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[PMID]:28353232
[Au] Autor:Guest PC
[Ad] Endereço:Laboratory of Neuroproteomics, Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas (UNICAMP), Rua Monteiro Lobato 255 F/01, Cidade Universitária Zeferino Vaz, 13083-862, Campinas, Brazil. paulcguest@yahoo.com.
[Ti] Título:Sequential Immunoprecipitation of Secretory Vesicle Proteins from Biosynthetically Labelled Cells.
[So] Source:Adv Exp Med Biol;974:157-165, 2017.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pulse radiolabelling of cells with radioactive amino acids is a common method for studying the biosynthesis of proteins. The labelled proteins can then be immunoprecipitated and analysed by electrophoresis and imaging techniques. This chapter presents a protocol for the biosynthetic labelling and immunoprecipitation of pancreatic islet proteins which are known to be affected in psychiatric disorders such as schizophrenia.
[Mh] Termos MeSH primário: Imunoprecipitação/métodos
Insulina/análise
Ilhotas Pancreáticas/química
Pró-Proteína Convertase 2/análise
Vesículas Secretórias/química
[Mh] Termos MeSH secundário: Especificidade de Anticorpos
Cromatografia em Agarose/métodos
Eletroforese/métodos
Glucose/farmacologia
Seres Humanos
Concentração de Íons de Hidrogênio
Imunoprecipitação/instrumentação
Imunoadsorventes
Insulina/biossíntese
Ilhotas Pancreáticas/efeitos dos fármacos
Ilhotas Pancreáticas/metabolismo
Marcação por Isótopo/métodos
Metionina/análise
Pró-Proteína Convertase 2/biossíntese
Vesículas Secretórias/enzimologia
Radioisótopos de Enxofre/análise
Ureia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunosorbents); 0 (Insulin); 0 (Sulfur Radioisotopes); 8W8T17847W (Urea); AE28F7PNPL (Methionine); EC 3.4.21.94 (PCSK2 protein, human); EC 3.4.21.94 (Proprotein Convertase 2); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170330
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-52479-5_11


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[PMID]:28353233
[Au] Autor:Guest PC
[Ad] Endereço:Laboratory of Neuroproteomics, Department of Biochemistry and Tissue Biology, Institute of Biology, University of Campinas (UNICAMP), Cidade Universitária Zeferino Vaz, Rua Monteiro Lobato 255 F/01, 13083-862, Campinas, Brazil. paulcguest@yahoo.com.
[Ti] Título:2D Gel Electrophoresis of Insulin Secretory Granule Proteins from Biosynthetically Labelled Pancreatic Islets.
[So] Source:Adv Exp Med Biol;974:167-174, 2017.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pulse radiolabelling of cells with radioactive amino acids such is a common method for investigating the biosynthetic rates of proteins. In this way, the abundance of newly synthesized proteins can be determined by several proteomic techniques including 2D gel electrophoresis (2DE). This chapter describes a protocol for labelling pancreatic islets with S-methionine in the presence of low and high concentrations of glucose, followed by subcellular fractionation enrichment of secretory granule proteins and analysis of the granule protein contents by 2DE. This demonstrated that the biosynthetic rates of most of the granule proteins are co-ordinately regulated in the presence of stimulatory glucose concentrations.
[Mh] Termos MeSH primário: Eletroforese em Gel Bidimensional/métodos
Insulina/análise
Ilhotas Pancreáticas/química
Vesículas Secretórias/química
[Mh] Termos MeSH secundário: Animais
Fracionamento Celular/métodos
Separação Celular/métodos
Glucose/farmacologia
Insulina/biossíntese
Ilhotas Pancreáticas/efeitos dos fármacos
Ilhotas Pancreáticas/metabolismo
Marcação por Isótopo/métodos
Metionina/análise
Ratos
Radioisótopos de Enxofre/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); 0 (Sulfur Radioisotopes); AE28F7PNPL (Methionine); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170330
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-52479-5_12


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[PMID]:26707235
[Au] Autor:Tóth F; Mallareddy JR; Tourwé D; Lipkowski AW; Bujalska-Zadrozny M; Benyhe S; Ballet S; Tóth G; Kleczkowska P
[Ad] Endereço:Institute of Biochemistry, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, 6726 Szeged, Hungary.
[Ti] Título:Synthesis and binding characteristics of [(3)H]neuromedin N, a NTS2 receptor ligand.
[So] Source:Neuropeptides;57:15-20, 2016 Jun.
[Is] ISSN:1532-2785
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Neurotensin (NT) and its analog neuromedin N (NN) are formed by the processing of a common precursor in mammalian brain tissue and intestines. The biological effects mediated by NT and NN (e.g. analgesia, hypothermia) result from the interaction with G protein-coupled receptors. The goal of this study consisted of the synthesis and radiolabeling of NN, as well as the determination of the binding characteristics of [(3)H]NN and G protein activation by the cold ligand. In homologous displacement studies a weak affinity was determined for NN, with IC50 values of 454nM in rat brain and 425nM in rat spinal cord membranes. In saturation binding experiments the Kd value proved to be 264.8±30.18nM, while the Bmax value corresponded to 3.8±0.2pmol/mg protein in rat brain membranes. The specific binding of [(3)H]NN was saturable, interacting with a single set of homogenous binding sites. In sodium sensitivity experiments, a very weak inhibitory effect of Na(+) ions was observed on the binding of [(3)H]NN, resulting in an IC50 of 150.6mM. In [(35)S]GTPγS binding experiments the Emax value was 112.3±1.4% in rat brain and 112.9±2.4% in rat spinal cord membranes and EC50 values of 0.7nM and 0.79nM were determined, respectively. NN showed moderate agonist activities in stimulating G proteins. The stimulatory effect of NN could be maximally inhibited via use of the NTS2 receptor antagonist levocabastine, but not by the opioid receptor specific antagonist naloxone, nor by the NTS1 antagonist SR48692. These observations allow us to conclude that [(3)H]NN labels NTS2 receptors in rat brain membranes.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Neurotensina/síntese química
Neurotensina/farmacocinética
Fragmentos de Peptídeos/síntese química
Fragmentos de Peptídeos/farmacocinética
Receptores de Neurotensina/metabolismo
Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/diagnóstico por imagem
Guanosina 5'-O-(3-Tiotrifosfato)/metabolismo
Concentração Inibidora 50
Ligantes
Masculino
Ligação Proteica
Ensaio Radioligante
Ratos
Ratos Wistar
Medula Espinal/diagnóstico por imagem
Radioisótopos de Enxofre/farmacocinética
Trítio/farmacocinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 0 (Ntsr2 protein, rat); 0 (Peptide Fragments); 0 (Receptors, Neurotensin); 0 (Sulfur Radioisotopes); 10028-17-8 (Tritium); 102577-25-3 (neuromedin N); 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate)); 39379-15-2 (Neurotensin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151229
[St] Status:MEDLINE


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[PMID]:26636433
[Au] Autor:Wolska N; Rybakowska P; Rasmussen A; Brown M; Montgomery C; Klopocki A; Grundahl K; Scofield RH; Radfar L; Stone DU; Anaya JM; Ice JA; Lessard CJ; Lewis DM; Rhodus NL; Gopalakrishnan R; Huang AJ; Hughes PJ; Rohrer MD; Weisman MH; Venuturupalli S; Guthridge JM; James JA; Sivils KL; Bagavant H; Deshmukh US
[Ad] Endereço:Oklahoma Medical Research Foundation, Oklahoma City.
[Ti] Título:Brief Report: Patients With Primary Sjögren's Syndrome Who Are Positive for Autoantibodies to Tripartite Motif-Containing Protein 38 Show Greater Disease Severity.
[So] Source:Arthritis Rheumatol;68(3):724-9, 2016 Mar.
[Is] ISSN:2326-5205
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Autoantibodies reactive with Ro52 (tripartite motif-containing protein 21 [TRIM21]) are detected in 70% of patients with primary Sjögren's syndrome (SS). TRIM21 belongs to a 34-member C-IV family of TRIM proteins. Although autoantibodies against other TRIM proteins within the C-IV family have been detected in the sera of patients with primary SS, their clinical relevance remains unclear. This study was undertaken to investigate the frequency of anti-TRIM38 in patients with primary SS and evaluate its association with various clinical measures of the disease. METHODS: Serum samples from patients with primary SS (n = 235) and controls (n = 50) were analyzed for reactivity with in vitro-transcribed and -translated (35) S-methionine-labeled TRIM38 protein. The associations of anti-TRIM38 with various laboratory and clinical measures of primary SS were evaluated. Reactivity of anti-TRIM38 with different structural domains of TRIM38 was analyzed. Affinity-purified anti-TRIM38 antibodies were used to immunoprecipitate TRIM21. RESULTS: TRIM38-reactive autoantibodies were detected in the sera of 24 of the 235 patients with primary SS and 2 of the 50 controls. Anti-TRIM38 positivity was significantly associated with the presence of anti-Ro60, anti-Ro52, anti-La, rheumatoid factor, and hypergammaglobulinemia. Clinically, anti-TRIM38 was associated with significantly higher ocular surface staining scores, lower Schirmer's test scores, and minor labial salivary gland biopsy focus scores of ≥3.0. Anti-TRIM38 antibodies mainly recognized the cortactin-binding protein 2 (CortBP-2; amino acids 128-238) and the B30.2/SPRY (amino acids 268-465) domains on TRIM38. Affinity-purified antibodies to TRIM38-CortBP-2 and TRIM38-B30.2/SPRY domains reacted with TRIM21. CONCLUSION: Our data demonstrate that anti-TRIM38 specificity arising in a subset of patients with primary SS is associated with increased severity of the disease.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Proteínas de Transporte/imunologia
Índice de Gravidade de Doença
Síndrome de Sjogren/imunologia
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Hipergamaglobulinemia/imunologia
Imunoprecipitação
Masculino
Metionina
Meia-Idade
Fator Reumatoide/sangue
Ribonucleoproteínas/imunologia
Síndrome de Sjogren/fisiopatologia
Radioisótopos de Enxofre
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Carrier Proteins); 0 (Ribonucleoproteins); 0 (SS-A antigen); 0 (Sulfur Radioisotopes); 0 (TRIM38 protein, human); 9009-79-4 (Rheumatoid Factor); AE28F7PNPL (Methionine)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170301
[Lr] Data última revisão:
170301
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:151205
[St] Status:MEDLINE
[do] DOI:10.1002/art.39497


  5 / 5594 MEDLINE  
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[PMID]:26523979
[Au] Autor:Martin TJ; Sexton T; Kim SA; Severino AL; Peters CM; Young LJ; Childers SR
[Ad] Endereço:Pain Mechanisms Laboratory, Department of Anesthesiology, Wake Forest University Health Sciences, Winston-Salem, NC, United States. Electronic address: tjmartin@wakehealth.edu.
[Ti] Título:Regional differences in mu and kappa opioid receptor G-protein activation in brain in male and female prairie voles.
[So] Source:Neuroscience;311:422-9, 2015 Dec 17.
[Is] ISSN:1873-7544
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prairie voles are unusual mammals in that, like humans, they are capable of forming socially monogamous pair bonds, display biparental care, and engage in alloparental behaviors. Both mu and kappa opioid receptors are involved in behaviors that either establish and maintain, or result from pair bond formation in these animals. Mu and kappa opioid receptors both utilize inhibitory G-proteins in signal transduction mechanisms, however the efficacy by which these receptor subtypes stimulate G-protein signaling across the prairie vole neuraxis is not known. Utilizing [(35)S]GTPγS autoradiography, we characterized the efficacy of G-protein stimulation in coronal sections throughout male and female prairie vole brains by [D-Ala2,NMe-Phe4,Gly-ol5]-enkephalin (DAMGO) and U50,488H, selective mu and kappa opioid agonists, respectively. DAMGO stimulation was highest in the forebrain, similar to that found with other rodent species. U-50,488H produced greater stimulation in prairie voles than is typically seen in mice and rats, particularly in select forebrain areas. DAMGO produced higher stimulation in the core versus the shell of the nucleus accumbens (NAc) in females, while the distribution of U-50,488H stimulation was the opposite. There were no gender differences for U50,488H stimulation of G-protein activity across the regions examined, while DAMGO stimulation was greater in sections from females compared to those from males for NAc core, entopeduncular nucleus, and hippocampus. These data suggest that the kappa opioid system may be more sensitive to manipulation in prairie voles compared to mice and rats, and that female prairie voles may be more sensitive to mu agonists in select brain regions than males.
[Mh] Termos MeSH primário: Arvicolinae/fisiologia
Encéfalo/fisiologia
Guanosina 5´-O-(3-Tiotrifosfato)/metabolismo
Receptores Opioides kappa/metabolismo
Receptores Opioides mu/metabolismo
Caracteres Sexuais
[Mh] Termos MeSH secundário: (trans)-Isômero de 3,4-Dicloro-N-metil-N-(2-(1-pirrolidinil)-ciclo-hexil)-benzenoacetamida/farmacologia
Analgésicos Opioides/farmacologia
Animais
Arvicolinae/anatomia & histologia
Autorradiografia
Encéfalo/anatomia & histologia
Encéfalo/efeitos dos fármacos
Ala(2)-MePhe(4)-Gly(5)-Encefalina/farmacologia
Feminino
Masculino
Receptores Opioides kappa/agonistas
Receptores Opioides mu/agonistas
Radioisótopos de Enxofre
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Analgesics, Opioid); 0 (Receptors, Opioid, kappa); 0 (Receptors, Opioid, mu); 0 (Sulfur Radioisotopes); 100929-53-1 (Enkephalin, Ala(2)-MePhe(4)-Gly(5)-); 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate)); 67198-13-4 (3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151103
[St] Status:MEDLINE


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[PMID]:26476280
[Au] Autor:Nikaido Y; Kurosawa A; Saikawa H; Kuroiwa S; Suzuki C; Kuwabara N; Hoshino H; Obata H; Saito S; Saito T; Osada H; Kobayashi I; Sezutsu H; Takeda S
[Ad] Endereço:Faculty of Science and Technology, Division of Molecular Science, Gunma University, 1-5-1 Tenjin-cho, Kiryu, Gunma 376-8515, Japan.
[Ti] Título:In vivo and in vitro evaluation of novel µ-opioid receptor agonist compounds.
[So] Source:Eur J Pharmacol;767:193-200, 2015 Nov 15.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Opioids are the most effective and widely used drugs for pain treatment. Morphine is an archetypal opioid and is an opioid receptor agonist. Unfortunately, the clinical usefulness of morphine is limited by adverse effects such as analgesic tolerance and addiction. Therefore, it is important to study the development of novel opioid agonists as part of pain control. The analgesic effects of opioids are mediated by three opioid receptors, namely opioid µ-, δ-, and κ-receptors. They belong to the G protein-coupled receptor superfamily and are coupled to Gi proteins. In the present study, we developed a ligand screening system to identify novel opioid µ-receptor agonists that measures [(35)S]GTPγS binding to cell membrane fractions prepared from the fat body of transgenic silkworms expressing µ-receptor-Gi1α fusion protein. We screened the RIKEN Natural Products Depository (NPDepo) chemical library, which contains 5848 compounds, and analogs of hit compounds. We successfully identified a novel, structurally unique compound, that we named GUM1, with agonist activity for the opioid µ-receptor (EC50 of 1.2 µM). The Plantar Test (Hargreaves' Method) demonstrated that subcutaneous injection of 3mg/kg of GUM1 into wild-type rats significantly extended latency time. This extension was also observed in a rat model of morphine tolerance and was inhibited by pre-treatment of naloxone. The unique molecular skeleton of GUM1 makes it an attractive molecule for further ligand-opioid receptor binding studies.
[Mh] Termos MeSH primário: Benzilaminas/agonistas
Benzilaminas/farmacologia
Produtos Biológicos/farmacologia
Piranos/agonistas
Piranos/farmacologia
Receptores Opioides mu/agonistas
[Mh] Termos MeSH secundário: Analgésicos Opioides/agonistas
Analgésicos Opioides/farmacologia
Animais
Animais Geneticamente Modificados
Bombyx
Tolerância a Medicamentos
Guanosina 5'-O-(3-Tiotrifosfato)/metabolismo
Seres Humanos
Masculino
Medição da Dor/efeitos dos fármacos
Ensaio Radioligante
Ratos
Receptores Opioides mu/genética
Radioisótopos de Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Analgesics, Opioid); 0 (Benzylamines); 0 (Biological Products); 0 (GUM1 compound); 0 (OPRM1 protein, human); 0 (Pyrans); 0 (Receptors, Opioid, mu); 0 (Sulfur Radioisotopes); 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate))
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151018
[St] Status:MEDLINE


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[PMID]:26296963
[Au] Autor:Kalloniati C; Krompas P; Karalias G; Udvardi MK; Rennenberg H; Herschbach C; Flemetakis E
[Ad] Endereço:Department of Biotechnology, Agricultural University of Athens, 11855 Athens, Greece.
[Ti] Título:Nitrogen-Fixing Nodules Are an Important Source of Reduced Sulfur, Which Triggers Global Changes in Sulfur Metabolism in Lotus japonicus.
[So] Source:Plant Cell;27(9):2384-400, 2015 Sep.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We combined transcriptomic and biochemical approaches to study rhizobial and plant sulfur (S) metabolism in nitrogen (N) fixing nodules (Fix(+)) of Lotus japonicus, as well as the link of S-metabolism to symbiotic nitrogen fixation and the effect of nodules on whole-plant S-partitioning and metabolism. Our data reveal that N-fixing nodules are thiol-rich organs. Their high adenosine 5'-phosphosulfate reductase activity and strong (35)S-flux into cysteine and its metabolites, in combination with the transcriptional upregulation of several rhizobial and plant genes involved in S-assimilation, highlight the function of nodules as an important site of S-assimilation. The higher thiol content observed in nonsymbiotic organs of N-fixing plants in comparison to uninoculated plants could not be attributed to local biosynthesis, indicating that nodules are an important source of reduced S for the plant, which triggers whole-plant reprogramming of S-metabolism. Enhanced thiol biosynthesis in nodules and their impact on the whole-plant S-economy are dampened in plants nodulated by Fix(-) mutant rhizobia, which in most respects metabolically resemble uninoculated plants, indicating a strong interdependency between N-fixation and S-assimilation.
[Mh] Termos MeSH primário: Loteae/metabolismo
Nódulos Radiculares de Plantas/metabolismo
Nódulos Radiculares de Plantas/microbiologia
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Regulação da Expressão Gênica de Plantas
Loteae/genética
Loteae/fisiologia
Mesorhizobium/genética
Mesorhizobium/fisiologia
Fixação de Nitrogênio
Oxirredutases/genética
Oxirredutases/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Proteínas de Plantas/metabolismo
Compostos de Sulfidrila/metabolismo
Radioisótopos de Enxofre/metabolismo
Radioisótopos de Enxofre/farmacocinética
Simbiose
Distribuição Tecidual
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (NifA protein, Bacteria); 0 (Plant Proteins); 0 (Sulfhydryl Compounds); 0 (Sulfur Radioisotopes); 0 (Transcription Factors); 70FD1KFU70 (Sulfur); EC 1.- (Oxidoreductases); EC 1.18.6.1 (nitrogenase reductase); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.99.2 (adenylylsulfate reductase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150823
[St] Status:MEDLINE
[do] DOI:10.1105/tpc.15.00108


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[PMID]:26253623
[Au] Autor:Erdozain AM; Rubio M; Meana JJ; Fernández-Ruiz J; Callado LF
[Ad] Endereço:Department of Pharmacology, University of the Basque Country UPV/EHU, Bizkaia, Spain Centro de Investigación Biomédica en Red de Salud Mental (CIBERSAM), Madrid, Spain Current address: Neuroscience Paris Seine, CNRS UMR 8246, INSERM U1130, Université Pierre et Marie Curie, Paris, France.
[Ti] Título:Altered CB1 receptor coupling to G-proteins in the post-mortem caudate nucleus and cerebellum of alcoholic subjects.
[So] Source:J Psychopharmacol;29(11):1137-45, 2015 Nov.
[Is] ISSN:1461-7285
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biochemical, pharmacological and genetic evidence suggests the involvement of the endocannabinoid system in alcohol dependence. The aim of the present study was to evaluate the state of CB1 receptors in post-mortem caudate nucleus, hippocampus and cerebellum of alcoholic subjects.CB1 protein levels were measured by Western blot, CB1 receptor density and affinity by [(3)H]WIN55,212-2 saturation assays and CB1 functionality by [(35)S]GTPγS binding assays. Experiments were performed in samples from 24 subjects classified as non-suicidal alcoholics (n = 6), suicidal alcoholics (n = 6), non-alcoholic suicide victims (n = 6) and control subjects (n = 6).Alcoholic subjects presented hyperfunctional CB1 receptors in the caudate nucleus resulting in a higher maximal effect in both alcoholic groups compared to the non-alcoholic groups (p < 0.001). Conversely, in the cerebellum the non-suicidal alcoholic subjects showed hypofunctional receptors with lower maximal effect and potency (p < 0.001). No changes were found in the CB1 protein expression in either region. In the hippocampus of alcoholic subjects, no changes were observed either in the functionality, density or protein levels.Our data support an association between endocannabinoid system activity and alcoholism. The modifications reported here could be either a consequence of high lifetime ethanol consumption or a vulnerability factor to develop alcohol addiction.
[Mh] Termos MeSH primário: Alcoolismo/metabolismo
Núcleo Caudado/metabolismo
Cerebelo/metabolismo
Proteínas Heterotriméricas de Ligação ao GTP/metabolismo
Mudanças Depois da Morte
Receptor CB1 de Canabinoide/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Benzoxazinas/metabolismo
Estudos de Casos e Controles
Núcleo Caudado/diagnóstico por imagem
Cerebelo/diagnóstico por imagem
Feminino
Guanosina 5'-O-(3-Tiotrifosfato)/metabolismo
Hipocampo/diagnóstico por imagem
Hipocampo/metabolismo
Seres Humanos
Masculino
Meia-Idade
Morfolinas/metabolismo
Naftalenos/metabolismo
Ensaio Radioligante
Cintilografia
Suicídio
Radioisótopos de Enxofre/metabolismo
Trítio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzoxazines); 0 (Morpholines); 0 (Naphthalenes); 0 (Receptor, Cannabinoid, CB1); 0 (Sulfur Radioisotopes); 10028-17-8 (Tritium); 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate)); 5H31GI9502 (Win 55212-2); EC 3.6.5.1 (Heterotrimeric GTP-Binding Proteins)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150809
[St] Status:MEDLINE
[do] DOI:10.1177/0269881115599388


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[PMID]:26179037
[Au] Autor:Manning DR; Shen F; Riobo NA
[Ad] Endereço:Department of Pharmacology, Perelman School of Medicine, University of Pennsylvania, 3620 Hamilton Walk, Pennsylvania, PA, 19104-6084, USA, manning@mail.med.upenn.edu.
[Ti] Título:Evaluating the Activity of Smoothened Toward G Proteins Using [³5S]Guanosine 5'-(3-O-thio)triphosphate ([³5S]GTPγS).
[So] Source:Methods Mol Biol;1322:35-44, 2015.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The utilization of heterotrimeric G protein, and in particular those of the Gi, family, by Hedgehogs through Smoothened has become increasingly clear. We describe here a method for evaluating the activity of Smoothened toward G proteins in membranes derived from human embryonic kidney-293 (HEK293) cells. The assay relies on receptor-promoted exchange of GDP for [(35)S]GTPγS on the Gα subunit. The assay is best suited for analysis of the constitutive activity of Smoothened, inverse agonism superimposed on this activity, and neutral antagonism superimposed on inverse agonism. The assay would also be suitable for several other applications requiring a proximal, quantifiable readout of Smoothened activity.
[Mh] Termos MeSH primário: Proteínas de Ligação ao GTP/metabolismo
Guanosina 5´-O-(3-Tiotrifosfato)
Receptores Acoplados a Proteínas-G/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Ligação ao GTP/química
Guanosina 5'-O-(3-Tiotrifosfato)/química
Células HEK293
Seres Humanos
Imunoprecipitação/métodos
Ligação Proteica
Receptores Acoplados a Proteínas-G/química
Receptor Smoothened
Radioisótopos de Enxofre/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Receptors, G-Protein-Coupled); 0 (SMO protein, human); 0 (Smoothened Receptor); 0 (Sulfur Radioisotopes); 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate)); EC 3.6.1.- (GTP-Binding Proteins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150717
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-2772-2_4


  10 / 5594 MEDLINE  
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[PMID]:26160155
[Au] Autor:Zhou L; Stahl EL; Lovell KM; Frankowski KJ; Prisinzano TE; Aubé J; Bohn LM
[Ad] Endereço:Department of Molecular Therapeutics, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA; Department of Neuroscience, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
[Ti] Título:Characterization of kappa opioid receptor mediated, dynorphin-stimulated [35S]GTPγS binding in mouse striatum for the evaluation of selective KOR ligands in an endogenous setting.
[So] Source:Neuropharmacology;99:131-41, 2015 Dec.
[Is] ISSN:1873-7064
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Differential modulation of kappa opioid receptor (KOR) signaling has been a proposed strategy for developing therapies for drug addiction and depression by either activating or blocking this receptor. Hence, there have been significant efforts to generate ligands with diverse pharmacological properties including partial agonists, antagonists, allosteric modulators as well as ligands that selectively activate some pathways while not engaging others (biased agonists). It is becoming increasingly evident that G protein coupled receptor signaling events are context dependent and that what may occur in cell based assays may not be fully indicative of signaling events that occur in the naturally occurring environment. As new ligands are developed, it is important to assess their signaling capacity in relevant endogenous systems in comparison to the performance of endogenous agonists. Since KOR is considered the cognate receptor for dynorphin peptides we have evaluated the selectivity profiles of dynorphin peptides in wild-type (WT), KOR knockout (KOR-KO), and mu opioid receptor knockout (MOR-KO) mice using [35S]GTPγS binding assay in striatal membrane preparations. We find that while the small molecule KOR agonist U69,593, is very selective for KOR, dynorphin peptides promiscuously stimulate G protein signaling in striatum. Furthermore, our studies demonstrate that norBNI and 5'GNTI are highly nonselective antagonists as they maintain full potency and efficacy against dynorphin signaling in the absence of KOR. Characterization of a new KOR antagonist, which may be more selective than NorBNI and 5'GNTI, is presented using this approach.
[Mh] Termos MeSH primário: Corpo Estriado/efeitos dos fármacos
Avaliação Pré-Clínica de Medicamentos/métodos
Dinorfinas/metabolismo
Guanosina 5´-O-(3-Tiotrifosfato)/metabolismo
Receptores Opioides kappa/metabolismo
[Mh] Termos MeSH secundário: Analgésicos Opioides/farmacologia
Animais
Benzenoacetamidas/farmacologia
Corpo Estriado/metabolismo
Dinorfinas/administração & dosagem
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Antagonistas de Entorpecentes/farmacologia
Ligação Proteica
Pirrolidinas/farmacologia
Receptores Opioides kappa/agonistas
Receptores Opioides kappa/antagonistas & inibidores
Receptores Opioides kappa/genética
Transdução de Sinais/efeitos dos fármacos
Radioisótopos de Enxofre
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Analgesics, Opioid); 0 (Benzeneacetamides); 0 (Narcotic Antagonists); 0 (Pyrrolidines); 0 (Receptors, Opioid, kappa); 0 (Sulfur Radioisotopes); 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate)); 74913-18-1 (Dynorphins); J5S4K6TKTG (U 69593)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161201
[Lr] Data última revisão:
161201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150711
[St] Status:MEDLINE



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