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[PMID]:29293597
[Au] Autor:Silva SR; Michael TP; Meer EJ; Pinheiro DG; Varani AM; Miranda VFO
[Ad] Endereço:Universidade Estadual Paulista (Unesp), Botucatu, Instituto de Biociências, São Paulo, Brazil.
[Ti] Título:Comparative genomic analysis of Genlisea (corkscrew plants-Lentibulariaceae) chloroplast genomes reveals an increasing loss of the ndh genes.
[So] Source:PLoS One;13(1):e0190321, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the carnivorous plant family Lentibulariaceae, all three genome compartments (nuclear, chloroplast, and mitochondria) have some of the highest rates of nucleotide substitutions across angiosperms. While the genera Genlisea and Utricularia have the smallest known flowering plant nuclear genomes, the chloroplast genomes (cpDNA) are mostly structurally conserved except for deletion and/or pseudogenization of the NAD(P)H-dehydrogenase complex (ndh) genes known to be involved in stress conditions of low light or CO2 concentrations. In order to determine how the cpDNA are changing, and to better understand the evolutionary history within the Genlisea genus, we sequenced, assembled and analyzed complete cpDNA from six species (G. aurea, G. filiformis, G. pygmaea, G. repens, G. tuberosa and G. violacea) together with the publicly available G. margaretae cpDNA. In general, the cpDNA structure among the analyzed Genlisea species is highly similar. However, we found that the plastidial ndh genes underwent a progressive process of degradation similar to the other terrestrial Lentibulariaceae cpDNA analyzed to date, but in contrast to the aquatic species. Contrary to current thinking that the terrestrial environment is a more stressful environment and thus requiring the ndh genes, we provide evidence that in the Lentibulariaceae the terrestrial forms have progressive loss while the aquatic forms have the eleven plastidial ndh genes intact. Therefore, the Lentibulariaceae system provides an important opportunity to understand the evolutionary forces that govern the transition to an aquatic environment and may provide insight into how plants manage water stress at a genome scale.
[Mh] Termos MeSH primário: Cloroplastos/genética
Genoma de Cloroplastos
Magnoliopsida/genética
NADPH Desidrogenase/genética
[Mh] Termos MeSH secundário: Magnoliopsida/classificação
Filogenia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.6.99.1 (NADPH Dehydrogenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190321


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[PMID]:28869767
[Au] Autor:Elegheert J; Brigé A; Van Beeumen J; Savvides SN
[Ad] Endereço:Laboratory for Protein Biochemistry and Biomolecular Engineering (L-ProBE), Department of Biochemistry and Microbiology, Ghent University, Belgium.
[Ti] Título:Structural dissection of Shewanella oneidensis old yellow enzyme 4 bound to a Meisenheimer complex and (nitro)phenolic ligands.
[So] Source:FEBS Lett;591(20):3391-3401, 2017 Oct.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Shewanella oneidensis, a Gram-negative γ-proteobacterium with an extensive redox capacity, possesses four old yellow enzyme (OYE) homologs. Of these, Shewanella yellow enzyme 4 (SYE4) is implicated in resistance to oxidative stress. Here, we present a series of high-resolution crystal structures for SYE4 in the oxidized and reduced states, and in complex with phenolic ligands and the nitro-aromatic explosive picric acid. The structures unmask new features, including the identification of a binding platform for long-chain hydrophobic molecules. Furthermore, we present the first structural observation of a hydride-Meisenheimer complex of picric acid with a flavoenzyme. Overall, our study exposes the binding promiscuity of SYE4 toward a variety of electrophilic substrates and is consistent with a general detoxification function for SYE4.
[Mh] Termos MeSH primário: Anisóis/química
Proteínas de Bactérias/química
Benzaldeídos/química
Cresóis/química
NADPH Desidrogenase/química
Shewanella/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Anisóis/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Benzaldeídos/metabolismo
Sítios de Ligação
Clonagem Molecular
Cresóis/metabolismo
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Interações Hidrofóbicas e Hidrofílicas
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
Ligantes
Modelos Moleculares
NADPH Desidrogenase/genética
NADPH Desidrogenase/metabolismo
Oxirredução
Estresse Oxidativo
Picratos/química
Picratos/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Shewanella/enzimologia
Especificidade por Substrato
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Anisoles); 0 (Bacterial Proteins); 0 (Benzaldehydes); 0 (Cresols); 0 (Isoenzymes); 0 (Ligands); 0 (Picrates); 0 (Recombinant Proteins); 6HT8U7K3AM (mequinol); A49OS0F91S (picric acid); EC 1.6.99.1 (NADPH Dehydrogenase); GF3CGH8D7Z (cresol); O1738X3Y38 (4-hydroxybenzaldehyde)
[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:170905
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12833


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[PMID]:28559282
[Au] Autor:Strand DD; Fisher N; Kramer DM
[Ad] Endereço:From the MSU-DOE Plant Research Laboratory and.
[Ti] Título:The higher plant plastid NAD(P)H dehydrogenase-like complex (NDH) is a high efficiency proton pump that increases ATP production by cyclic electron flow.
[So] Source:J Biol Chem;292(28):11850-11860, 2017 Jul 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cyclic electron flow around photosystem I (CEF) is critical for balancing the photosynthetic energy budget of the chloroplast by generating ATP without net production of NADPH. We demonstrate that the chloroplast NADPH dehydrogenase complex, a homolog to respiratory Complex I, pumps approximately two protons from the chloroplast stroma to the lumen per electron transferred from ferredoxin to plastoquinone, effectively increasing the efficiency of ATP production via CEF by 2-fold compared with CEF pathways involving non-proton-pumping plastoquinone reductases. By virtue of this proton-pumping stoichiometry, we hypothesize that NADPH dehydrogenase not only efficiently contributes to ATP production but operates near thermodynamic reversibility, with potentially important consequences for remediating mismatches in the thylakoid energy budget.
[Mh] Termos MeSH primário: Arabidopsis/enzimologia
Cloroplastos/enzimologia
Modelos Moleculares
NADPH Desidrogenase/metabolismo
Complexo de Proteína do Fotossistema I/metabolismo
Folhas de Planta/enzimologia
Spinacia oleracea/enzimologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Algoritmos
Biocatálise
Domínio Catalítico
Transporte de Elétrons
Ferredoxinas/química
Ferredoxinas/metabolismo
Cinética
NADPH Desidrogenase/química
NADPH Desidrogenase/isolamento & purificação
Complexo de Proteína do Fotossistema I/química
Complexo de Proteína do Fotossistema I/isolamento & purificação
Plastoquinona/química
Plastoquinona/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Subunidades Proteicas/química
Subunidades Proteicas/isolamento & purificação
Subunidades Proteicas/metabolismo
Especificidade da Espécie
Termodinâmica
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ferredoxins); 0 (Photosystem I Protein Complex); 0 (Protein Subunits); 8L70Q75FXE (Adenosine Triphosphate); EC 1.6.99.1 (NADPH Dehydrogenase); OAC30J69CN (Plastoquinone)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.770792


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[PMID]:28322084
[Au] Autor:Halasy K; Szoke B; Janzsó G
[Ad] Endereço:Department of Anatomy and Histology, University of Veterinary Sciences , H-1078 Budapest, István u. 2 . Hungary.
[Ti] Título:Fine structure and synaptology of the nitrergic neurons in medial septum of the rat brain.
[So] Source:Acta Biol Hung;68(1):1-13, 2017 Mar.
[Is] ISSN:0236-5383
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:The nitrergic neuron population and certain aspects of their connectivity (peptidergic inputs, co-localization with GABA, synaptic target distribution) were studied in the medial septum of the rat brain. The histochemical localization of NADPH diaphorase and immunohistochemical identification of nNOS at light and electron microscopic level was applied. Double-labeling experiments with galanin and leucine enkephalin, moreover the postembedding GABA immunogold staining was also carried out. NADPH diaphorase- and nNOS-immunopositive neurons could be identified inside the borders of medial septum. Out of their peptidergic inputs galanin- and leucine enkephaline-immunopositive varicose fibers were found in close apposition with nNOS-immunopositive neurons. Based on fine structural characteristics (large indented nucleus, thin cytoplasmic rim, lack of axosomatic synapses) the nitrergic neurons are suggested to be identical with the septal cholinergic nerve cells. Their boutons established asymmetrical synapses mainly on dendritic shafts and spines, some of which were also nNOS-immunopositive. A lower amount of nNOS-immunopositive boutons of presumably extrinsic origin were found to be GABAergic.
[Mh] Termos MeSH primário: Microscopia Eletrônica/métodos
Neurônios Nitrérgicos/ultraestrutura
Septo do Cérebro/ultraestrutura
Sinapses/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Imuno-Histoquímica/métodos
Masculino
NADPH Desidrogenase/metabolismo
Neurônios Nitrérgicos/metabolismo
Óxido Nítrico Sintase Tipo I/metabolismo
Ratos Wistar
Septo do Cérebro/metabolismo
Sinapses/metabolismo
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
56-12-2 (gamma-Aminobutyric Acid); EC 1.14.13.39 (Nitric Oxide Synthase Type I); EC 1.6.99.1 (NADPH Dehydrogenase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1556/018.68.2017.1.1


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[PMID]:28258322
[Au] Autor:Yoshikawa K; Toya Y; Shimizu H
[Ad] Endereço:Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan.
[Ti] Título:Metabolic engineering of Synechocystis sp. PCC 6803 for enhanced ethanol production based on flux balance analysis.
[So] Source:Bioprocess Biosyst Eng;40(5):791-796, 2017 May.
[Is] ISSN:1615-7605
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Synechocystis sp. PCC 6803 is an attractive host for bio-ethanol production due to its ability to directly convert atmospheric carbon dioxide into ethanol using photosystems. To enhance ethanol production in Synechocystis sp. PCC 6803, metabolic engineering was performed based on in silico simulations, using the genome-scale metabolic model. Comprehensive reaction knockout simulations by flux balance analysis predicted that the knockout of NAD(P)H dehydrogenase enhanced ethanol production under photoautotrophic conditions, where ammonium is the nitrogen source. This deletion inhibits the re-oxidation of NAD(P)H, which is generated by ferredoxin-NADP reductase and imposes re-oxidation in the ethanol synthesis pathway. The effect of deleting the ndhF1 gene, which encodes NADH dehydrogenase subunit 5, on ethanol production was experimentally evaluated using ethanol-producing strains of Synechocystis sp. PCC 6803. The ethanol titer of the ethanol-producing ∆ndhF1 strain increased by 145%, compared with that of the control strain.
[Mh] Termos MeSH primário: Etanol/metabolismo
Engenharia Metabólica/métodos
Modelos Biológicos
Synechocystis
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Técnicas de Silenciamento de Genes
Genoma Bacteriano
NADPH Desidrogenase/genética
NADPH Desidrogenase/metabolismo
Synechocystis/genética
Synechocystis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 3K9958V90M (Ethanol); EC 1.6.99.1 (NADPH Dehydrogenase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170501
[Lr] Data última revisão:
170501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170305
[St] Status:MEDLINE
[do] DOI:10.1007/s00449-017-1744-8


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[PMID]:28167040
[Au] Autor:Sun Y; Geng Q; Du Y; Yang X; Zhai H
[Ad] Endereço:State Key Lab of Crop Biology, Tai'an 271018, Shandong, China; College of Life Sciences, Shandong Agricultural University, Tai'an 271018, Shandong, China.
[Ti] Título:Induction of cyclic electron flow around photosystem I during heat stress in grape leaves.
[So] Source:Plant Sci;256:65-71, 2017 Mar.
[Is] ISSN:1873-2259
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Photosystem II (PSII) in plants is susceptible to high temperatures. The cyclic electron flow (CEF) around PSI is thought to protect both PSII and PSI from photodamage. However, the underlying physiological mechanisms of the photosynthetic electron transport process and the role of CEF in grape at high temperatures remain unclear. To investigate this issue, we examined the responses of PSII energy distribution, the P700 redox state and CEF to high temperatures in grape leaves. After exposing 'Cabernet Sauvignon' leaves to various temperatures (25, 30, 35, 40 and 45°C) in the light (600µmol photons m s ) for 4h, the maximum quantum yield of PSII (Fv/Fm) significantly decreased at high temperatures (40 and 45°C), while the maximum photo-oxidizable P700 (Pm) was not affected. As the temperature increased, higher initial rates of increase in post-illumination Chl fluorescence were detected, which were accompanied by an increase in high energy state quenching (qE). The chloroplast NAD(P)H dehydrogenase-dependent CEF (NDH-dependent CEF) activities were different among grape cultivators. 'Gold Finger' with greater susceptibility to photoinhibition, exhibited lower NDH-dependent CEF activities under acute heat stress than a more heat tolerant 'Cabernet Sauvignon'. These results suggest that overclosure of PSII reaction centers at high temperature resulted in the photoinhibition of PSII, while the stimulation of CEF in grape played an important role in the photoprotection of PSII and PSI at high temperatures through contributing to the generation of a proton gradient.
[Mh] Termos MeSH primário: Adaptação Fisiológica
Transporte de Elétrons
Temperatura Alta
Complexo de Proteína do Fotossistema I/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Folhas de Planta/metabolismo
Vitis/metabolismo
[Mh] Termos MeSH secundário: Clorofila/metabolismo
Fluorescência
Luz
NADPH Desidrogenase/metabolismo
Oxirredução
Fotossíntese
Especificidade da Espécie
Estresse Fisiológico
Vitis/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex); 1406-65-1 (Chlorophyll); EC 1.6.99.1 (NADPH Dehydrogenase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE


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[PMID]:28107586
[Au] Autor:Nett N; Duewel S; Richter AA; Hoebenreich S
[Ad] Endereço:Department of Chemistry, Philipps-Universität Marburg, Hans-Meerwein-Strasse 4, 35032, Marburg, Germany.
[Ti] Título:Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues.
[So] Source:Chembiochem;18(7):685-691, 2017 Apr 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Every year numerous protein engineering and directed evolution studies are published, increasing the knowledge that could be used by protein engineers. Here we test a protein engineering strategy that allows quick access to improved biocatalysts with very little screening effort. Conceptually it is assumed that engineered residues previously identified by rational and random methods induce similar improvements when transferred to family members. In an application to ene-reductases from the Old Yellow Enzyme (OYE) family, the newly created variants were tested with three compounds, revealing more stereocomplementary OYE pairs with potent turnover frequencies (up to 660 h ) and excellent stereoselectivities (up to >99 %). Although systematic prediction of absolute enantioselectivity of OYE variants remains a challenge, "scaffold sampling" was confirmed as a promising addition to protein engineers' collection of strategies.
[Mh] Termos MeSH primário: NADPH Desidrogenase/química
NADPH Desidrogenase/genética
[Mh] Termos MeSH secundário: Acrilatos/química
Ácido Aspártico/química
Cicloexanos/química
Estabilidade Enzimática
Glicina/química
Cinética
Monoterpenos/química
Mutagênese
Engenharia de Proteínas
Estereoisomerismo
Treonina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3-methyl-2-cyclohexen-1-one); 0 (Acrylates); 0 (Cyclohexanes); 0 (Monoterpenes); 2ZD004190S (Threonine); 30KYC7MIAI (Aspartic Acid); 75GK9XIA8I (carvone); EC 1.6.99.1 (NADPH Dehydrogenase); TE7660XO1C (Glycine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600688


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[PMID]:28091926
[Au] Autor:Eliseeva EV; Romanchenko EF; Dyuizen IV; Tyrtyshnikova AV; Pigolkin YI
[Ad] Endereço:Department of General and Clinical Pharmacology, Pacific State Medical University, Vladivostok, Russia. yeliseeff@rbcmail.ru.
[Ti] Título:Effect of Hypotensive Drugs on Dynamics of Nitroxide-Producing Renal Function in Rats with Nephrogenic Hypertension.
[So] Source:Bull Exp Biol Med;162(3):357-361, 2017 Jan.
[Is] ISSN:1573-8221
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An original model of nephrogenic hypertension in rats was used for histochemical mapping of NADPH diaphorase (NO synthase) in various renal segments to examine the effect of hypotensive drugs furosemide, bendazol, and clonidine on the time course of nitroxide production in the kidneys. In various nephron segments, these drugs modulated NO synthesis in different ways. Clonidine induced a stable up-regulation of NO synthesis, which can maintain active vasodilation and gradually diminish the rennin production. Bendazol also enhanced NO synthase activity in renal glomeruli and collecting tubules, but this effect was less pronounced and short lasting. During the first week after injection of bendazol, insignificant elevation of NO synthase activity was observed in the proximal nephron segments. Furosemide exerted the least effect on NO production in kidneys.
[Mh] Termos MeSH primário: Anti-Hipertensivos/farmacologia
Benzimidazóis/farmacologia
Clonidina/farmacologia
Furosemida/farmacologia
Hipertensão Renal/tratamento farmacológico
Óxido Nítrico/biossíntese
[Mh] Termos MeSH secundário: Animais
Animais não Endogâmicos
Regulação da Expressão Gênica
Hipertensão Renal/genética
Hipertensão Renal/metabolismo
Hipertensão Renal/patologia
Glomérulos Renais/efeitos dos fármacos
Glomérulos Renais/metabolismo
Glomérulos Renais/patologia
Túbulos Renais Coletores/efeitos dos fármacos
Túbulos Renais Coletores/metabolismo
Túbulos Renais Coletores/patologia
Masculino
NADPH Desidrogenase/genética
NADPH Desidrogenase/metabolismo
Óxido Nítrico Sintase/genética
Óxido Nítrico Sintase/metabolismo
Ratos
Renina/genética
Renina/metabolismo
Fatores de Tempo
Vasodilatação/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antihypertensive Agents); 0 (Benzimidazoles); 26601THN1D (bendazole); 31C4KY9ESH (Nitric Oxide); 7LXU5N7ZO5 (Furosemide); EC 1.14.13.39 (Nitric Oxide Synthase); EC 1.6.99.1 (NADPH Dehydrogenase); EC 3.4.23.15 (Renin); MN3L5RMN02 (Clonidine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170208
[Lr] Data última revisão:
170208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE
[do] DOI:10.1007/s10517-017-3615-3


  9 / 3429 MEDLINE  
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[PMID]:27447458
[Au] Autor:Melleu FF; Lino-de-Oliveira C; Marino-Neto J
[Ad] Endereço:Department of Physiological Sciences, CCB, Federal University of Santa Catarina, Florianópolis, SC, 88040-900, Brazil. fmelleu@gmail.com.
[Ti] Título:The mesencephalic GCt-ICo complex and tonic immobility in pigeons (Columba livia): a c-Fos study.
[So] Source:Brain Struct Funct;222(3):1253-1265, 2017 Apr.
[Is] ISSN:1863-2661
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Tonic immobility (TI) is a response to a predator attack, or other inescapable danger, characterized by immobility, analgesia and unresponsiveness to external stimuli. In mammals, the periaqueductal gray (PAG) and deep tectal regions control the expression of TI as well as other defensive behaviors. In birds, little is known about the mesencephalic circuitry involved in the control of TI. Here, adult pigeons (both sex, n = 4/group), randomly assigned to non-handled, handled or TI groups, were killed 90 min after manipulations and the brains processed for detection of c-Fos immunoreactive cells (c-Fos-ir, marker for neural activity) in the mesencephalic central gray (GCt) and the adjacent nucleus intercollicularis (ICo). The NADPH-diaphorase staining delineated the boundaries of the sub nuclei in the ICo-GCt complex. Compared to non-handled, TI (but not handling) induced c-Fos-ir in NADPH-diaphorase-rich and -poor regions. After TI, the number of c-Fos-ir increased in the caudal and intermediate areas of the ICo (but not in the GCt), throughout the rostrocaudal axis of the dorsal stratum griseum periventriculare (SGPd) of the optic tectum and in the n. mesencephalicus lateralis pars dorsalis (MLd), which is part of the ascending auditory pathway. These data suggest that inescapable threatening stimuli such as TI may recruit neurons in discrete areas of ICo-GCt complex, deep tectal layer and in ascending auditory circuits that may control the expression of defensive behaviors in pigeons. Additionally, data indicate that the contiguous deep tectal SCPd (but not GCt) in birds may be functionally comparable to the mammalian dorsal PAG.
[Mh] Termos MeSH primário: Resposta de Imobilidade Tônica/fisiologia
Vias Neurais/fisiologia
Substância Cinzenta Periaquedutal/metabolismo
Proteínas Proto-Oncogênicas c-fos/metabolismo
Colículos Superiores/metabolismo
[Mh] Termos MeSH secundário: Animais
Mapeamento Encefálico
Columbidae
Feminino
Masculino
NADPH Desidrogenase/metabolismo
Neurônios/metabolismo
Substância Cinzenta Periaquedutal/citologia
Estatísticas não Paramétricas
Colículos Superiores/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proto-Oncogene Proteins c-fos); EC 1.6.99.1 (NADPH Dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160723
[St] Status:MEDLINE
[do] DOI:10.1007/s00429-016-1275-0


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Fotocópia
[PMID]:26954778
[Au] Autor:Grassi D; Lagunas N; Pinos H; Panzica G; Garcia-Segura LM; Collado P
[Ad] Endereço:Department of Psychobiology, Universidad Nacional de Educacion a Distancia (UNED), Madrid, Spain.
[Ti] Título:NADPH-Diaphorase Colocalizes with GPER and Is Modulated by the GPER Agonist G1 in the Supraoptic and Paraventricular Nuclei of Ovariectomized Female Rats.
[So] Source:Neuroendocrinology;104(1):94-104, 2017.
[Is] ISSN:1423-0194
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Nitric oxide is produced in the brain by the neuronal nitric oxide synthase (nNOS) and carries out a wide range of functions by acting as a neurotransmitter-like molecule. Gonadal hormones are involved in the regulation of the brain nitrergic system. We have previously demonstrated that estradiol, via classical estrogen receptors (ERs), regulates NOS activity in the supraoptic (SON) and paraventricular (PVN) nuclei of the hypothalamus, acting through both ERα and ERß. Magnocellular and parvocellular neurons in the SON and PVN also express the G protein-coupled ER (GPER). In this study, we have assessed whether GPER is also involved in the regulation of nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase in the SON and PVN. Adult female ovariectomized rats were treated with G1, a selective GPER agonist, or with G1 in combination with G15, a selective GPER antagonist. G1 treatment decreased NADPH-diaphorase expression in the SON and in all PVN subnuclei. The treatment with G1 + G15 effectively rescued the G1-dependent decrease in NADPH-diaphorase expression in both brain regions. In addition, the activation of extracellular signal-regulated kinase (ERK) 1/2, one of the kinases involved in the GPER-dependent intracellular signaling pathway and in NOS phosphorylation, was assessed in the same brain nuclei. Treatment with G1 significantly decreased the number of p-ERK 1/2-positive cells in the SON and PVN, while the treatment with G1 + G15 significantly recovered its number to control values. These findings suggest that the activation of GPER in the SON and PVN inhibits the phosphorylation of ERK 1/2, which induces a decrease in NADPH-diaphorase expression.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/efeitos dos fármacos
NADPH Desidrogenase/metabolismo
Núcleo Hipotalâmico Paraventricular/efeitos dos fármacos
Núcleo Hipotalâmico Paraventricular/metabolismo
Quinolinas/farmacologia
Receptores Acoplados a Proteínas-G/agonistas
Receptores Acoplados a Proteínas-G/metabolismo
Núcleo Supraóptico/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Benzodioxóis/farmacologia
Contagem de Células
Feminino
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Ovariectomia
Ratos
Ratos Wistar
Núcleo Supraóptico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-(6-bromo-1,3-benzodioxol-5-yl)-3a,4,5,9b-3H-cyclopenta(c)quinoline); 0 (Benzodioxoles); 0 (GPR30 protein, rat); 0 (Quinolines); 0 (Receptors, G-Protein-Coupled); EC 1.6.99.1 (NADPH Dehydrogenase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170501
[Lr] Data última revisão:
170501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160309
[St] Status:MEDLINE



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