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Pesquisa : D12.776.157.530.200.500.100 [Categoria DeCS]
Referências encontradas : 233 [refinar]
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[PMID]:28272791
[Au] Autor:Todd AC; Marx MC; Hulme SR; Bröer S; Billups B
[Ad] Endereço:Eccles Institute of Neuroscience, The John Curtin School of Medical Research, The Australian National University, 131 Garran Road, Canberra, ACT 2601, Australia.
[Ti] Título:SNAT3-mediated glutamine transport in perisynaptic astrocytes in situ is regulated by intracellular sodium.
[So] Source:Glia;65(6):900-916, 2017 Jun.
[Is] ISSN:1098-1136
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The release of glutamine from astrocytes adjacent to synapses in the central nervous system is thought to play a vital role in the mechanism of glutamate recycling and is therefore important for maintaining excitatory neurotransmission. Here we investigate the nature of astrocytic membrane transport of glutamine in rat brainstem slices, using electrophysiological recording and fluorescent imaging of pH and Nai+. Glutamine application to perisynaptic astrocytes induced a membrane current, caused by activation of system A (SA) family transporters. A significant electroneutral component was also observed, which was mediated by the system N (SN) family transporters. This response was stimulated by glutamine (K of 1.57 mM), histidine, and asparagine, but not by leucine or serine, indicating activation of the SNAT3 isoform of SN. We hypothesized that increasing the [Na ] would alter the SNAT3 transporter equilibrium, thereby stimulating glutamine release. In support of this hypothesis, we show that SNAT3 transport can be driven by changing cation concentration and that manipulations to raise [Na ] (activation of excitatory amino acid transporters (EAATs), SA transporters or AMPA receptors) all directly influence SNAT3 transport rate. A kinetic model of glutamine fluxes is presented, which shows that EAAT activation causes the release of glutamine, driven mainly by the increased [Na ] . These data demonstrate that SNAT3 is functionally active in perisynaptic astrocytes in situ. As a result, astrocytic Nai+ signaling, as would be stimulated by neighboring synaptic activity, has the capacity to stimulate astrocytic glutamine release to support glutamate recycling.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Neutros/metabolismo
Astrócitos/metabolismo
Glutamina/metabolismo
Espaço Intracelular/metabolismo
Sódio/metabolismo
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Sistema A de Transporte de Aminoácidos/metabolismo
Animais
Astrócitos/efeitos dos fármacos
Tronco Encefálico/efeitos dos fármacos
Tronco Encefálico/metabolismo
Cátions Monovalentes/metabolismo
Feminino
Proteínas de Transporte de Glutamato da Membrana Plasmática/metabolismo
Concentração de Íons de Hidrogênio
Espaço Intracelular/efeitos dos fármacos
Cinética
Lítio/metabolismo
Masculino
Modelos Neurológicos
Ratos Wistar
Receptores de AMPA/metabolismo
Sinapses/efeitos dos fármacos
Técnicas de Cultura de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (Amino Acid Transport Systems, Neutral); 0 (Cations, Monovalent); 0 (Glutamate Plasma Membrane Transport Proteins); 0 (Receptors, AMPA); 0 (system N protein 1); 0RH81L854J (Glutamine); 9FN79X2M3F (Lithium); 9NEZ333N27 (Sodium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1002/glia.23133


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[PMID]:28224429
[Au] Autor:Zhou FF; Xie W; Chen SQ; Wang XK; Liu Q; Pan XK; Su F; Feng MH
[Ad] Endereço:Department of Oncology, Zhongnan Hospital of Wuhan University, Wuhan, 430071, China.
[Ti] Título:SLC38A1 promotes proliferation and migration of human colorectal cancer cells.
[So] Source:J Huazhong Univ Sci Technolog Med Sci;37(1):30-36, 2017 Feb.
[Is] ISSN:1672-0733
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Current studies have demonstrated that SLC38A1 proteins play a causal role in neoplastic cell transformation. The twofold aim of this study was to provide insight into whether a variance in the expression of SLC38A1 exists between human colorectal cancer and healthy human tissues and to determine how silencing or overexpressing the SLC38A1 gene could affect the proliferation, viability and migration of colorectal cancer cells. Immunohistochemical staining was used to analyze the expression of SLC38A1 in colorectal cancer tissues and adjacent normal mucosa in 77 patients who underwent surgical resection. The expression of SLC38A1 in colorectal cancer tissues and cell lines was detected using RT-PCR and Western blotting. Two colorectal cancer cell lines SW480 and HCT116 were used to examine whether silencing SLC38A1 with siRNA and overexpressing SLC38A1 with shRNA could affect cell viability and migration. As a result, the SLC38A1 protein was very low or undetectable in the normal colon mucosa. In contrast, strong staining of SLC38A1 protein was found in the cytoplasm in 79.2% colorectal cancer samples. More pronounced SLC38A1 expression in colorectal cancer tissues was significantly associated with tumor node metastasis (TNM) stage. Inhibition of SLC38A1 reduced tumour growth and suppressed proliferation and migration of SW480 cells. In contrast, overexpression of SLC38A1 had the opposite effects on HCT116 cells. SLC38A1 is overexpressed in colorectal cancer, which suggests that it is associated with tumour progression. These results encourage the exploration of SLC38A1 as a target for intervention in colorectal cancer.
[Mh] Termos MeSH primário: Sistema A de Transporte de Aminoácidos/genética
Sistema A de Transporte de Aminoácidos/metabolismo
Neoplasias Colorretais/patologia
Citoplasma/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Neoplasias Colorretais/genética
Neoplasias Colorretais/metabolismo
Citoplasma/genética
Feminino
Regulação Neoplásica da Expressão Gênica
Células HCT116
Seres Humanos
Masculino
Estadiamento de Neoplasias
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (SLC38A1 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171104
[Lr] Data última revisão:
171104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE
[do] DOI:10.1007/s11596-017-1690-3


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[PMID]:28082201
[Au] Autor:Carnicelli D; Arfilli V; Onofrillo C; Alfieri RR; Petronini PG; Montanaro L; Brigotti M
[Ad] Endereço:Dipartimento di Medicina Specialistica, Diagnostica e Sperimentale, Università di Bologna, Bologna, Italy.
[Ti] Título:Cap-independent protein synthesis is enhanced by betaine under hypertonic conditions.
[So] Source:Biochem Biophys Res Commun;483(3):936-940, 2017 Feb 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein synthesis is one of the main cellular functions inhibited during hypertonic challenge. The subsequent accumulation of the compatible osmolyte betaine during the later adaptive response allows not only recovery of translation but also its stimulation. In this paper, we show that betaine modulates translation by enhancing the formation of cap-independent 48 S pre-initiation complexes, leaving cap-dependent 48 S pre-initiation complexes basically unchanged. In the presence of betaine, CrPV IRES- and sodium-dependent neutral amino acid transporter-2 (SNAT2) 5'-UTR-driven translation is 2- and 1.5-fold stimulated in MCF7 cells, respectively. Thus, betaine could provide an advantage in translation of messengers coding for proteins implicated in the response of cells to different stressors, which are often recognized by ribosomal 40 S subunit through simplified cap-independent mechanisms.
[Mh] Termos MeSH primário: Betaína/metabolismo
Betaína/farmacologia
Biossíntese de Proteínas/efeitos dos fármacos
Capuzes de RNA/metabolismo
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Sistema A de Transporte de Aminoácidos/metabolismo
Animais
Sistema Livre de Células
Seres Humanos
Soluções Hipertônicas
Luciferases/genética
Luciferases/metabolismo
Células MCF-7
Pressão Osmótica
Polirribossomos/metabolismo
Biossíntese de Proteínas/genética
Coelhos
Reticulócitos/efeitos dos fármacos
Reticulócitos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Amino Acid Transport System A); 0 (Hypertonic Solutions); 0 (RNA Caps); 0 (SLC38A2 protein, human); 3SCV180C9W (Betaine); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE


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[PMID]:27956114
[Au] Autor:Chen YY; Powell TL; Jansson T
[Ad] Endereço:Division of Reproductive Science, Department of Obstetrics & Gynecology, University of Colorado Anschutz Medical Campus, Aurora, CO, USA; Division of High-risk Pregnancy, Department of Obstetrics & Gynecology, Mackay Memorial Hospital, Taipei, Taiwan. Electronic address: yhyy@mmh.org.tw.
[Ti] Título:1,25-Dihydroxy vitamin D stimulates system A amino acid transport in primary human trophoblast cells.
[So] Source:Mol Cell Endocrinol;442:90-97, 2017 Feb 15.
[Is] ISSN:1872-8057
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Vitamin D deficiency during pregnancy is linked to adverse perinatal outcomes such as small for gestational age infants. Recent evidence suggests that changes in placental amino acid transport contribute to altered fetal growth. We tested the hypothesis that 1,25-dihydroxy vitamin D increases the gene expression of System A and L amino acid transporter isoforms and stimulates placental amino acid transport activity in cultured primary human trophoblast cells mediated by mTOR signaling. Treatment with 1,25-dihydroxy vitamin D significantly increased mRNA expression of the System A isoform SNAT2 and System A activity, but had no effect on System L and did not affect mTOR signaling. siRNA silencing of the vitamin D receptor prevented 1,25-dihydroxy vitamin D -stimulated System A transport. In conclusion, 1,25-dihydroxy vitamin D regulates System A activity through increased mRNA expression of SNAT2 transporters. Effects on placental amino acid transport may be the mechanism underlying the association between maternal vitamin D status and fetal growth.
[Mh] Termos MeSH primário: Sistema A de Transporte de Aminoácidos/metabolismo
Aminoácidos/metabolismo
Trofoblastos/efeitos dos fármacos
Vitamina D/análogos & derivados
[Mh] Termos MeSH secundário: Células Cultivadas
Colecalciferol/metabolismo
Feminino
Desenvolvimento Fetal/efeitos dos fármacos
Idade Gestacional
Seres Humanos
Placenta/efeitos dos fármacos
Placenta/metabolismo
Gravidez
RNA Interferente Pequeno/metabolismo
Receptores de Calcitriol/metabolismo
Transdução de Sinais/efeitos dos fármacos
Serina-Treonina Quinases TOR/metabolismo
Trofoblastos/metabolismo
Vitamina D/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (Amino Acids); 0 (RNA, Small Interfering); 0 (Receptors, Calcitriol); 0 (dihydroxy-vitamin D3); 1406-16-2 (Vitamin D); 1C6V77QF41 (Cholecalciferol); EC 2.7.1.1 (TOR Serine-Threonine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE


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[PMID]:27742667
[Au] Autor:Moen MN; Fjær R; Hamdani EH; Laerdahl JK; Menchini RJ; Vigeland MD; Sheng Y; Undlien DE; Hassel B; Salih MA; El Khashab HY; Selmer KK; Chaudhry FA
[Ad] Endereço:1 The Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Oslo, Norway.
[Ti] Título:Pathogenic variants in KCTD7 perturb neuronal K+ fluxes and glutamine transport.
[So] Source:Brain;139(Pt 12):3109-3120, 2016 Dec.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Progressive myoclonus epilepsy is a heterogeneous group of disorders characterized by myoclonic and tonic-clonic seizures, ataxia and cognitive decline. We here present two affected brothers. At 9 months of age the elder brother developed ataxia and myoclonic jerks. In his second year he lost the ability to walk and talk, and he developed drug-resistant progressive myoclonus epilepsy. The cerebrospinal fluid level of glutamate was decreased while glutamine was increased. His younger brother manifested similar symptoms from 6 months of age. By exome sequencing of the proband we identified a novel homozygous frameshift variant in the potassium channel tetramerization domain 7 (KCTD7) gene (NM_153033.1:c.696delT: p.F232fs), which results in a truncated protein. The identified F232fs variant is inherited in an autosomal recessive manner, and the healthy consanguineous parents carry the variant in a heterozygous state. Bioinformatic analyses and structure modelling showed that KCTD7 is a highly conserved protein, structurally similar to KCTD5 and several voltage-gated potassium channels, and that it may form homo- or heteromultimers. By heterologous expression in Xenopus laevis oocytes, we demonstrate that wild-type KCTD7 hyperpolarizes cells in a K dependent manner and regulates activity of the neuronal glutamine transporter SAT2 (Slc38a2), while the F232fs variant impairs K fluxes and obliterates SAT2-dependent glutamine transport. Characterization of four additional disease-causing variants (R94W, R184C, N273I, Y276C) bolster these results and reveal the molecular mechanisms involved in the pathophysiology of KCTD7-related progressive myoclonus epilepsy. Thus, our data demonstrate that KCTD7 has an impact on K fluxes, neurotransmitter synthesis and neuronal function, and that malfunction of the encoded protein may lead to progressive myoclonus epilepsy.
[Mh] Termos MeSH primário: Glutamina/metabolismo
Epilepsias Mioclônicas Progressivas/genética
Neurônios/metabolismo
Canais de Potássio/genética
Potássio/metabolismo
[Mh] Termos MeSH secundário: Sistema A de Transporte de Aminoácidos/metabolismo
Animais
Transporte Biológico
Pré-Escolar
Consanguinidade
Evolução Fatal
Seres Humanos
Masculino
Oócitos
Linhagem
Arábia Saudita
Irmãos
Xenopus laevis
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (KCTD7 protein, human); 0 (Potassium Channels); 0 (Slc38a2 protein, mouse); 0RH81L854J (Glutamine); RWP5GA015D (Potassium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161016
[St] Status:MEDLINE


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[PMID]:27655909
[Au] Autor:Iyer RP; Gu S; Jiang JX
[Ad] Endereço:Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA.
[Ti] Título:N-Glycosylation influences transport, but not cellular trafficking, of a neuronal amino acid transporter SNAT1.
[So] Source:Biochem J;473(22):4227-4242, 2016 Nov 15.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SNAT1 is a system N/A neutral amino acid transporter that primarily expresses in neurons and mediates the transport of l-glutamine (Gln). Gln is an important amino acid involved in multiple cellular functions and also is a precursor for neurotransmitters, glutamate and GABA. In the present study, we demonstrated that SNAT1 is an N-glycoprotein expressed in neurons. We identified three glycosylation sites at asparagine residues 251, 257 and 310 in SNAT1 protein, and that the first two are the primary sites. The biotinylation and confocal immunofluorescence analysis showed that the glycosylation-impaired mutants and deglycosylated SNAT1 were equally capable of expressing on the cell surface. However, l-Gln and 3H-labeled methyl amino isobutyrate (MeAIB) was significantly compromised in N-glycosylation-impaired mutants and deglycosylated SNAT1 when compared with the wild-type control. Taken together, these results suggest that SNAT1 is an N-glycosylated protein with three de novo glycosylation sites and N-glycosylation of SNAT1 may play an important role in the transport of substrates across the cell membrane.
[Mh] Termos MeSH primário: Sistema A de Transporte de Aminoácidos/química
Sistema A de Transporte de Aminoácidos/metabolismo
[Mh] Termos MeSH secundário: Animais
Asparagina/química
Asparagina/metabolismo
Western Blotting
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Células CHO
Cricetulus
Imunofluorescência
Glicosilação
Microscopia Confocal
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Peptídeo-N4-(N-acetil-beta-glucosaminil) Asparagina Amidase/metabolismo
Transporte Proteico
Tunicamicina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (Slc38a1 protein, mouse); 11089-65-9 (Tunicamycin); 7006-34-0 (Asparagine); EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160923
[St] Status:MEDLINE


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[PMID]:27613819
[Au] Autor:Yang X; Tao Z; Zhu Z; Liao H; Zhao Y; Fan H
[Ad] Endereço:Department of Otorhinolaryngology - Head and Neck SurgeryRenmin Hospital of Wuhan University, Wuhan, China.
[Ti] Título:MicroRNA-593-3p regulates insulin-promoted glucose consumption by targeting Slc38a1 and CLIP3.
[So] Source:J Mol Endocrinol;57(4):211-222, 2016 Nov.
[Is] ISSN:1479-6813
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Insulin plays an important role in the regulation of glucose metabolism. However, the molecular mechanisms involved are not entirely clarified. In this context, we found that miR-593-3p negatively regulates insulin-regulated glucose metabolism in hepatocellular carcinoma HepG2 and Bel7402 cells. We then identified Slc38a1 and CLIP3 as novel targets of miR-593-3p. Further studies demonstrated that Slc38a1 and CLIP3 mediate insulin-regulated glucose metabolism. Interestingly, we also demonstrated that miR-593-3p expression was negatively associated with Slc38a1 and CLIP3 expression in insulin-treated HepG2 cells, and insulin-induced Slc38a1 and CLIP3 expression via downregulation of miR-593-3p. Taken together, this study indicates that inhibition of miRNA-593-3p by insulin promotes glucose metabolism through the regulation of Slc38a1 and CLIP3 expression, and provides a new insight into the role and mechanism of insulin-induced glycolysis.
[Mh] Termos MeSH primário: Sistema A de Transporte de Aminoácidos/genética
Regulação da Expressão Gênica
Glucose/metabolismo
Insulina/metabolismo
MicroRNAs/genética
Interferência de RNA
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Pareamento de Bases
Linhagem Celular
Proliferação Celular
Metabolismo Energético/genética
Hepatócitos
Seres Humanos
Ácido Láctico/biossíntese
Camundongos
RNA Mensageiro/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Amino Acid Transport System A); 0 (Insulin); 0 (MIRN593 microRNA, human); 0 (MicroRNAs); 0 (RNA, Messenger); 0 (SLC38A1 protein, human); 33X04XA5AT (Lactic Acid); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160911
[St] Status:MEDLINE


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Texto completo
[PMID]:27355203
[Au] Autor:Chen C; Wang J; Cai R; Yuan Y; Guo Z; Grewer C; Zhang Z
[Ad] Endereço:College of Life Science and Biopharmacy, Shenyang Pharmaceutical University, Shenyang 110015, People's Republic of China.
[Ti] Título:Identification of a Disulfide Bridge in Sodium-Coupled Neutral Amino Acid Transporter 2(SNAT2) by Chemical Modification.
[So] Source:PLoS One;11(6):e0158319, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sodium-coupled neutral amino acid transporter 2 (SNAT2) belongs to solute carrier 38 (SLC38) family of transporters, which is ubiquitously expressed in mammalian tissues and mediates transport of small, neutral amino acids, exemplified by alanine(Ala, A). Yet structural data on SNAT2, including the relevance of intrinsic cysteine residues on structure and function, is scarce, in spite of its essential roles in many tissues. To better define the potential of intrinsic cysteines to form disulfide bonds in SNAT2, mutagenesis experiments and thiol-specific chemical modifications by N-ethylmaleimide (NEM) and methoxy-polyethylene glycol maleimide (mPEG-Mal, MW 5000) were performed, with or without the reducing regent dithiothreitol (DTT) treatment. Seven single mutant transporters with various cysteine (Cys, C) to alanine (Ala, A) substitutions, and a C245,279A double mutant were introduced to SNAT2 with a hemagglutinin (HA) tag at the C-terminus. The results showed that the cells expressing C245A or C279A were labeled by one equivalent of mPEG-Mal in the presence of DTT, while wild-type or all the other single Cys to Ala mutants were modified by two equivalents of mPEG-Mal. Furthermore, the molecular weight of C245,279A was not changed in the presence or absence of DTT treatment. The results suggest a disulfide bond between Cys245 and Cys279 in SNAT2 which has no effect on cell surface trafficking, as well as transporter function. The proposed disulfide bond may be important to delineate proximity in the extracellular domain of SNAT2 and related proteins.
[Mh] Termos MeSH primário: Sistema A de Transporte de Aminoácidos/química
Sistemas de Transporte de Aminoácidos/química
Dissulfetos/química
[Mh] Termos MeSH secundário: Alanina/química
Animais
Cisteína/química
Ditiotreitol/química
Etilmaleimida/química
Células HEK293
Seres Humanos
Transporte de Íons
Mutagênese
Mutação
Polietilenoglicóis/química
Ratos
Sódio/metabolismo
Compostos de Sulfidrila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (Amino Acid Transport Systems); 0 (Disulfides); 0 (SLC38A2 protein, human); 0 (SNAT2 protein, rat); 0 (Sulfhydryl Compounds); 30IQX730WE (Polyethylene Glycols); 9NEZ333N27 (Sodium); K848JZ4886 (Cysteine); O3C74ACM9V (Ethylmaleimide); OF5P57N2ZX (Alanine); T8ID5YZU6Y (Dithiothreitol)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0158319


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[PMID]:27129276
[Au] Autor:Bröer A; Rahimi F; Bröer S
[Ad] Endereço:From the Research School of Biology, The Australian National University, Canberra, Australian Capital Territory 2601, Australia.
[Ti] Título:Deletion of Amino Acid Transporter ASCT2 (SLC1A5) Reveals an Essential Role for Transporters SNAT1 (SLC38A1) and SNAT2 (SLC38A2) to Sustain Glutaminolysis in Cancer Cells.
[So] Source:J Biol Chem;291(25):13194-205, 2016 Jun 17.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many cancer cells depend on glutamine as they use the glutaminolysis pathway to generate building blocks and energy for anabolic purposes. As a result, glutamine transporters are essential for cancer growth and are potential targets for cancer chemotherapy with ASCT2 (SLC1A5) being investigated most intensively. Here we show that HeLa epithelial cervical cancer cells and 143B osteosarcoma cells express a set of glutamine transporters including SNAT1 (SLC38A1), SNAT2 (SLC38A2), SNAT4 (SLC38A4), LAT1 (SLC7A5), and ASCT2 (SLC1A5). Net glutamine uptake did not depend on ASCT2 but required expression of SNAT1 and SNAT2. Deletion of ASCT2 did not reduce cell growth but caused an amino acid starvation response and up-regulation of SNAT1 to replace ASCT2 functionally. Silencing of GCN2 in the ASCT2(-/-) background reduced cell growth, showing that a combined targeted approach would inhibit growth of glutamine-dependent cancer cells.
[Mh] Termos MeSH primário: Sistema ASC de Transporte de Aminoácidos/genética
Sistema A de Transporte de Aminoácidos/fisiologia
[Mh] Termos MeSH secundário: Proliferação Celular
Deleção de Genes
Expressão Gênica
Glutamina/metabolismo
Células HeLa
Homeostase
Seres Humanos
Transporte de Íons
Redes e Vias Metabólicas
Antígenos de Histocompatibilidade Menor
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (Amino Acid Transport System ASC); 0 (Minor Histocompatibility Antigens); 0 (SLC1A5 protein, human); 0 (SLC38A1 protein, human); 0 (SLC38A2 protein, human); 0RH81L854J (Glutamine)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170618
[Lr] Data última revisão:
170618
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160430
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.700534


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[PMID]:26884386
[Au] Autor:Boutry C; El-Kadi SW; Suryawan A; Steinhoff-Wagner J; Stoll B; Orellana RA; Nguyen HV; Kimball SR; Fiorotto ML; Davis TA
[Ad] Endereço:United States Department of Agriculture/Agricultural Research Service Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, Texas; and.
[Ti] Título:Pulsatile delivery of a leucine supplement during long-term continuous enteral feeding enhances lean growth in term neonatal pigs.
[So] Source:Am J Physiol Endocrinol Metab;310(8):E699-E713, 2016 Apr 15.
[Is] ISSN:1522-1555
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neonatal pigs are used as a model to study and optimize the clinical treatment of infants who are unable to maintain oral feeding. Using this model, we have shown previously that pulsatile administration of leucine during continuous feeding over 24 h via orogastric tube enhanced protein synthesis in skeletal muscle compared with continuous feeding alone. To determine the long-term effects of leucine pulses, neonatal piglets (n = 11-12/group) were continuously fed formula via orogastric tube for 21 days, with an additional parenteral infusion of either leucine (CON + LEU; 800 µmol·kg ·h ) or alanine (CON + ALA) for 1 h every 4 h. The results show that body and muscle weights and lean gain were ∼25% greater, and fat gain was 48% lower in CON + LEU than CON + ALA; weights of other tissues were unaffected by treatment. Fractional protein synthesis rates in longissimus dorsi, gastrocnemius, and soleus muscles were ∼30% higher in CON + LEU compared with CON + ALA and were associated with decreased Deptor abundance and increased mTORC1, mTORC2, 4E-BP1, and S6K1 phosphorylation, SNAT2 abundance, and association of eIF4E with eIF4G and RagC with mTOR. There were no treatment effects on PKB, eIF2α, eEF2, or PRAS40 phosphorylation, Rheb, SLC38A9, v-ATPase, LAMTOR1, LAMTOR2, RagA, RagC, and LAT1 abundance, the proportion of polysomes to nonpolysomes, or the proportion of mRNAs encoding rpS4 or rpS8 associated with polysomes. Our results demonstrate that pulsatile delivery of a leucine supplement during 21 days of continuous enteral feeding enhances lean growth by stimulating the mTORC1-dependent translation initiation pathway, leading to protein synthesis in skeletal muscle of neonates.
[Mh] Termos MeSH primário: Leucina/farmacologia
Proteínas Musculares/efeitos dos fármacos
Músculo Esquelético/efeitos dos fármacos
Biossíntese de Proteínas/efeitos dos fármacos
[Mh] Termos MeSH secundário: Alanina/farmacologia
Sistema A de Transporte de Aminoácidos/efeitos dos fármacos
Sistema A de Transporte de Aminoácidos/metabolismo
Animais
Animais Recém-Nascidos
Músculos do Dorso
Suplementos Nutricionais
Nutrição Enteral
Infusões Parenterais
Leucina/administração & dosagem
Alvo Mecanístico do Complexo 1 de Rapamicina
Alvo Mecanístico do Complexo 2 de Rapamicina
Complexos Multiproteicos/efeitos dos fármacos
Complexos Multiproteicos/metabolismo
Proteínas Musculares/metabolismo
Músculo Esquelético/metabolismo
Fosforilação/efeitos dos fármacos
RNA Mensageiro/efeitos dos fármacos
RNA Mensageiro/metabolismo
Proteínas Quinases S6 Ribossômicas 90-kDa/efeitos dos fármacos
Proteínas Quinases S6 Ribossômicas 90-kDa/metabolismo
Proteínas Ribossômicas/efeitos dos fármacos
Proteínas Ribossômicas/genética
Sus scrofa
Suínos
Serina-Treonina Quinases TOR/efeitos dos fármacos
Serina-Treonina Quinases TOR/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System A); 0 (Multiprotein Complexes); 0 (Muscle Proteins); 0 (RNA, Messenger); 0 (Ribosomal Proteins); 0 (ribosomal protein S4); 0 (ribosomal protein S8); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2); EC 2.7.11.1 (Ribosomal Protein S6 Kinases, 90-kDa); GMW67QNF9C (Leucine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160218
[St] Status:MEDLINE
[do] DOI:10.1152/ajpendo.00479.2015



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