class B GPCR have remained unsolved, preventing a mechanistic understanding of how these receptors are activated. Using a combination of structural modeling and mutagenesis studies, we present here two modes of ligand-independent activation of GCGR. First, we identified a GCGR-specific hydrophobic lock comprising Met-338 and Phe-345 within the IC3 loop and transmembrane helix 6 (TM6) and found that this lock stabilizes the TM6 helix in the inactive conformation. Disruption of this hydrophobic lock led to constitutive G protein and arrestin signaling. Second, we discovered a polar core comprising conserved residues in TM2, TM3, TM6, and TM7, and mutations that disrupt this polar core led to constitutive GCGR activity. On the basis of these results, we propose a mechanistic model of GCGR activation in which TM6 is held in an inactive conformation by the conserved polar core and the hydrophobic lock. Mutations that disrupt these inhibitory elements allow TM6 to swing outward to adopt an active TM6 conformation similar to that of the canonical ß -adrenergic receptor complexed with G protein and to that of rhodopsin complexed with arrestin. Importantly, mutations in the corresponding polar core of several other members of class B GPCRs, including PTH1R, PAC1R, VIP1R, and CRFR1, also induce constitutive G protein signaling, suggesting that the rearrangement of the polar core is a conserved mechanism for class B GPCR activation.
[Mh] Termos MeSH primário: Modelos Moleculares
Receptor Tipo 1 de Hormônio Paratireóideo/agonistas
Receptores de Hormônio Liberador da Corticotropina/agonistas
Receptores de Glucagon/agonistas
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/agonistas
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/agonistas
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Sítios de Ligação
Linhagem Celular
Sequência Conservada
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Ligantes
Mutagênese Sítio-Dirigida
Mutação
Fragmentos de Peptídeos/agonistas
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Receptor Tipo 1 de Hormônio Paratireóideo/química
Receptor Tipo 1 de Hormônio Paratireóideo/genética
Receptor Tipo 1 de Hormônio Paratireóideo/metabolismo
Receptores de Hormônio Liberador da Corticotropina/química
Receptores de Hormônio Liberador da Corticotropina/genética
Receptores de Hormônio Liberador da Corticotropina/metabolismo
Receptores de Glucagon/química
Receptores de Glucagon/genética
Receptores de Glucagon/metabolismo
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/química
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/química
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/genética
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sistemas do Segundo Mensageiro
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ADCYAP1R1 protein, human); 0 (CRF receptor type 1); 0 (Ligands); 0 (PTH1R protein, human); 0 (Peptide Fragments); 0 (Receptor, Parathyroid Hormone, Type 1); 0 (Receptors, Corticotropin-Releasing Hormone); 0 (Receptors, Glucagon); 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (VIPR1 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.782987


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[PMID]:28075510
[Au] Autor:Trabulsi EJ; Tripathi SK; Gomella L; Solomides C; Wickstrom E; Thakur ML
[Ad] Endereço:Department of Urology, Thomas Jefferson University, Philadelphia, PA, USA.
[Ti] Título:Development of a voided urine assay for detecting prostate cancer non-invasively: a pilot study.
[So] Source:BJU Int;119(6):885-895, 2017 Jun.
[Is] ISSN:1464-410X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To validate a hypothesis that prostate cancer can be detected non-invasively by a simple and reliable assay by targeting genomic VPAC receptors expressed on malignant prostate cancer cells shed in voided urine. PATIENTS/SUBJECTS AND METHODS: VPAC receptors were targeted with a specific biomolecule, TP4303, developed in our laboratory. With an Institutional Review Board exempt approval of use of de-identified discarded samples, an aliquot of urine collected as a standard of care, from patients presenting to the urology clinic (207 patients, 176 men and 31 women, aged ≥21 years) was cytospun. The cells were fixed and treated with TP4303 and 4,6-diamidino-2-phenylindole (DAPI). The cells were then observed under a microscope and cells with TP4303 orange fluorescence around the blue (DAPI) nucleus were considered 'malignant' and those only with a blue nucleus were regarded as 'normal'. VPAC presence was validated using receptor blocking assay and cell malignancy was confirmed by prostate cancer gene profile examination. RESULTS: The urine specimens were labelled only with gender and presenting diagnosis, with no personal health identifiers or other clinical data. The assay detected VPAC positive cells in 98.6% of the men with a prostate cancer diagnosis (141), and none of the 10 men with benign prostatic hyperplasia. Of the 56 'normal' patients, 62.5% (35 patients, 10 men and 25 women) were negative for VPAC cells; 19.6% (11, 11 men and no women) had VPAC positive cells; and 17.8% (10, four men and six women) were uninterpretable due to excessive crystals in the urine. Although data are limited, the sensitivity of the assay was 99.3% with a confidence interval (CI) of 96.1-100% and the specificity was 100% with a CI of 69.2-100%. Receptor blocking assay and fluorescence-activated cell sorting (FACS) analyses demonstrated the presence of VPAC receptors and gene profiling examinations confirmed that the cells expressing VPAC receptors were malignant prostate cancer cells. CONCLUSION: These preliminary data are highly encouraging and warrant further evaluation of the assay to serve as a simple and reliable tool to detect prostate cancer non-invasively.
[Mh] Termos MeSH primário: Neoplasias da Próstata/diagnóstico
Neoplasias da Próstata/urina
Receptores Tipo II de Peptídeo Intestinal Vasoativo/análise
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/análise
[Mh] Termos MeSH secundário: Adulto
Feminino
Seres Humanos
Masculino
Projetos Piloto
Urinálise/métodos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Receptors, Vasoactive Intestinal Peptide, Type II); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170112
[St] Status:MEDLINE
[do] DOI:10.1111/bju.13775


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[PMID]:28043808
[Au] Autor:Gherghina FL; Tica AA; Deliu E; Abood ME; Brailoiu GC; Brailoiu E
[Ad] Endereço:Department of Pharmacology, University of Medicine and Pharmacy, Craiova, Romania.
[Ti] Título:Effects of VPAC1 activation in nucleus ambiguus neurons.
[So] Source:Brain Res;1657:297-303, 2017 Feb 15.
[Is] ISSN:1872-6240
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The pituitary adenylyl cyclase-activating polypeptide (PACAP) and its G protein-coupled receptors, PAC1, VPAC1 and VPAC2 form a system involved in a variety of biological processes. Although some sympathetic stimulatory effects of this system have been reported, its central cardiovascular regulatory properties are poorly characterized. VPAC1 receptors are expressed in the nucleus ambiguus (nAmb), a key center controlling cardiac parasympathetic tone. In this study, we report that selective VPAC1 activation in rhodamine-labeled cardiac vagal preganglionic neurons of the rat nAmb produces inositol 1,4,5-trisphosphate receptor-mediated Ca mobilization, membrane depolarization and activation of P/Q-type Ca channels. In vivo, this pathway converges onto transient reduction in heart rate of conscious rats. Therefore we demonstrate a VPAC1-dependent mechanism in the central parasympathetic regulation of the heart rate, adding to the complexity of PACAP-mediated cardiovascular modulation.
[Mh] Termos MeSH primário: Bulbo/metabolismo
Neurônios/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
[Mh] Termos MeSH secundário: Animais
Pressão Sanguínea/efeitos dos fármacos
Pressão Sanguínea/fisiologia
Bradicardia/induzido quimicamente
Bradicardia/metabolismo
Cálcio/metabolismo
Sinalização do Cálcio/efeitos dos fármacos
Sinalização do Cálcio/fisiologia
Células Cultivadas
Retículo Endoplasmático/efeitos dos fármacos
Retículo Endoplasmático/metabolismo
Feminino
Frequência Cardíaca/efeitos dos fármacos
Frequência Cardíaca/fisiologia
Masculino
Bulbo/citologia
Bulbo/efeitos dos fármacos
Potenciais da Membrana/efeitos dos fármacos
Potenciais da Membrana/fisiologia
Técnicas de Rastreamento Neuroanatômico
Neurônios/citologia
Neurônios/efeitos dos fármacos
Parassimpatolíticos/farmacologia
Ratos Sprague-Dawley
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/agonistas
Nervo Vago/citologia
Nervo Vago/efeitos dos fármacos
Nervo Vago/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Parasympatholytics); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE


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[PMID]:27900577
[Au] Autor:Józwiak-Bebenista M; Kowalczyk E
[Ad] Endereço:Department of Pharmacology and Toxicology, The Interfaculty Chair of Basic and Clinical Pharmacology and Toxicology, Medical University of Lodz, Zeligowskiego 7/9, 90-752, Lodz, Poland. marta.jozwiak-bebenista@umed.lodz.pl.
[Ti] Título:Neuroleptic Drugs and PACAP Differentially Affect the mRNA Expression of Genes Encoding PAC1/VPAC Type Receptors.
[So] Source:Neurochem Res;42(4):943-952, 2017 Apr.
[Is] ISSN:1573-6903
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Several lines of evidence suggest that pituitary adenylate cyclase-activating polypeptide (PACAP) is a neuropeptide playing an important role as a neuromodulator. It has been indicated that PACAP is associated with mental diseases, and that regulation of the PACAPergic signals could be a potential target for the treatment of such psychiatric states as schizophrenia. Recent studies have suggested that action of neuroleptic drugs is mediated not only by dopaminergic and serotonergic neurotransmission, but also via neuropeptides which may act both as neurotransmitters and as neuromodulators. The present study examines whether currently-used neuroleptics influence the action of PACAP receptors, whose expression is altered in a schizophrenic patient. Real-time polymerase chain reaction (PCR) was used to examine the effects of haloperidol, olanzapine and amisulpride on the expression of genes coding PAC1/VPAC type receptors in the T98G glioblastoma cell line, as an example of an in vitro model of glial cells. PAC1 mRNA expression fell after 24-h incubation with haloperidol or olanzapine; however the effect was not maintained after 72 h, and haloperidol even up-regulated PAC1 mRNA expression in a dose-dependent manner. All the examined drugs decreased VPAC2 mRNA expression, especially after 72-h incubation. Haloperidol (typical neuroleptic) was distinctly more potent than atypical neuroleptic drugs (olanzapine and amisulpride). In addition, PACAP increased PAC1 and VPAC2 mRNA expression. In conclusion, our findings suggest PACAP receptors may be involved in the mechanism of typical and atypical neuroleptic drugs.
[Mh] Termos MeSH primário: Antipsicóticos/farmacologia
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/biossíntese
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/farmacologia
RNA Mensageiro/biossíntese
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/biossíntese
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/biossíntese
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/fisiologia
Relação Dose-Resposta a Droga
Expressão Gênica
Seres Humanos
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
RNA Mensageiro/genética
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ADCYAP1 protein, human); 0 (Antipsychotic Agents); 0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (RNA, Messenger); 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161201
[St] Status:MEDLINE
[do] DOI:10.1007/s11064-016-2127-2


  8 / 439 MEDLINE  
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[PMID]:27816700
[Au] Autor:Pecoraro V; Sardone LM; Chisari M; Licata F; Li Volsi G; Perciavalle V; Ciranna L; Costa L
[Ad] Endereço:Instituto de Neurociencias, Consejo Superior de Investigaciones Científicas, Universidad Miguel Hernández de Elche, San Juan de Alicante, Spain.
[Ti] Título:A subnanomolar concentration of Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP) pre-synaptically modulates glutamatergic transmission in the rat hippocampus acting through acetylcholine.
[So] Source:Neuroscience;340:551-562, 2017 Jan 06.
[Is] ISSN:1873-7544
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The neuropeptide PACAP modulates synaptic transmission in the hippocampus exerting multiple effects through different receptor subtypes: the underlying mechanisms have not yet been completely elucidated. The neurotransmitter acetylcholine (ACh) also exerts a well-documented modulation of hippocampal synaptic transmission and plasticity. Since PACAP was shown to stimulate ACh release in the hippocampus, we tested whether PACAP acting through ACh might indirectly modulate glutamate-mediated synaptic transmission at a pre- and/or at a post-synaptic level. Using patch clamp on rat hippocampal slices, we tested PACAP effects on stimulation-evoked AMPA receptor-mediated excitatory post-synaptic currents (EPSCs ) in the CA3-CA1 synapse and on spontaneous miniature EPSCs (mEPSCs) in CA1 pyramidal neurons. A subnanomolar dose of PACAP (0.5nM) decreased EPSCs amplitude, enhanced EPSC paired-pulse facilitation (PPF) and reduced mEPSC frequency, indicating a pre-synaptic decrease of glutamate release probability: these effects were abolished by simultaneous blockade of muscarinic and nicotinic ACh receptors, indicating the involvement of endogenous ACh. The effect of subnanomolar PACAP was abolished by a PAC1 receptor antagonist but not by a VPAC receptor blocker. At a higher concentration (10nM), PACAP inhibited EPSCs : this effect persisted in the presence of ACh receptor antagonists and did not involve any change in PPF or in mEPSC frequency, thus was not mediated by ACh and was exerted post- synaptically on CA1 pyramidal neurons. We suggest that a high-affinity PAC1 receptor pre-synaptically modulates hippocampal glutamatergic transmission acting through ACh. Therefore, administration of PACAP at very low doses might be envisaged in cognitive diseases with reduced cholinergic transmission.
[Mh] Termos MeSH primário: Acetilcolina/metabolismo
Ácido Glutâmico/metabolismo
Hipocampo/metabolismo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Transmissão Sináptica/fisiologia
[Mh] Termos MeSH secundário: Animais
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/administração & dosagem
Terminações Pré-Sinápticas/efeitos dos fármacos
Terminações Pré-Sinápticas/metabolismo
Células Piramidais/efeitos dos fármacos
Células Piramidais/metabolismo
Ratos Sprague-Dawley
Ratos Wistar
Receptores de AMPA/antagonistas & inibidores
Receptores de AMPA/metabolismo
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Receptores Tipo II de Peptídeo Intestinal Vasoativo/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
Técnicas de Cultura de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (Receptors, AMPA); 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I); 0 (Receptors, Vasoactive Intestinal Peptide, Type II); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); 3KX376GY7L (Glutamic Acid); N9YNS0M02X (Acetylcholine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


  9 / 439 MEDLINE  
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[PMID]:27453364
[Au] Autor:Sasaki S; Watanabe J; Ohtaki H; Matsumoto M; Murai N; Nakamachi T; Hannibal J; Fahrenkrug J; Hashimoto H; Watanabe H; Sueki H; Honda K; Miyazaki A; Shioda S
[Ad] Endereço:Department of Biochemistry, Showa University School of Medicine, Tokyo, Japan.
[Ti] Título:Pituitary adenylate cyclase-activating polypeptide promotes eccrine gland sweat secretion.
[So] Source:Br J Dermatol;176(2):413-422, 2017 Feb.
[Is] ISSN:1365-2133
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Sweat secretion is the major function of eccrine sweat glands; when this process is disturbed (paridrosis), serious skin problems can arise. To elucidate the causes of paridrosis, an improved understanding of the regulation, mechanisms and factors underlying sweat production is required. Pituitary adenylate cyclase-activating polypeptide (PACAP) exhibits pleiotropic functions that are mediated via its receptors [PACAP-specific receptor (PAC1R), vasoactive intestinal peptide (VIP) receptor type 1 (VPAC1R) and VPAC2R]. Although some studies have suggested a role for PACAP in the skin and several exocrine glands, the effects of PACAP on the process of eccrine sweat secretion have not been examined. OBJECTIVES: To investigate the effect of PACAP on eccrine sweat secretion. METHODS: Reverse transcriptase-polymerase chain reaction and immunostaining were used to determine the expression and localization of PACAP and its receptors in mouse and human eccrine sweat glands. We injected PACAP subcutaneously into the footpads of mice and used the starch-iodine test to visualize sweat-secreting glands. RESULTS: Immunostaining showed PACAP and PAC1R expression by secretory cells from mouse and human sweat glands. PACAP immunoreactivity was also localized in nerve fibres around eccrine sweat glands. PACAP significantly promoted sweat secretion at the injection site, and this could be blocked by the PAC1R-antagonist PACAP6-38. VIP, an agonist of VPAC1R and VPAC2R, failed to induce sweat secretion. CONCLUSIONS: This is the first report demonstrating that PACAP may play a crucial role in sweat secretion via its action on PAC1R located in eccrine sweat glands. The mechanisms underlying the role of PACAP in sweat secretion may provide new therapeutic options to combat sweating disorders.
[Mh] Termos MeSH primário: Glândulas Écrinas/secreção
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/fisiologia
Suor/secreção
[Mh] Termos MeSH secundário: Adulto
Animais
Feminino

Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Fibras Nervosas/metabolismo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/farmacologia
RNA Mensageiro/metabolismo
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/fisiologia
Receptores Tipo II de Peptídeo Intestinal Vasoativo/metabolismo
Receptores Tipo II de Peptídeo Intestinal Vasoativo/fisiologia
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/metabolismo
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (RNA, Messenger); 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (Receptors, Vasoactive Intestinal Peptide, Type II); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I)
[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:160726
[St] Status:MEDLINE
[do] DOI:10.1111/bjd.14885


  10 / 439 MEDLINE  
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[PMID]:28044141
[Au] Autor:Nakata M; Zhang B; Yang Y; Okada T; Shintani N; Hashimoto H; Yada T
[Ad] Endereço:Department of Physiology, Division of Integrative Physiology, Jichi Medical University School of Medicine, Shimotsuke, Tochigi 329-0498, Japan.
[Ti] Título:High-Fat Diet Augments VPAC1 Receptor-Mediated PACAP Action on the Liver, Inducing LAR Expression and Insulin Resistance.
[So] Source:J Diabetes Res;2016:9321395, 2016.
[Is] ISSN:2314-6753
[Cp] País de publicação:Egypt
[La] Idioma:eng
[Ab] Resumo:Pituitary adenylate cyclase-activating polypeptide (PACAP) acts on multiple processes of glucose and energy metabolism. PACAP potentiates insulin action in adipocytes and insulin release from pancreatic -cells, thereby enhancing glucose tolerance. Contrary to these effects at organ levels, PACAP null mice exhibit hypersensitivity to insulin. However, this apparent discrepancy remains to be solved. We aimed to clarify the mechanism underlying the antidiabetic phenotype of PACAP null mice. Feeding with high-fat diet (HFD) impaired insulin sensitivity and glucose tolerance in wild type mice, whereas these changes were prevented in PACAP null mice. HFD also impaired insulin-induced Akt phosphorylation in the liver in wild type mice, but not in PACAP null mice. Using GeneFishing method, HFD increased the leukocyte common antigen-related (LAR) protein tyrosine phosphatase in the liver in wild type mice. Silencing of LAR restored the insulin signaling in the liver of HFD mice. Moreover, the increased LAR expression by HFD was prevented in PACAP null mice. HFD increased the expression of VPAC1 receptor (VPAC1-R), one of three PACAP receptors, in the liver of wild type mice. These data indicate that PACAP-VPAC1-R signaling induces LAR expression and insulin resistance in the liver of HFD mice. Antagonism of VPAC1-R may prevent progression of HFD-induced insulin resistance in the liver, providing a novel antidiabetic strategy.
[Mh] Termos MeSH primário: Dieta Hiperlipídica/efeitos adversos
Resistência à Insulina
Fígado/metabolismo
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/farmacologia
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/fisiologia
[Mh] Termos MeSH secundário: Animais
Expressão Gênica/efeitos dos fármacos
Hipoglicemiantes
Fígado/química
Fígado/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/deficiência
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/genética
RNA Mensageiro/análise
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/antagonistas & inibidores
Receptores Tipo I de Polipeptídeo Intestinal Vasoativo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hypoglycemic Agents); 0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (RNA, Messenger); 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE
[do] DOI:10.1155/2016/9321395



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