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Pesquisa : D12.776.157.530.200.374.600.200 [Categoria DeCS]
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[PMID]:28334039
[Au] Autor:Meng Q; Cooney M; Yepuri N; Cooney RN
[Ad] Endereço:Department of Surgery, SUNY Upstate Medical University, Syracuse, New York, United States of America.
[Ti] Título:L-arginine attenuates Interleukin-1ß (IL-1ß) induced Nuclear Factor Kappa-Beta (NF-κB) activation in Caco-2 cells.
[So] Source:PLoS One;12(3):e0174441, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Specific nutrients like L-arginine (L-Arg) ameliorate intestinal inflammation, however the exact mechanisms of this effect are unclear. We hypothesized the anti-inflammatory effects of L-Arg require active transport and metabolism by inducible nitric oxide synthase (iNOS) to generate nitric oxide (NO). To test this hypothesis we examined the effects of L-Arg, L-Arg transport activity, NO production and iNOS inhibitor on IL-1ß-mediated NF-κB-activation in Caco-2 cells. METHODS: Caco-2 cells were cultured, transfected with a NF-κB promoter luciferase vector, incubated ± L-Arg, ± IL-1ß and luciferase activity was measured. Using siRNA we inhibited the L-Arg cationic amino acid transporter system y+ (CAT1) expression and examined its effects on L-Arg transport activity and IL-1ß-mediated NF-κB-activation. Finally, the effects of sodium nitroprusside (SNP, a NO donor) and Nω-nitro-L-arginine (NNA, an iNOS inhibitor) on IL-1ß-mediated NF-κB-activation were examined. RESULTS: IL-1ß increased NF-κB luciferase activity (8-fold) and NF-κB expression (mRNA and protein), both of these were significantly decreased by L-Arg. System y+ CAT1 siRNA decreased CAT1 expression, L-Arg transport activity and attenuated the inhibitory effects of L-Arg on NF- κB activity. SNP attenuated the IL-1ß-induced increase in NF-κB luciferase activity and expression, whereas NNA diminished the inhibitory effects of L-Arg on IL-1ß-inducible NF- κB luciferase activity. CONCLUSION: The inhibitory effects of L-Arg on IL-1ß-mediated NF-κB-activation in Caco-2 cells involve L-Arg transport activity by CAT1, regulation of IL-1ß-mediated increases in NF-κB expression, changes in iNOS expression and NO production. Our data suggest the inhibitory effects of L-Arg on NF-κB activation are mediated in part by iNOS since SNP preserves and NNA attenuates the effects of L-Arg on IL-1ß-mediated NF-κB-activation and expression.
[Mh] Termos MeSH primário: Arginina/farmacologia
Interleucina-1beta/farmacologia
NF-kappa B/metabolismo
[Mh] Termos MeSH secundário: Células CACO-2
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Inibidores Enzimáticos/farmacologia
Seres Humanos
Interleucina-6/metabolismo
Óxido Nítrico/metabolismo
Óxido Nítrico Sintase Tipo II/antagonistas & inibidores
RNA Interferente Pequeno
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 0 (Enzyme Inhibitors); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (NF-kappa B); 0 (RNA, Small Interfering); 31C4KY9ESH (Nitric Oxide); 94ZLA3W45F (Arginine); EC 1.14.13.39 (Nitric Oxide Synthase Type II)
[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:170324
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174441


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[PMID]:28089735
[Au] Autor:Tun T; Kang YS
[Ad] Endereço:College of Pharmacy and Research Center for Cell Fate Control, Sookmyung Women's University, Chungpa-dong 2-ga, Yongsan-gu, Seoul 140-742, Republic of Korea.
[Ti] Título:Effects of simvastatin on CAT-1-mediated arginine transport and NO level under high glucose conditions in conditionally immortalized rat inner blood-retinal barrier cell lines (TR-iBRB).
[So] Source:Microvasc Res;111:60-66, 2017 May.
[Is] ISSN:1095-9319
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Hyperglycemia causes the breakdown of the blood-retinal barrier by impairing endothelial nitric oxide synthase (eNOS) function. Statins have many pleiotropic effects such as improving endothelial barrier permeability and increasing eNOS mRNA stability. The objective of this study was to determine effect of simvastatin on l-arginine transport and NO production under high-glucose conditions in conditionally immortalized rat retinal capillary endothelial cell line (TR-iBRB). METHODS: Changes in l-arginine transport uptake and, expression levels of cationic amino acid transporter 1 (CAT-1) and eNOS mRNA were investigated after pre-treatment with simvastatin and NOS inhibitors (l-NMMA and l-NAME) under high-glucose conditions using TR-iBRB, an in vitro model of iBRB. The NO level released from TR-iBRB cells was examined using Griess reagents. RESULTS: Under high glucose conditions, [ H]l-arginine uptake was decreased in TR-iBRB cells. Simvastatin pretreatment elevated [ H]l-arginine uptake, the expression levels of CAT-1 and eNOS mRNA, and NO production under high-glucose conditions. Moreover, the co-treatment with simvastatin and NOS inhibitors reduced [ H]l-arginine uptake compared to pretreatment with simvastatin alone. CONCLUSION: Our results suggest that, in the presence of high-glucose levels, increased l-arginine uptake due to simvastatin treatment was associated with increased CAT-1 and eNOS mRNA levels, leading to higher NO production in TR-iBRB cells. Thus, simvastatin might be a good modulator for diabetic retinopathy therapy by increasing of the l-arginine uptake and improving endothelial function in retinal capillary endothelial cells.
[Mh] Termos MeSH primário: Arginina/metabolismo
Barreira Hematorretiniana/efeitos dos fármacos
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Glucose/toxicidade
Óxido Nítrico/metabolismo
Sinvastatina/farmacologia
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Barreira Hematorretiniana/metabolismo
Transportador 1 de Aminoácidos Catiônicos/genética
Linhagem Celular
Retinopatia Diabética/tratamento farmacológico
Retinopatia Diabética/metabolismo
Óxido Nítrico Sintase Tipo III/genética
Óxido Nítrico Sintase Tipo III/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ratos
Fatores de Tempo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 0 (RNA, Messenger); 31C4KY9ESH (Nitric Oxide); 94ZLA3W45F (Arginine); AGG2FN16EV (Simvastatin); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 1.14.13.39 (Nos3 protein, rat); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE


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[PMID]:27431938
[Au] Autor:Watson CP; Pazarentzos E; Fidanboylu M; Padilla B; Brown R; Thomas SA
[Ad] Endereço:King's College London, Institute of Pharmaceutical Science, Waterloo, London, UK.
[Ti] Título:The transporter and permeability interactions of asymmetric dimethylarginine (ADMA) and L-arginine with the human blood-brain barrier in vitro.
[So] Source:Brain Res;1648(Pt A):232-242, 2016 Oct 01.
[Is] ISSN:1872-6240
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The blood-brain barrier (BBB) is a biological firewall that carefully regulates the cerebral microenvironment by acting as a physical, metabolic and transport barrier. This selectively permeable interface was modelled using the immortalised human cerebral microvascular endothelial cell line (hCMEC/D3) to investigate interactions with the cationic amino acid (CAA) L-arginine, the precursor for nitric oxide (NO), and with asymmetric dimethylarginine (ADMA), an endogenously derived analogue of L-arginine that potently inhibits NO production. The transport mechanisms utilised by L-arginine are known but they are not fully understood for ADMA, particularly at the BBB. This is of clinical significance giving the emerging role of ADMA in many brain and cerebrovascular diseases and its potential as a therapeutic target. We discovered that high concentrations of ADMA could induce endothelial dysfunction in the hCMEC/D3s BBB permeability model, leading to an increase in paracellular permeability to the paracellular marker FITC-dextran (40kDa). We also investigated interactions of ADMA with a variety of transport mechanisms, comparing the data with L-arginine interactions. Both molecules are able to utilise the CAA transport system y(+). Furthermore, the expression of CAT-1, the best known protein from this group, was confirmed in the hCMEC/D3s. It is likely that influx systems, such as y(+)L and b(0,+), have an important physiological role in ADMA transport at the BBB. These data are not only important with regards to the brain, but apply to other microvascular endothelia where ADMA is a major area of investigation.
[Mh] Termos MeSH primário: Arginina/análogos & derivados
Arginina/metabolismo
Barreira Hematoencefálica/metabolismo
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Óxido Nítrico/metabolismo
[Mh] Termos MeSH secundário: Arginina/farmacologia
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Seres Humanos
Técnicas In Vitro
Interferon gama/farmacologia
Ornitina/análogos & derivados
Ornitina/farmacologia
Permeabilidade
Espécies Reativas de Oxigênio/metabolismo
Sacarose/metabolismo
Fator de Necrose Tumoral alfa/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 0 (Enzyme Inhibitors); 0 (Reactive Oxygen Species); 0 (SLC7A1 protein, human); 0 (Tumor Necrosis Factor-alpha); 31C4KY9ESH (Nitric Oxide); 36889-13-1 (N(G)-iminoethylornithine); 57-50-1 (Sucrose); 63CV1GEK3Y (N,N-dimethylarginine); 82115-62-6 (Interferon-gamma); 94ZLA3W45F (Arginine); E524N2IXA3 (Ornithine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171008
[Lr] Data última revisão:
171008
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160720
[St] Status:MEDLINE


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[PMID]:27426075
[Au] Autor:Bentur OS; Chernichovski T; Ingbir M; Weinstein T; Schwartz IF
[Ad] Endereço:Department of Nephrology, Tel Aviv Sourasky Medical Center, Tel Aviv University, Sackler School of Medicine, Tel Aviv, Israel.
[Ti] Título:Dimethyl sulfoxide attenuates nitric oxide generation via modulation of cationic amino acid transporter-1 in human umbilical vein endothelial cells.
[So] Source:Cryobiology;73(2):226-31, 2016 Oct.
[Is] ISSN:1090-2392
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Dimethyl sulfoxide (DMSO) is a solvent that is commonly used in medicine. Conflicting data exist as to its effects on endothelial function. Endothelial cell dysfunction (ECD) is characterized by decreased endothelial nitric oxide synthase (eNOS) activity. Cationic amino acid transporter-1 (CAT-1), the specific arginine transporter for eNOS, has been shown to modulate eNOS activity. We hypothesize that DMSO inhibits eNOS activity through modulation of its selective arginine supplier CAT-1. We studied the effect of DMSO on arginine transport, NO2/NO3 generation as an index of NO production, as well as CAT-1 and Protein Kinase C alpha (PKC-α) (CAT-1 inhibitor) protein expression in human umbilical vein endothelial cell cultures (HUVECs). DMSO 2.5% and 3.5% (v/v) significantly attenuated arginine transport, a phenomenon which was prevented by co-incubation with l-arginine (1 mM). The aforementioned findings were accompanied by a decrease in NO2/NO3 generation. DMSO significantly increased the abundance of phosphorylated CAT-1 (the inactive form) and phosphorylated PKC-α protein, an effect that was attenuated by l-arginine. GO 6976 (PKC-α antagonist) prevented the decrease in arginine transport caused by DMSO. DMSO also induced profound transient morphological changes in HUVECs' structure but these were not related to its effect on arginine transport. In conclusion, DMSO inhibits NO generation by endothelial cells through modulation of CAT-1 activity.
[Mh] Termos MeSH primário: Dimetil Sulfóxido/farmacologia
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Óxido Nítrico/biossíntese
[Mh] Termos MeSH secundário: Transportador 1 de Aminoácidos Catiônicos/efeitos dos fármacos
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Células Cultivadas
Seres Humanos
Óxido Nítrico Sintase Tipo III/efeitos dos fármacos
Óxido Nítrico Sintase Tipo III/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 31C4KY9ESH (Nitric Oxide); EC 1.14.13.39 (Nitric Oxide Synthase Type III); YOW8V9698H (Dimethyl Sulfoxide)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160719
[St] Status:MEDLINE


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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]:27264891
[Au] Autor:Cervantes M; Cota M; Arce N; Castillo G; Avelar E; Espinoza S; Morales A
[Ad] Endereço:Instituto de Ciencias Agrícolas, Universidad Autónoma de Baja California, Álvaro Obregón S/N, Colonia Nueva, CP 21100 Mexicali, BC, México.
[Ti] Título:Effect of heat stress on performance and expression of selected amino acid and glucose transporters, HSP90, leptin and ghrelin in growing pigs.
[So] Source:J Therm Biol;59:69-76, 2016 Jul.
[Is] ISSN:0306-4565
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Exposing animals to high ambient temperature provokes heat stress (HS) that may affect cellular function and reduced productive performance. The effect of chronic exposure (21d) of pigs to high ambient temperature on expression of amino acid (b(0,+)AT, CAT1) and glucose (SGLT1, GLUT4) transporters, ghrelin, leptin and HSP90 was evaluated. Eighteen pigs (32.6kg body weight) were distributed into 3 groups: (1) pigs housed under natural high ambient temperature conditions, and fed ad libitum (HS); (2) pigs housed in an air-conditioned room at 24°C (thermo-neutral) fed ad libitum (TNad); (3) pigs housed as in (2), but pair-fed with the HS pigs (TNpf). Body temperature, respiratory frequency, weight gain, feed intake, and feed conversion ratio were measured. At d-21 pigs were euthanized and samples from stomach, duodenum, jejunum, liver, longissimus and semitendinosus muscles, and white adipose tissue were collected for mRNA analysis. In the HS room ambient temperature fluctuated every day (23.6-37.6°C). Respiratory frequency and body temperature were higher in HS pigs (P<0.001). Weight gain and feed intake of TNad were higher (P<0.001) than TNpf and HS; gain: feed ratio was not affected by ambient temperature. Expression of HSP90 was higher in duodenum and longissimus (P≤0.038) of HS compared to TNpf. Expression of ghrelin, leptin and b(0,+)AT were not affected by ambient temperature (P>0.050). CAT1 expression in liver was higher (P=0.050) but in longissimus was lower (P=0.017) in HS than in TNpf pigs. Expression of SGLT1 was higher (P=0.045) in duodenum of HS than in TNpf but it was not different in jejunum (P=0.545); GLUT4 tended to be higher in liver and semitendinosus of HS pigs (P=0.063). In conclusion, feed intake remains low whereas respiratory frequency and body temperature remain higher; and expression of HSP90, CAT1, SGLT1 and GLUT4 increases in some tissues in pigs under chronic HS conditions.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/genética
Grelina/genética
Transportador de Glucose Tipo 4/genética
Proteínas de Choque Térmico HSP90/genética
Leptina/genética
Transportador 1 de Glucose-Sódio/genética
Suínos/fisiologia
[Mh] Termos MeSH secundário: Aclimatação
Animais
Temperatura Corporal
Transportador 1 de Aminoácidos Catiônicos/genética
Regulação da Expressão Gênica
Resposta ao Choque Térmico
Temperatura Alta
Umidade
Respiração
Suínos/genética
Suínos/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Cationic Amino Acid Transporter 1); 0 (Ghrelin); 0 (Glucose Transporter Type 4); 0 (HSP90 Heat-Shock Proteins); 0 (Leptin); 0 (Sodium-Glucose Transporter 1)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170314
[Lr] Data última revisão:
170314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160607
[St] Status:MEDLINE


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[PMID]:26710791
[Au] Autor:Guzmán-Gutiérrez E; Armella A; Toledo F; Pardo F; Leiva A; Sobrevia L
[Ad] Endereço:Cellular and Molecular Physiology Laboratory (CMPL), Division of Obstetrics and Gynaecology, School of Medicine, Faculty of Medicine, Pontificia Universidad Católica de Chile, P.O. Box 114-D, Santiago, 8330024, Chile.
[Ti] Título:Insulin requires A1 adenosine receptors expression to reverse gestational diabetes-increased L-arginine transport in human umbilical vein endothelium.
[So] Source:Purinergic Signal;12(1):175-90, 2016 Mar.
[Is] ISSN:1573-9546
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Gestational diabetes mellitus (GDM) associates with increased L-arginine transport and extracellular concentration of adenosine in human umbilical vein endothelial cells (HUVECs). In this study we aim to determine whether insulin reverses GDM-increased L-arginine transport requiring adenosine receptors expression in HUVECs. Primary cultured HUVECs from full-term normal (n = 38) and diet-treated GDM (n = 38) pregnancies were used. Insulin effect was assayed on human cationic amino acid transporter 1 (hCAT1) expression (protein, mRNA, SLC7A1 promoter activity) and activity (initial rates of L-arginine transport) in the absence or presence of adenosine receptors agonists or antagonists. A1 adenosine receptors (A1AR) and A2AAR expression (Western blot, quantitative PCR) was determined. Experiments were done in cells expressing or siRNA-suppressed expression of A1AR or A2AAR. HUVECs from GDM exhibit higher maximal transport capacity (maximal velocity (V max)/apparent Michaelis Menten constant (K m), V max/K m), which is blocked by insulin by reducing the V max to values in cells from normal pregnancies. Insulin also reversed the GDM-associated increase in hCAT-1 protein abundance and mRNA expression, and SLC7A1 promoter activity for the fragment -606 bp from the transcription start point. Insulin effects required A1AR, but not A2AAR expression and activity in this cell type. In the absence of insulin, GDM-increased hCAT-1 expression and activity required A2AAR expression and activity. HUVECs from GDM pregnancies exhibit a differential requirement of A1AR or A2AAR depending on the level of insulin, a phenomenon that represent a condition where adenosine or analogues of this nucleoside could be acting as helpers of insulin biological effects in GDM.
[Mh] Termos MeSH primário: Arginina/metabolismo
Diabetes Gestacional/tratamento farmacológico
Diabetes Gestacional/metabolismo
Endotélio Vascular/metabolismo
Hipoglicemiantes/farmacologia
Insulina/farmacologia
Receptor A1 de Adenosina/metabolismo
Veias Umbilicais/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Transportador 1 de Aminoácidos Catiônicos/biossíntese
Transportador 1 de Aminoácidos Catiônicos/genética
Diabetes Gestacional/dietoterapia
Endotélio Vascular/efeitos dos fármacos
Transportador Equilibrativo 1 de Nucleosídeo/metabolismo
Feminino
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/metabolismo
Seres Humanos
Recém-Nascido
Masculino
Gravidez
Cultura Primária de Células
Receptor A1 de Adenosina/efeitos dos fármacos
Veias Umbilicais/efeitos dos fármacos
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 (Equilibrative Nucleoside Transporter 1); 0 (Hypoglycemic Agents); 0 (Insulin); 0 (Receptor, Adenosine A1); 0 (SLC7A1 protein, human); 94ZLA3W45F (Arginine)
[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:151230
[St] Status:MEDLINE
[do] DOI:10.1007/s11302-015-9491-2


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[PMID]:26555760
[Au] Autor:Vanoaica L; Behera A; Camargo SM; Forster IC; Verrey F
[Ad] Endereço:Institute of Physiology, Zurich Center for Integrative Human Physiology (ZIHP) and NCCR Kidney.CH, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
[Ti] Título:Real-time functional characterization of cationic amino acid transporters using a new FRET sensor.
[So] Source:Pflugers Arch;468(4):563-72, 2016 Apr.
[Is] ISSN:1432-2013
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:L-arginine is a semi-essential amino acid that serves as precursor for the production of urea, nitric oxide (NO), polyamines, and other biologically important metabolites. Hence, a fast and reliable assessment of its intracellular concentration changes is highly desirable. Here, we report on a genetically encoded Förster resonance energy transfer (FRET)-based arginine nanosensor that employs the arginine repressor/activator ahrC gene from Bacillus subtilis. This new nanosensor was expressed in HEK293T cells, and experiments with cell lysate showed that it binds L-arginine with high specificity and with a K d of ∼177 µM. Live imaging experiments showed that the nanosensor was expressed throughout the cytoplasm and displayed a half maximal FRET increase at an extracellular L-arginine concentration of ∼22 µM. By expressing the nanosensor together with SLC7A1, SLC7A2B, or SLC7A3 cationic amino acid transporters (CAT1-3), it was shown that L-arginine was imported at a similar rate via SLC7A1 and SLC7A2B and slower via SLC7A3. In contrast, upon withdrawal of extracellular L-arginine, intracellular levels decreased as fast in SLC7A3-expressing cells compared with SLC7A1, but the efflux was slower via SLC7A2B. SLC7A4 (CAT4) could not be convincingly shown to transport L-arginine. We also demonstrated the impact of membrane potential on L-arginine transport and showed that physiological concentrations of symmetrical and asymmetrical dimethylarginine do not significantly interfere with L-arginine transport through SLC7A1. Our results demonstrate that the FRET nanosensor can be used to assess L-arginine transport through plasma membrane in real time.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Técnicas Biossensoriais/métodos
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Transferência Ressonante de Energia de Fluorescência/métodos
Proteínas Repressoras/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Arginina/metabolismo
Proteínas de Bactérias/química
Células HEK293
Seres Humanos
Potenciais da Membrana
Proteínas Repressoras/química
Transativadores/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AhrC protein, Bacillus subtilis); 0 (Bacterial Proteins); 0 (Cationic Amino Acid Transporter 1); 0 (Repressor Proteins); 0 (Trans-Activators); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151112
[St] Status:MEDLINE
[do] DOI:10.1007/s00424-015-1754-9


  9 / 173 MEDLINE  
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[PMID]:26449889
[Au] Autor:Werner A; Amann E; Schnitzius V; Habermeier A; Luckner-Minden C; Leuchtner N; Rupp J; Closs EI; Munder M
[Ad] Endereço:Department of Pharmacology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz, Germany.
[Ti] Título:Induced arginine transport via cationic amino acid transporter-1 is necessary for human T-cell proliferation.
[So] Source:Eur J Immunol;46(1):92-103, 2016 Jan.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Availability of the semiessential amino acid arginine is fundamental for the efficient function of human T lymphocytes. Tumor-associated arginine deprivation, mainly induced by myeloid-derived suppressor cells, is a central mechanism of tumor immune escape from T-cell-mediated antitumor immune responses. We thus assumed that transmembranous transport of arginine must be crucial for T-cell function and studied which transporters are responsible for arginine influx into primary human T lymphocytes. Here, we show that activation via CD3 and CD28 induces arginine transport into primary human T cells. Both naïve and memory CD4(+) T cells as well as CD8(+) T cells specifically upregulated the human cationic amino acid transporter-1 (hCAT-1), with an enhanced and persistent expression under arginine starvation. When hCAT-1 induction was suppressed via siRNA transfection, arginine uptake, and cellular proliferation were impaired. In summary, our results demonstrate that hCAT-1 is a key component of efficient T-cell activation and a novel potential target structure to modulate adaptive immune responses in tumor immunity or inflammation.
[Mh] Termos MeSH primário: Arginina/metabolismo
Transportador 1 de Aminoácidos Catiônicos/imunologia
Ativação Linfocitária/imunologia
Linfócitos T/imunologia
[Mh] Termos MeSH secundário: Western Blotting
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Proliferação Celular
Células Cultivadas
Seres Humanos
RNA Interferente Pequeno
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Linfócitos T/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 0 (RNA, Small Interfering); 0 (SLC7A1 protein, human); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:160111
[Lr] Data última revisão:
160111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151010
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201546047


  10 / 173 MEDLINE  
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[PMID]:26446563
[Au] Autor:Tudela RC; Loiola RA; Torres TC; Gil NL; Assunção NA; de Noronha SM; Correa-Noronh SA; Landgraf RG; Fernandes L
[Ti] Título:L-Arginine Transport and Nitric Oxide Production in Kinin Receptor B1-/- Endothelial Cells.
[So] Source:Protein Pept Lett;22(12):1111-6, 2015.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Kinins are important vasoactive peptides, but the role of the B1 receptor subtype in the vascular control is poorly understood. This study analyzed the nitric oxide (NO) release, L-arginine (L-Arg) uptake and the expression of the cationic amino acid transporter (CAT) -1 in endothelial cells obtained from B1 receptor knockout (B1-/-) and wild type (WT) mice. NO production was assessed through a fluorescent dye in living cells stimulated with acetylcholine. L-Arg uptake was determined indirectly in the culture medium by HPLC, in the presence or absence of the CAT-1 blocker N-ethylmaleimide (NEM). CAT-1 mRNA levels and protein expression were determined by qPCR and western blot, respectively. NO release was significantly reduced in B1-/- when compared to WT cells. This result was accompanied by a decreased rate in the L-Arg uptake by B1-/- cells. Incubation with NEM impaired the L-Arg uptake in WT, but had no effect in B1-/- cells. Protein expression and mRNA levels for CAT-1 were reduced in B1-/- in comparison to WT cells. These findings suggest an important role of the endothelial B1 receptor in the vascular control by interfering with CAT-1 expression, L-Arg uptake and NO release.
[Mh] Termos MeSH primário: Arginina/metabolismo
Células Endoteliais/metabolismo
Óxido Nítrico/metabolismo
Receptor B1 da Bradicinina/genética
Receptor B1 da Bradicinina/metabolismo
[Mh] Termos MeSH secundário: Animais
Transportador 1 de Aminoácidos Catiônicos/genética
Transportador 1 de Aminoácidos Catiônicos/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cationic Amino Acid Transporter 1); 0 (Receptor, Bradykinin B1); 31C4KY9ESH (Nitric Oxide); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151105
[Lr] Data última revisão:
151105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151009
[St] Status:MEDLINE



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