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Pesquisa : D12.776.157.530.200.374.600.300 [Categoria DeCS]
Referências encontradas : 103 [refinar]
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[PMID]:28053121
[Au] Autor:Anantharaman A; Tripathi V; Khan A; Yoon JH; Singh DK; Gholamalamdari O; Guang S; Ohlson J; Wahlstedt H; Öhman M; Jantsch MF; Conrad NK; Ma J; Gorospe M; Prasanth SG; Prasanth KV
[Ad] Endereço:Department of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, 601 S Goodwin Avenue, Urbana, IL 61801, USA.
[Ti] Título:ADAR2 regulates RNA stability by modifying access of decay-promoting RNA-binding proteins.
[So] Source:Nucleic Acids Res;45(7):4189-4201, 2017 Apr 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Adenosine deaminases acting on RNA (ADARs) catalyze the editing of adenosine residues to inosine (A-to-I) within RNA sequences, mostly in the introns and UTRs (un-translated regions). The significance of editing within non-coding regions of RNA is poorly understood. Here, we demonstrate that association of ADAR2 with RNA stabilizes a subset of transcripts. ADAR2 interacts with and edits the 3΄UTR of nuclear-retained Cat2 transcribed nuclear RNA (Ctn RNA). In absence of ADAR2, the abundance and half-life of Ctn RNA are significantly reduced. Furthermore, ADAR2-mediated stabilization of Ctn RNA occurred in an editing-independent manner. Unedited Ctn RNA shows enhanced interaction with the RNA-binding proteins HuR and PARN [Poly(A) specific ribonuclease deadenylase]. HuR and PARN destabilize Ctn RNA in absence of ADAR2, indicating that ADAR2 stabilizes Ctn RNA by antagonizing its degradation by PARN and HuR. Transcriptomic analysis identified other RNAs that are regulated by a similar mechanism. In summary, we identify a regulatory mechanism whereby ADAR2 enhances target RNA stability by limiting the interaction of RNA-destabilizing proteins with their cognate substrates.
[Mh] Termos MeSH primário: Adenosina Desaminase/metabolismo
Proteína Semelhante a ELAV 1/metabolismo
Exorribonucleases/metabolismo
Estabilidade de RNA
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Transportador 2 de Aminoácidos Catiônicos/genética
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Camundongos
Edição de RNA
RNA Longo não Codificante/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Cationic Amino Acid Transporter 2); 0 (ELAV-Like Protein 1); 0 (Elavl1 protein, mouse); 0 (RNA, Long Noncoding); 0 (RNA-Binding Proteins); EC 3.1.- (Exoribonucleases); EC 3.1.13.4 (poly(A)-specific ribonuclease); EC 3.5.4.4 (ADAR2 protein, mouse); EC 3.5.4.4 (Adenosine Deaminase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1304


  2 / 103 MEDLINE  
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[PMID]:27783672
[Au] Autor:Singh K; Al-Greene NT; Verriere TG; Coburn LA; Asim M; Barry DP; Allaman MM; Hardbower DM; Delgado AG; Piazuelo MB; Vallance BA; Gobert AP; Wilson KT
[Ad] Endereço:Division of Gastroenterology, Hepatology, and Nutrition, Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee, United States of America.
[Ti] Título:The L-Arginine Transporter Solute Carrier Family 7 Member 2 Mediates the Immunopathogenesis of Attaching and Effacing Bacteria.
[So] Source:PLoS Pathog;12(10):e1005984, 2016 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Solute carrier family 7 member 2 (SLC7A2) is an inducible transporter of the semi-essential amino acid L-arginine (L-Arg), which has been implicated in immune responses to pathogens. We assessed the role of SLC7A2 in murine infection with Citrobacter rodentium, an attaching and effacing enteric pathogen that causes colitis. Induction of SLC7A2 was upregulated in colitis tissues, and localized predominantly to colonic epithelial cells. Compared to wild-type mice, Slc7a2-/-mice infected with C. rodentium had improved survival and decreased weight loss, colon weight, and histologic injury; this was associated with decreased colonic macrophages, dendritic cells, granulocytes, and Th1 and Th17 cells. In infected Slc7a2-/-mice, there were decreased levels of the proinflammatory cytokines G-CSF, TNF-α, IL-1α, IL-1ß, and the chemokines CXCL1, CCL2, CCL3, CCL4, CXCL2, and CCL5. In bone marrow chimeras, the recipient genotype drove the colitis phenotype, indicative of the importance of epithelial, rather than myeloid SLC7A2. Mice lacking Slc7a2 exhibited reduced adherence of C. rodentium to the colonic epithelium and decreased expression of Talin-1, a focal adhesion protein involved in the attachment of the bacterium. The importance of SLC7A2 and Talin-1 in the intimate attachment of C. rodentium and induction of inflammatory response was confirmed in vitro, using conditionally-immortalized young adult mouse colon (YAMC) cells with shRNA knockdown of Slc7a2 or Tln1. Inhibition of L-Arg uptake with the competitive inhibitor, L-lysine (L-Lys), also prevented attachment of C. rodentium and chemokine expression. L-Lys and siRNA knockdown confirmed the role of L-Arg and SLC7A2 in human Caco-2 cells co-cultured with enteropathogenic Escherichia coli. Overexpression of SLC7A2 in human embryonic kidney cells increased bacterial adherence and chemokine expression. Taken together, our data indicate that C. rodentium enhances its own pathogenicity by inducing the expression of SLC7A2 to favor its attachment to the epithelium and thus create its ecological niche.
[Mh] Termos MeSH primário: Transportador 2 de Aminoácidos Catiônicos/metabolismo
Infecções por Enterobacteriaceae/metabolismo
Interações Hospedeiro-Parasita/fisiologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Transportador 2 de Aminoácidos Catiônicos/imunologia
Linhagem Celular
Citrobacter rodentium
Modelos Animais de Doenças
Infecções por Enterobacteriaceae/imunologia
Seres Humanos
Imunofenotipagem
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 2)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161027
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005984


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[PMID]:27413255
[Au] Autor:Hsu YR; Chang SW; Yang CH; Lee YA; Kao TY
[Ad] Endereço:Department of Ophthalmology, National Taiwan University Hospital, No. 7, Chung-Shan South Road, Taipei 10002, Taiwan; Department of Ophthalmology, Far Eastern Memorial Hospital, No. 21, Sec. 2, Nanya South Road, Banqiao District, New Taipei City 22056, Taiwan.
[Ti] Título:Expression Profile of Cationic Amino Acid Transporters in Rats with Endotoxin-Induced Uveitis.
[So] Source:Mediators Inflamm;2016:6586857, 2016.
[Is] ISSN:1466-1861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose. The transcellular arginine transportation via cationic amino acid transporter (CAT) is the rate-limiting step in nitric oxide (NO) synthesis, which is crucial in intraocular inflammation. In this study, CAT isoforms and inducible nitric oxide synthase (iNOS) expression was investigated in endotoxin-induced uveitis (EIU). Methods. EIU was induced in Lewis rats by lipopolysaccharide (LPS) injection. In the treatment group, the rats were injected intraperitoneally with the proteasome inhibitor bortezomib before EIU induction. After 24 hours, leukocyte quantification, NO measurement of the aqueous humor, and histopathological examination were evaluated. The expression of CAT isoforms and iNOS was determined by reverse transcription-polymerase chain reaction, western blotting, and immunofluorescence staining. Nuclear factor-kappa B (NF-κB) binding activity was evaluated by electrophoretic mobility shift assay. The mouse macrophage cell line RAW 264.7 was used to validate the in vivo findings. Results. LPS significantly stimulated iNOS, CAT-2A, and CAT-2B mRNA and protein expression but did not affect CAT-1 in EIU rats and RAW 264.7 cells. Bortezomib attenuated inflammation and inhibited iNOS, CAT-2A, and CAT-2B expression through NF-κB inhibition. Conclusions. CAT-2 and iNOS, but not CAT-1, are specifically involved in EIU. NF-κB is essential in the induction of CAT-2 and iNOS in EIU.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo
Endotoxinas/toxicidade
Uveíte/induzido quimicamente
Uveíte/metabolismo
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/genética
Animais
Western Blotting
Transportador 1 de Aminoácidos Catiônicos/genética
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Transportador 2 de Aminoácidos Catiônicos/genética
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Ensaio de Desvio de Mobilidade Eletroforética
Ensaio de Imunoadsorção Enzimática
Masculino
Camundongos
Óxido Nítrico Sintase Tipo II/genética
Óxido Nítrico Sintase Tipo II/metabolismo
Células RAW 264.7
Ratos
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems, Basic); 0 (Cationic Amino Acid Transporter 1); 0 (Cationic Amino Acid Transporter 2); 0 (Endotoxins); EC 1.14.13.39 (Nitric Oxide Synthase Type II)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE
[do] DOI:10.1155/2016/6586857


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[PMID]:26985027
[Au] Autor:Ezcurra M; Walker DS; Beets I; Swoboda P; Schafer WR
[Ad] Endereço:Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom, Department of Biosciences and Nutrition, Karolinska Institute, Hälsovägen 7, S-141 83 Huddinge, Sweden, and Institute of Healthy Ageing, and Research Department of Genetics, Evolution, and Environment, Unive
[Ti] Título:Neuropeptidergic Signaling and Active Feeding State Inhibit Nociception in Caenorhabditis elegans.
[So] Source:J Neurosci;36(11):3157-69, 2016 Mar 16.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Food availability and nutritional status are important cues affecting behavioral states. Here we report that, in Caenorhabditis elegans, a cascade of dopamine and neuropeptide signaling acts to inhibit nociception in food-poor environments. In the absence of food, animals show decreased sensitivity and increased adaptation to soluble repellents sensed by the polymodal ASH nociceptors. The effects of food on adaptation are affected by dopamine and neuropeptide signaling; dopamine acts via the DOP-1 receptor to decrease adaptation on food, whereas the neuropeptide receptors NPR-1 and NPR-2 act to increase adaptation off food. NPR-1 and NPR-2 function cell autonomously in the ASH neurons to increase adaptation off food, whereas the DOP-1 receptor controls neuropeptide release from interneurons that modulate ASH activity indirectly. These results indicate that feeding state modulates nociception through the interaction of monoamine and neuropeptide signaling pathways.
[Mh] Termos MeSH primário: Adaptação Fisiológica/fisiologia
Comportamento Alimentar/fisiologia
Neuropeptídeos/metabolismo
Nociceptividade/fisiologia
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Adaptação Fisiológica/efeitos dos fármacos
Adaptação Fisiológica/genética
Animais
Animais Geneticamente Modificados
Células CHO
Caenorhabditis elegans/genética
Caenorhabditis elegans/metabolismo
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Proteínas de Ligação ao Cálcio/genética
Proteínas de Ligação ao Cálcio/metabolismo
Transportador 2 de Aminoácidos Catiônicos/genética
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Cobre/farmacologia
Cricetulus
Dopamina/genética
Dopamina/metabolismo
Jejum
Nociceptividade/efeitos dos fármacos
Regiões Promotoras Genéticas/genética
Receptores de Dopamina D1/genética
Receptores de Dopamina D1/metabolismo
Receptores de Neuropeptídeo Y/genética
Receptores de Neuropeptídeo Y/metabolismo
Células Receptoras Sensoriais/efeitos dos fármacos
Células Receptoras Sensoriais/metabolismo
Transdução de Sinais/efeitos dos fármacos
Transdução de Sinais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Calcium-Binding Proteins); 0 (Cationic Amino Acid Transporter 2); 0 (Dop-1 protein, C elegans); 0 (NPR-1 protein, C elegans); 0 (Neuropeptides); 0 (Receptors, Dopamine D1); 0 (Receptors, Neuropeptide Y); 0 (UNC-31 protein, C elegans); 789U1901C5 (Copper); S2QG84156O (cupric chloride); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160318
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1128-15.2016


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[PMID]:26491198
[Au] Autor:Cimen Bozkus C; Elzey BD; Crist SA; Ellies LG; Ratliff TL
[Ad] Endereço:Comparative Pathobiology Department, Purdue University Center for Cancer Research, Purdue University, West Lafayette, IN 47907; and.
[Ti] Título:Expression of Cationic Amino Acid Transporter 2 Is Required for Myeloid-Derived Suppressor Cell-Mediated Control of T Cell Immunity.
[So] Source:J Immunol;195(11):5237-50, 2015 Dec 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myeloid-derived suppressor cells (MDSCs) are a heterogeneous population of immature cells that expand during benign and cancer-associated inflammation and are characterized by their ability to inhibit T cell immunity. Increased metabolism of l-Arginine (l-Arg), through the enzymes arginase 1 and NO synthase 2 (NOS2), is well documented as a major MDSC suppressive mechanism. Therefore, we hypothesized that restricting MDSC uptake of l-Arg is a critical control point to modulate their suppressor activity. Using murine models of prostate-specific inflammation and cancer, we have identified the mechanisms by which extracellular l-Arg is transported into MDSCs. We have shown that MDSCs recruited to localized inflammation and tumor sites upregulate cationic amino acid transporter 2 (Cat2), coordinately with Arg1 and Nos2. Cat2 expression is not induced in MDSCs in peripheral organs. CAT2 contributes to the transport of l-Arg in MDSCs and is an important regulator of MDSC suppressive function. MDSCs that lack CAT2 have significantly reduced suppressive ability ex vivo and display impaired capacity for regulating T cell responses in vivo as evidenced by increased T cell expansion and decreased tumor growth in Cat2(-/-) mice. The abrogation of suppressive function is due to low intracellular l-Arg levels, which leads to the impaired ability of NOS2 to catalyze l-Arg-dependent metabolic processes. Together, these findings demonstrate that CAT2 modulates MDSC function. In the absence of CAT2, MDSCs display diminished capacity for controlling T cell immunity in prostate inflammation and cancer models, where the loss of CAT2 results in enhanced antitumor activity.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/genética
Transportador 2 de Aminoácidos Catiônicos/biossíntese
Células Mieloides/imunologia
Neoplasias da Próstata/imunologia
Linfócitos T/imunologia
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/biossíntese
Animais
Arginase/biossíntese
Arginina/metabolismo
Transporte Biológico
Transportador 2 de Aminoácidos Catiônicos/genética
Linhagem Celular Tumoral
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Células Mieloides/metabolismo
Óxido Nítrico Sintase Tipo II/biossíntese
Neoplasias da Próstata/patologia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Amino Acid Transport Systems, Basic); 0 (Cationic Amino Acid Transporter 2); 0 (Reactive Oxygen Species); 156320-25-1 (Slc7a2 protein, mouse); 94ZLA3W45F (Arginine); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.14.13.39 (Nos2 protein, mouse); EC 3.5.3.1 (Arg1 protein, mouse); EC 3.5.3.1 (Arginase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:151023
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1500959


  6 / 103 MEDLINE  
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[PMID]:25619276
[Au] Autor:Wang Q; Zhou T
[Ad] Endereço:School of Mathematics and Computational Science, Sun Yat-Sen University, Guangzhou 510275, People's Republic of China.
[Ti] Título:Dynamical analysis of mCAT2 gene models with CTN-RNA nuclear retention.
[So] Source:Phys Biol;12(1):016010, 2015 Jan 26.
[Is] ISSN:1478-3975
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:As an experimentally well-studied nuclear-retained RNA, CTN-RNA plays a significant role in many aspects of mouse cationic amino acid transporter 2 (mCAT2) gene expression, but relevant dynamical mechanisms have not been completely clarified. Here we first show that CTN-RNA nuclear retention can not only reduce pre-mCAT2 RNA noise but also mediate its coding partner noise. Then, by collecting experimental observations, we conjecture a heterodimer formed by two proteins, p54(nrb) and PSP1, named p54(nrb)-PSP1, by which CTN-RNA can positively regulate the expression of nuclear mCAT2 RNA. Therefore, we construct a sequestration model at the molecular level. By analyzing the dynamics of this model system, we demonstrate why most nuclear-retained CTN-RNAs stabilize at the periphery of paraspeckles, how CTN-RNA regulates its protein-coding partner, and how the mCAT2 gene can maintain a stable expression. In particular, we obtain results that can easily explain the experimental phenomena observed in two cases, namely, when cells are stressed and unstressed. Our entire analysis not only reveals that CTN-RNA nuclear retention may play an essential role in indirectly preventing diseases but also lays the foundation for further study of other members of the nuclear-regulatory RNA family with more complicated molecular mechanisms.
[Mh] Termos MeSH primário: Transportador 2 de Aminoácidos Catiônicos/genética
Núcleo Celular/genética
Modelos Genéticos
RNA Nuclear/metabolismo
[Mh] Termos MeSH secundário: Animais
Camundongos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Nuclear/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 2); 0 (RNA, Messenger); 0 (RNA, Nuclear)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:150127
[Lr] Data última revisão:
150127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150127
[St] Status:MEDLINE
[do] DOI:10.1088/1478-3975/12/1/016010


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[PMID]:25243167
[Au] Autor:Ferrigno A; Rizzo V; Bianchi A; Di Pasqua LG; Berardo C; Richelmi P; Vairetti M
[Ad] Endereço:Department of Internal Medicine and Therapeutics, University of Pavia, 27100 Pavia, Italy.
[Ti] Título:Changes in ADMA/DDAH pathway after hepatic ischemia/reperfusion injury in rats: the role of bile.
[So] Source:Biomed Res Int;2014:627434, 2014.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We investigated the effects of hepatic ischemia/reperfusion (I/R) injury on asymmetric dimethylarginine (ADMA, a nitric oxide synthase inhibitor), protein methyltransferase (PRMT) and dimethylarginine dimethylaminohydrolase (DDAH) (involved, resp., in ADMA synthesis and degradation), and the cationic transporter (CAT). Male Wistar rats were subjected to 30 or 60 min hepatic ischemia followed by 60 min reperfusion. ADMA levels in serum and bile were determined. Tissue ADMA, DDAH activity, DDAH-1 and CAT-2 protein, DDAH-1 and PRMT-1 mRNA expression, GSH/GSSG, ROS production, and lipid peroxidation were detected. ADMA was found in bile. I/R increased serum and bile ADMA levels while an intracellular decrease was detected after 60 min ischemia. Decreased DDAH activity, mRNA, and protein expression were observed at the end of reperfusion. No significant difference was observed in GSH/GSSG, ROS, lipid peroxidation, and CAT-2; a decrease in PRMT-1 mRNA expression was found after I/R. Liver is responsible for the biliary excretion of ADMA, as documented here for the first time, and I/R injury is associated with an oxidative stress-independent alteration in DDAH activity. These data are a step forward in the understanding of the pathways that regulate serum, tissue, and biliary levels of ADMA in which DDAH enzyme plays a crucial role.
[Mh] Termos MeSH primário: Amidoidrolases/metabolismo
Arginina/análogos & derivados
Bile/fisiologia
Fígado/lesões
Traumatismo por Reperfusão/metabolismo
[Mh] Termos MeSH secundário: Amidoidrolases/análise
Amidoidrolases/genética
Animais
Arginina/análise
Arginina/metabolismo
Bile/química
Transportador 2 de Aminoácidos Catiônicos/análise
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Modelos Animais de Doenças
Fígado/química
Fígado/metabolismo
Masculino
Especificidade de Órgãos
Estresse Oxidativo
Proteína-Arginina N-Metiltransferases/análise
Proteína-Arginina N-Metiltransferases/genética
Proteína-Arginina N-Metiltransferases/metabolismo
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 2); 63CV1GEK3Y (N,N-dimethylarginine); 94ZLA3W45F (Arginine); EC 2.1.1.319 (PRMT1 protein, rat); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases); EC 3.5.- (Amidohydrolases); EC 3.5.3.18 (dimethylargininase)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140923
[St] Status:MEDLINE
[do] DOI:10.1155/2014/627434


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[PMID]:24834798
[Au] Autor:Awad WA; Aschenbach JR; Ghareeb K; Khayal B; Hess C; Hess M
[Ad] Endereço:Clinic for Poultry and Fish Medicine, Department for Farm Animals and Veterinary Public Health, University of Veterinary Medicine, A-1210 Vienna, Austria; Department of Animal Hygiene, Poultry and Environment and Department of Animal Behaviour and Management, Faculty of Veterinary Medicine, South Va
[Ti] Título:Campylobacter jejuni influences the expression of nutrient transporter genes in the intestine of chickens.
[So] Source:Vet Microbiol;172(1-2):195-201, 2014 Aug 06.
[Is] ISSN:1873-2542
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The gastrointestinal tract represents the first barrier against pathogens. However, the interaction of Campylobacter with intestinal epithelial cells and its effects on the intestinal function of chickens are poorly studied. Therefore, the goal of the present study was to characterize the effects of C. jejuni oral infection on the mRNA expression of nutrient transporters in the intestine. Newly hatched specific pathogen-free (SPF) chickens were orally infected with C. jejuni (NCTC 12744; 1 × 10(8)CFU/bird) at 14 days of age. Quantitative RT-PCR analyses at 14 days-post infection (dpi) revealed that the relative gene expression of the sodium/glucose cotransporter (SGLT-1) and the peptide transporter (PepT-1) was down-regulated (P<0.05) in all investigated segments (duodenum, jejunum and cecum) of Campylobacter-infected birds, while the facilitated glucose transporter (GLUT-2) was down-regulated (P<0.05) in jejunal and cecal tissues only. Furthermore, down-regulation (P<0.05) of the cationic amino acid transporter (CAT-2) and the excitatory amino acid transporter (EAAT-3) was seen in the jejunum, and down-regulation (P<0.05) of the l-type amino acid transporter (y(+)LAT-2) was noticed in the duodenum of infected birds. The decreased expression of intestinal nutrient transporters coincided with a decrease (P<0.05) in body weight and body weight gain during a 2-week post infection period. For the first time, it can be concluded that nutrient transporter expression is compromised in the small and large intestine of Campylobacter-infected birds with negative consequences on growth performance. Furthermore, the down-regulation of mRNA expression of glucose and amino acid transporters may result in accumulation of nutrients in the intestinal lumen, which may favor C. jejuni replication and colonization.
[Mh] Termos MeSH primário: Infecções por Campylobacter/veterinária
Campylobacter jejuni/fisiologia
Galinhas/microbiologia
Regulação da Expressão Gênica
Doenças das Aves Domésticas/microbiologia
[Mh] Termos MeSH secundário: Animais
Peso Corporal
Infecções por Campylobacter/genética
Infecções por Campylobacter/metabolismo
Infecções por Campylobacter/microbiologia
Transportador 2 de Aminoácidos Catiônicos/genética
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Ceco/metabolismo
Ceco/microbiologia
Duodeno/metabolismo
Duodeno/microbiologia
Transportador 3 de Aminoácido Excitatório/genética
Transportador 3 de Aminoácido Excitatório/metabolismo
Transportador de Glucose Tipo 2/genética
Transportador de Glucose Tipo 2/metabolismo
Interações Hospedeiro-Patógeno
Jejuno/metabolismo
Jejuno/microbiologia
Transportador 1 de Peptídeos
Doenças das Aves Domésticas/genética
Doenças das Aves Domésticas/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transportador 1 de Glucose-Sódio/genética
Transportador 1 de Glucose-Sódio/metabolismo
Organismos Livres de Patógenos Específicos
Simportadores/genética
Simportadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 2); 0 (Excitatory Amino Acid Transporter 3); 0 (Glucose Transporter Type 2); 0 (Peptide Transporter 1); 0 (RNA, Messenger); 0 (Sodium-Glucose Transporter 1); 0 (Symporters)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140520
[St] Status:MEDLINE


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[PMID]:24421349
[Au] Autor:Jiang Z; Yang J; Purpura LA; Liu Y; Ripps H; Shen W
[Ad] Endereço:Department of Biomedical Science, Charles E Schmidt College of Medicine, Florida Atlantic University, Boca Raton, FL 33431, USA. wshen@fau.edu.
[Ti] Título:Glycinergic feedback enhances synaptic gain in the distal retina.
[So] Source:J Physiol;592(7):1479-92, 2014 Apr 01.
[Is] ISSN:1469-7793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycine input originates with interplexiform cells, a group of neurons situated within the inner retina that transmit signals centrifugally to the distal retina. The effect on visual function of this novel mechanism is largely unknown. Using gramicidin-perforated patch whole cell recordings, intracellular recordings and specific antibody labelling techniques, we examined the effects of the synaptic connections between glycinergic interplexiform cells, photoreceptors and bipolar cells. To confirm that interplexiform cells make centrifugal feedback on bipolar cell dendrites, we recorded the postsynaptic glycine currents from axon-detached bipolar cells while stimulating presynaptic interplexiform cells. The results show that glycinergic interplexiform cells activate bipolar cell dendrites that express the α3 subunit of the glycine receptor, as well as a subclass of unidentified receptors on photoreceptors. By virtue of their synaptic contacts, glycine centrifugal feedback increases glutamate release from photoreceptors and suppresses the uptake of glutamate by the type 2A excitatory amino acid transporter on photoreceptors. The net effect is a significant increase in synaptic gain between photoreceptors and their second-order neurons.
[Mh] Termos MeSH primário: Comunicação Celular
Glicina/metabolismo
Células Bipolares da Retina/metabolismo
Segmento Interno das Células Fotorreceptoras da Retina/metabolismo
Transmissão Sináptica
[Mh] Termos MeSH secundário: Ambystoma
Animais
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Potenciais Pós-Sinápticos Excitadores
Retroalimentação Fisiológica
Ácido Glutâmico/metabolismo
Luz
Estimulação Luminosa
Receptores da Glicina/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 2); 0 (Receptors, Glycine); 0 (glycine receptor alpha3 subunit); 3KX376GY7L (Glutamic Acid); TE7660XO1C (Glycine)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140115
[St] Status:MEDLINE
[do] DOI:10.1113/jphysiol.2013.265785


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[PMID]:23950140
[Au] Autor:Leiva A; de Medina CD; Salsoso R; Sáez T; San Martín S; Abarzúa F; Farías M; Guzmán-Gutiérrez E; Pardo F; Sobrevia L
[Ad] Endereço:From the Cellular and Molecular Physiology Laboratory, Division of Obstetrics and Gynaecology, School of Medicine, Faculty of Medicine, Pontificia Universidad Católica de Chile, Santiago, Chile (A.L., C.D.d.M., R.S., T.S., F.A., M.F., E.G.-G., F.P., L.S.); Biomedical Research Centre, Department of Biomedical Sciences, School of Medicine, Universidad de Valparaíso, Valparaíso, Chile (S.S.M.); Obstetrics and Gynecology Unit, Clínica Alemana, Temuco, Chile (F.A.); and the University of Queensland Centre for Clinical Research, Faculty of Health Sciences, The University of Queensland, Herston, Queensland, Australia (L.S.).
[Ti] Título:Maternal hypercholesterolemia in pregnancy associates with umbilical vein endothelial dysfunction: role of endothelial nitric oxide synthase and arginase II.
[So] Source:Arterioscler Thromb Vasc Biol;33(10):2444-53, 2013 Oct.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Human pregnancy that courses with maternal supraphysiological hypercholesterolemia (MSPH) correlates with atherosclerotic lesions in fetal arteries. It is known that hypercholesterolemia associates with endothelial dysfunction in adults, a phenomenon where nitric oxide (NO) and arginase are involved. However, nothing is reported on potential alterations in the fetoplacental endothelial function in MSPH. The aim of this study was to determine whether MSPH alters fetal vascular reactivity via endothelial arginase/urea and L-arginine transport/NO signaling pathways. APPROACH AND RESULTS: Total cholesterol <280 mg/dL was considered as maternal physiological hypercholesterolemia (n=46 women) and ≥ 280 mg/dL as MSPH (n=28 women). Maternal but not fetal total cholesterol and low-density lipoprotein-cholesterol levels were elevated in MSPH. Umbilical veins were used for vascular reactivity assays (wire myography), and primary cultures of umbilical vein endothelial cells to determine arginase, endothelial NO synthase (eNOS), and human cationic amino acid transporter 1 and human cationic amino acid transporter 2A/B expression and activity. MSPH reduced calcitonine gene-related peptide-umbilical vein relaxation and increased intima/media ratio (histochemistry), as well as reduced eNOS activity (L-citrulline synthesis from L-arginine, eNOS phosphorylation/dephosphorylation), but increased arginase activity and arginase II protein abundance. Arginase inhibition increased eNOS activity and L-arginine transport capacity without altering human cationic amino acid transporter 1 or human cationic amino acid transporter 2A/B protein abundance in maternal physiological hypercholesterolemia and MSPH. CONCLUSIONS: MSPH is a pathophysiological condition altering umbilical vein reactivity because of fetal endothelial dysfunction associated with arginase and eNOS signaling imbalance. We speculate that elevated maternal circulating cholesterol is a factor leading to fetal endothelial dysfunction, which could have serious consequences to the growing fetus.
[Mh] Termos MeSH primário: Arginase/metabolismo
Células Endoteliais da Veia Umbilical Humana/enzimologia
Hipercolesterolemia/enzimologia
Óxido Nítrico Sintase Tipo III/metabolismo
Complicações na Gravidez/enzimologia
Veias Umbilicais/enzimologia
[Mh] Termos MeSH secundário: Adulto
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Transportador 2 de Aminoácidos Catiônicos/metabolismo
Células Cultivadas
Feminino
Células Endoteliais da Veia Umbilical Humana/patologia
Seres Humanos
Hipercolesterolemia/sangue
Hipercolesterolemia/patologia
Hipercolesterolemia/fisiopatologia
Cinética
Lipídeos/sangue
Óxido Nítrico/metabolismo
Gravidez
Complicações na Gravidez/sangue
Complicações na Gravidez/patologia
Complicações na Gravidez/fisiopatologia
Trimestres da Gravidez/metabolismo
Transdução de Sinais
Veias Umbilicais/patologia
Veias Umbilicais/fisiopatologia
Ureia/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 0 (Cationic Amino Acid Transporter 2); 0 (Lipids); 31C4KY9ESH (Nitric Oxide); 8W8T17847W (Urea); EC 1.14.13.39 (NOS3 protein, human); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 3.5.3.1 (Arginase); EC 3.5.3.1 (arginase II, human)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:130912
[Lr] Data última revisão:
130912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130817
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.113.301987



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