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[PMID]: 29402931 [Au] Autor: Bianchi F; Syga L; Moiset G; Spakman D; Schavemaker PE; Punter CM; Seinen AB; van Oijen AM; Robinson A; Poolman B [Ad] Endereço: Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9700AB, Groningen, The Netherlands. [Ti] Título: Steric exclusion and protein conformation determine the localization of plasma membrane transporters. [So] Source: Nat Commun;9(1):501, 2018 02 05. [Is] ISSN: 2041-1723 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: The plasma membrane (PM) of Saccharomyces cerevisiae contains membrane compartments, MCC/eisosomes and MCPs, named after the protein residents Can1 and Pma1, respectively. Using high-resolution fluorescence microscopy techniques we show that Can1 and the homologous transporter Lyp1 are able to diffuse into the MCC/eisosomes, where a limited number of proteins are conditionally trapped at the (outer) edge of the compartment. Upon addition of substrate, the immobilized proteins diffuse away from the MCC/eisosomes, presumably after taking a different conformation in the substrate-bound state. Our data indicate that the mobile fraction of all integral plasma membrane proteins tested shows extremely slow Brownian diffusion through most of the PM. We also show that proteins with large cytoplasmic domains, such as Pma1 and synthetic chimera of Can1 and Lyp1, are excluded from the MCC/eisosomes. We hypothesize that the distinct localization patterns found for these integral membrane proteins in S. cerevisiae arises from a combination of slow lateral diffusion, steric exclusion, and conditional trapping in membrane compartments. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/química Membrana Celular/metabolismo ATPases Translocadoras de Prótons/química Proteínas de Saccharomyces cerevisiae/química Saccharomyces cerevisiae/metabolismo [Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo Membrana Celular/ultraestrutura Difusão Recuperação de Fluorescência Após Fotodegradação Cinética Microdomínios da Membrana Conformação Proteica Transporte Proteico ATPases Translocadoras de Prótons/metabolismo Saccharomyces cerevisiae/ultraestrutura Proteínas de Saccharomyces cerevisiae/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (CAN1 protein, S cerevisiae); 0 (LYP1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (PMA1 protein, S cerevisiae); EC 3.6.3.14 (Proton-Translocating ATPases) [Em] Mês de entrada: 1803 [Cu] Atualização por classe: 180307 [Lr] Data última revisão: 180307 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 180207 [St] Status: MEDLINE [do] DOI: 10.1038/s41467-018-02864-2

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[PMID]: 28454689 [Au] Autor: Steinhauser CB; Wing TT; Gao H; Li X; Burghardt RC; Wu G; Bazer FW; Johnson GA [Ad] Endereço: Department of Veterinary Integrative Biosciences, Texas A&M University, 4458 TAMU, College Station, TX 77843-4458, USA. [Ti] Título: Identification of appropriate reference genes for qPCR analyses of placental expression of SLC7A3 and induction of SLC5A1 in porcine endometrium. [So] Source: Placenta;52:1-9, 2017 Apr. [Is] ISSN: 1532-3102 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: INTRODUCTION: Endometria and placentae undergo developmental changes that affect the stability of genes used as references for normalization of qPCR data. We identified genes that are stable within the porcine endometrium and placenta throughout pregnancy, and elucidated the temporal/spatial mRNA localization of the glucose and arginine transporters, solute carrier family (SLC) 5A1 and SLC7A3, respectively. MATERIALS AND METHODS: qPCR was performed for 10 genes within porcine endometria from Days 5, 11, and 15 of the estrous cycle and 11, 15, 25, 40, 60, and 85 of pregnancy; and chorioallantois from Days 30, 35, 45, 50, 60, and 85. Gene stability was analyzed using GeNorm and NormFinder algorithms. qPCR and in situ hybridization determined temporal/spatial localization of SLC5A1 and SLC7A3 at the uterine-placental interface. RESULTS: The geometric mean of TATA-binding protein (TBP), hypoxanthine phosphoribosyl transferase 1 (HPRT1), and tubulin alpha 1B (TUBA1B) provides acceptable reference values for porcine placenta. The geometric mean of TBP, beta actin (ACTB), and succinate dehydrogenase complex subunit A flavoprotein (SDHA) is acceptable for endometria. SLC5A1 is induced by estrogen in endometrial luminal epithelium (LE) on Days 12 and 13 of pregnancy. SLC7A3 is expressed in the chorion. DISCUSSION AND CONCLUSION: Using appropriate reference genes resulted in complementary results between qPCR and in situ hybridization techniques for SLC5A1 and SLC7A3 mRNAs. SLC5A1 is induced in uterine LE by estrogen of trophectoderm origin when the blastocyst is free-floating and dependent on glucose from the endometrium, and SLC7A3 is expressed by the established placenta to support fetal growth. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo Endométrio/metabolismo Genes Essenciais Placenta/metabolismo Reação em Cadeia da Polimerase em Tempo Real/métodos Transportador 1 de Glucose-Sódio/metabolismo [Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/genética Animais Feminino Gravidez Transportador 1 de Glucose-Sódio/genética Suínos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (Sodium-Glucose Transporter 1) [Em] Mês de entrada: 1803 [Cu] Atualização por classe: 180305 [Lr] Data última revisão: 180305 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170430 [St] Status: MEDLINE

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[PMID]: 29277611 [Au] Autor: Li H; Chen S; Liu J; Guo X; Xiang X; Dong T; Ran P; Li Q; Zhu B; Zhang X; Wang D; Xiao C; Zheng S [Ad] Endereço: School of Medicine, Yunnan University, Kunming, PR China. [Ti] Título: Long non-coding RNA PVT1-5 promotes cell proliferation by regulating miR-126/SLC7A5 axis in lung cancer. [So] Source: Biochem Biophys Res Commun;495(3):2350-2355, 2018 01 15. [Is] ISSN: 1090-2104 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Dysregulated long non-coding RNAs (lncRNAs) and microRNAs (miRNAs) play key roles in the development of human cancers. The lncRNA plasmacytoma variant translocation 1 (PVT1) is reported to be an oncogene in a variety of cancers. However, the roles of PVT1-5 and its related miRNAs in lung cancer are poorly understood. In this study, we found that PVT1-5 expression was significantly increased in lung cancer tissues and cell lines. By using biotin-labeled lncRNA-PVT1-5 probe for miRNA in vivo precipitation (miRIP) in lung cancer cells and dual-luciferase reporterassays, we identified that miR-126 was associated with lncRNA-PVT1-5. Furthermore, knockdown of lncRNA-PVT1-5 in cells could down-regulate the expression of SLC7A5, the target of oncogenic miR-126, resulting in the cell proliferation. Conversely, inhibiting the expression of miR-126 markedly increased the expression of SLC7A5 and alleviated cell proliferation inhibition. Thus, our results indicated that lncRNA-PVT1-5 may function as a competing endogenous RNA (ceRNA) for miR-126 to promote cell proliferation by regulating the miR-126/SLC7A5 pathway, suggesting that lncRNA-PVT1-5 plays a crucial role in lung cancer progression and lncRNA-PVT1-5/miR-126/SLC7A5 regulatory network may shed light on tumorigenesis in lung cancer. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo Proliferação Celular Neoplasias Pulmonares/metabolismo Neoplasias Pulmonares/patologia MicroRNAs/metabolismo RNA Longo não Codificante/metabolismo [Mh] Termos MeSH secundário: Células A549 Regulação Neoplásica da Expressão Gênica Seres Humanos Redes e Vias Metabólicas [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (MIRN126 microRNA, human); 0 (MicroRNAs); 0 (PVT1 long-non-coding RNA, human); 0 (RNA, Long Noncoding); 0 (SLC7A6 protein, human) [Em] Mês de entrada: 1802 [Cu] Atualização por classe: 180214 [Lr] Data última revisão: 180214 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 171227 [St] Status: MEDLINE

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[PMID]: 28937983 [Au] Autor: Dadone-Montaudié B; Ambrosetti D; Dufour M; Darcourt J; Almairac F; Coyne J; Virolle T; Humbert O; Burel-Vandenbos F [Ad] Endereço: Department of Pathology, University Hospital, Nice, France. [Ti] Título: [18F] FDOPA standardized uptake values of brain tumors are not exclusively dependent on LAT1 expression. [So] Source: PLoS One;12(9):e0184625, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: [18F]-FDOPA is a labeled amino acid (AA) analog used for positron emission tomography (PET) which is gaining increasing interest in the evaluation of brain tumors (BT). The AA-transporter LAT1 has been shown to be involved in [18F]-FDOPA uptake. The aim of this study was to determine whether the [18F]-FDOPA uptake was correlated with level of LAT1 expression in BT. Twenty-eight BT (including 19 gliomas and 9 metastases) were investigated by [18F]-FDOPA-PET prior to surgery and by anti-LAT1 immunohistochemistry on surgical specimens. The quantitative [18F]-FDOPA measured parameters were SUVmax, SUVmean and SUVpeak. LAT1 expression was quantified using a score (0 to 400). A significant [18F]-FDOPA uptake was associated with a LAT1 score ≥ 100 (p = 0.02) but there was no linear correlation between intensity of [18F]-FDOPA uptake and score of LAT1 expression whatever the parameters considered. LAT1 expression alone is not sufficient to explain variation of intensity of [18F]-FDOPA uptake in BT. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo Neoplasias Encefálicas/metabolismo Di-Hidroxifenilalanina/farmacocinética Radioisótopos de Flúor/farmacocinética Tomografia por Emissão de Pósitrons Compostos Radiofarmacêuticos/farmacocinética [Mh] Termos MeSH secundário: Adulto Idoso Encéfalo/diagnóstico por imagem Encéfalo/metabolismo Encéfalo/patologia Encéfalo/cirurgia Neoplasias Encefálicas/diagnóstico por imagem Neoplasias Encefálicas/patologia Neoplasias Encefálicas/cirurgia Feminino Glioma/diagnóstico por imagem Glioma/metabolismo Glioma/patologia Glioma/cirurgia Seres Humanos Imuno-Histoquímica Masculino Meia-Idade [Pt] Tipo de publicação: CLINICAL TRIAL; JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (Fluorine Radioisotopes); 0 (Radiopharmaceuticals); 0 (SLC7A6 protein, human); 63-84-3 (Dihydroxyphenylalanine) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171017 [Lr] Data última revisão: 171017 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170923 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0184625

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[PMID]: 28701241 [Au] Autor: Zheng P; Yu B; He J; Yu J; Mao X; Luo Y; Luo J; Huang Z; Tian G; Zeng Q; Che L; Chen D [Ad] Endereço: 1Animal Nutrition Institute,Sichuan Agricultural University,Xinkang Road 46#,Ya'an,Sichuan Province 625014,People's Republic of China. [Ti] Título: Arginine metabolism and its protective effects on intestinal health and functions in weaned piglets under oxidative stress induced by diquat. [So] Source: Br J Nutr;117(11):1495-1502, 2017 Jun. [Is] ISSN: 1475-2662 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: The intestine plays key roles in maintaining body arginine (Arg) homoeostasis. Meanwhile, the intestine is very susceptible to reactive oxygen species. In light of this, the study aimed to explore the effects of Arg supplementation on intestinal morphology, Arg transporters and metabolism, and the potential protective mechanism of Arg supplementation in piglets under oxidative stress. A total of thirty-six weaned piglets were randomly allocated to six groups with six replicates and fed a base diet (0·95 % Arg,) or base diet supplemented with 0·8 % and 1·6 % l-Arg for 1 week, respectively. Subsequently, a challenge test was conducted by intraperitoneal injection of diquat, an initiator of radical production, or sterile saline. The whole trial lasted 11 d. The diquat challenge significantly decreased plasma Arg concentration at 6 h after injection (P<0·05), lowered villus height in the jejunum and ileum (P<0·05) as well as villus width and crypt depth in the duodenum, jejunum and ileum (P<0·05). Oxidative stress significantly increased cationic amino acid transporter (CAT)-1, CAT-2 and CAT-3, mRNA levels (P<0·05), decreased arginase II (ARGII) and inducible nitric oxide synthase mRNA levels, and increased TNF- α mRNA level in the jejunum (P<0·05). Supplementation with Arg significantly decreased crypt depth (P<0·05), suppressed CAT-1 mRNA expression induced by diquat (P<0·05), increased ARGII and endothelial nitric oxide synthase mRNA levels (P<0·05), and effectively relieved the TNF- α mRNA expression induced by diquat in the jejunum (P<0·05). It is concluded that oxidative stress decreased Arg bioavailability and increased expression of inflammatory cytokines in the jejunum, and that Arg supplementation has beneficial effects in the jejunum through regulation of the metabolism of Arg and suppression of inflammatory cytokine expression in piglets. [Mh] Termos MeSH primário: Arginina/farmacologia Suplementos Nutricionais Diquat/efeitos adversos Jejuno/efeitos dos fármacos Óxido Nítrico Sintase Tipo II/metabolismo Estresse Oxidativo/efeitos dos fármacos Fator de Necrose Tumoral alfa/metabolismo [Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo Animais Arginase/metabolismo Arginina/sangue Arginina/metabolismo Duodeno/efeitos dos fármacos Íleo/efeitos dos fármacos Inflamação/metabolismo Inflamação/prevenção & controle Mucosa Intestinal/efeitos dos fármacos Mucosa Intestinal/metabolismo Jejuno/metabolismo Jejuno/patologia RNA Mensageiro/metabolismo Suínos Desmame [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (RNA, Messenger); 0 (Tumor Necrosis Factor-alpha); 94ZLA3W45F (Arginine); A9A615U4MP (Diquat); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 3.5.3.1 (Arginase) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170731 [Lr] Data última revisão: 170731 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170714 [St] Status: MEDLINE [do] DOI: 10.1017/S0007114517001519

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[PMID]: 28700644 [Au] Autor: Moretti ML; Alárcon-Reverte R; Pearce S; Morran S; Hanson BD [Ad] Endereço: Department of Plant Sciences, University of California, Davis, California, United States of America. [Ti] Título: Transcription of putative tonoplast transporters in response to glyphosate and paraquat stress in Conyza bonariensis and Conyza canadensis and selection of reference genes for qRT-PCR. [So] Source: PLoS One;12(7):e0180794, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Herbicide resistance is a challenge for modern agriculture further complicated by cases of resistance to multiple herbicides. Conyza bonariensis and Conyza canadensis are invasive weeds of field crops, orchards, and non-cropped areas in many parts of the world. In California, USA, Conyza populations resistant to the herbicides glyphosate and paraquat have recently been described. Although the mechanism conferring resistance to glyphosate and paraquat in these species was not elucidated, reduced translocation of these herbicides was observed under experimental conditions in both species. Glyphosate and paraquat resistance associated with reduced translocation are hypothesized to be a result of sequestration of herbicides into the vacuole, with the possible involvement of over-expression of genes encoding tonoplast transporters of ABC-transporter families in cases of glyphosate resistance or cationic amino acid transporters (CAT) in cases of paraquat resistance. However, gene expression in response to herbicide treatment has not been studied in glyphosate and paraquat resistant populations. In the current study, we evaluated the transcript levels of genes possibly involved in resistance using real-time PCR. First, we evaluated eight candidate reference genes following herbicide treatment and selected three genes that exhibited stable expression profiles; ACTIN, HEAT-SHOCK-PROTEIN-70, and CYCLOPHILIN. The reference genes identified here can be used for further studies related to plant-herbicide interactions. We used these reference genes to assay the transcript levels of EPSPS, ABC transporters, and CAT in response to herbicide treatment in susceptible and resistant Conyza spp. lines. No transcription changes were observed in EPSPS or CAT genes after glyphosate or paraquat treatment, suggesting that these genes are not involved in the resistance mechanism. Transcription of the two ABC transporter genes increased following glyphosate treatment in all Conyza spp. lines. Transcription of ABC transporters also increased after paraquat treatment in all three lines of C. bonariensis. However, in C. canadensis, paraquat treatment increased transcription of only one ABC transporter gene in the susceptible line. The increase in transcription of ABC transporters after herbicide treatment is likely a stress response based on similar response observed across all Conyza lines regardless of resistance or sensitivity to glyphosate or paraquat, thus these genes do not appear to be directly involved in the mechanism of resistance in Conyza spp. [Mh] Termos MeSH primário: Conyza/efeitos dos fármacos Conyza/metabolismo Glicina/análogos & derivados Paraquat/farmacologia [Mh] Termos MeSH secundário: Actinas/genética Actinas/metabolismo Sistemas de Transporte de Aminoácidos Básicos/genética Sistemas de Transporte de Aminoácidos Básicos/metabolismo Conyza/genética Ciclofilinas/genética Ciclofilinas/metabolismo Glicina/farmacologia Proteínas de Choque Térmico HSP70/genética Proteínas de Choque Térmico HSP70/metabolismo Proteínas de Plantas/genética Proteínas de Plantas/metabolismo Reação em Cadeia da Polimerase em Tempo Real Reação em Cadeia da Polimerase Via Transcriptase Reversa [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actins); 0 (Amino Acid Transport Systems, Basic); 0 (HSP70 Heat-Shock Proteins); 0 (Plant Proteins); 4632WW1X5A (glyphosate); EC 5.2.1.- (Cyclophilins); PLG39H7695 (Paraquat); TE7660XO1C (Glycine) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170925 [Lr] Data última revisão: 170925 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170713 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0180794

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[PMID]: 28382174 [Au] Autor: Jiang Y; Cao Y; Wang Y; Li W; Liu X; Lv Y; Li X; Mi J [Ad] Endereço: Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine; Institute of Cancer Stem Cell, Dalian Medical University. [Ti] Título: Cysteine transporter SLC3A1 promotes breast cancer tumorigenesis. [So] Source: Theranostics;7(4):1036-1046, 2017. [Is] ISSN: 1838-7640 [Cp] País de publicação: Australia [La] Idioma: eng [Ab] Resumo: Cysteine is an essential amino acid for infants, aged people as well as patients with metabolic disorders. Although the thiol group of cysteine side chain is active in oxidative reactions, the role of cysteine in cancer remains largely unknown. Here, we report that the expression level of the solute carrier family 3, member 1 (SLC3A1), the cysteine carrier, tightly correlated with clinical stages and patients' survival. Elevated SLC3A1 expression accelerated the cysteine uptake and the accumulation of reductive glutathione (GSH), leading to reduced reactive oxygen species (ROS). ROS increased the stability and activity of PP2Ac, resulting in decreased AKT activity. Hence, SLC3A1 activated the AKT signaling through inhibiting PP2A phosphatase activity. Consistently, overexpression of SLC3A1 enhanced tumorigenesis of breast cancer cells, whereas blocking SLC3A1 either with specific siRNA or SLC3A1 specific inhibitor sulfasalazine suppressed tumor growth and also abolished dietary NAC-promoted tumor growth. Collectively, our data demonstrate that SLC3A1 promotes cysteine uptake and determines cellular response to antioxidant N-acetylcysteine, suggesting SLC3A1 is a potential therapeutic target for breast cancer. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo Sistemas de Transporte de Aminoácidos Neutros/metabolismo Neoplasias da Mama/fisiopatologia Carcinogênese Cisteína/metabolismo [Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/genética Sistemas de Transporte de Aminoácidos Neutros/genética Animais Neoplasias da Mama/patologia Linhagem Celular Tumoral Modelos Animais de Doenças Perfilação da Expressão Gênica Células HEK293 Xenoenxertos Seres Humanos Camundongos Endogâmicos BALB C Camundongos Nus Análise de Sobrevida [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (Amino Acid Transport Systems, Neutral); 0 (SLC3A1 protein, human); K848JZ4886 (Cysteine) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171023 [Lr] Data última revisão: 171023 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170407 [St] Status: MEDLINE [do] DOI: 10.7150/thno.18005

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[PMID]: 28270646 [Au] Autor: Fazaeli S; Ashouri S; Kheirollahi M; Mohammadi M; Fazilati M [Ti] Título: A Novel Mutation in SLC7A9 Gene in Cystinuria. [So] Source: Iran J Kidney Dis;11(2):138-141, 2017 Mar. [Is] ISSN: 1735-8604 [Cp] País de publicação: Iran [La] Idioma: eng [Ab] Resumo: INTRODUCTION: Cystinuria is an inherited disorder affecting luminal transport of cystine and dibasic amino acids. Because of the poor solubility of cystine in urine, stone formation in the kidney occurs frequently. Cystinuria is associated with mutations in the SLC3A1 and SLC7A9 genes. Despite the population-specific distribution of mutations in the SLC7A9 genes, there are few genetic data reported for cystinuric patients from the Middle East. MATERIALS AND METHODS: Exon 4 of the SLC7A9 gene was sequenced in 21 patients with cystinuria, using the polymerase chain reaction and sequencing methods. RESULTS: A new variation in exon 4 of the SLC7A9 gene was identified, which was insertion of 1 adenine nucleotide between 2 cytosine nucleotides in position c.213-214insA. CONCLUSIONS: It seems to be important since it causes frame shift and it may be an important cause to make disease. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/genética Cistinúria/genética [Mh] Termos MeSH secundário: Adolescente Adulto Idoso Criança Éxons Feminino Seres Humanos Irã (Geográfico) Masculino Meia-Idade Mutação Reação em Cadeia da Polimerase Adulto Jovem [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (SLC7A9 protein, human) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170915 [Lr] Data última revisão: 170915 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170309 [St] Status: MEDLINE

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[PMID]: 28184026 [Au] Autor: Zhu Y; Yang C; Weng M; Zhang Y; Yang C; Jin Y; Yang W; He Y; Wu Y; Zhang Y; Wang G; RajkumarEzakiel Redpath RJ; Zhang L; Jin X; Liu Y; Sun Y; Ning N; Qiao Y; Zhang F; Li Z; Wang T; Zhang Y; Li X [Ad] Endereço: Department of Gastrointestinal Medical Oncology, The Affiliated Tumor Hospital of Harbin Medical University, Harbin, China. [Ti] Título: Identification of TMEM208 and PQLC2 as reference genes for normalizing mRNA expression in colorectal cancer treated with aspirin. [So] Source: Oncotarget;8(14):22759-22771, 2017 Apr 04. [Is] ISSN: 1949-2553 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Numerous evidences indicate that aspirin usage causes a significant reduction in colorectal cancer. However, the molecular mechanisms about aspirin preventing colon cancer are largely unknown. Quantitative reverse transcription polymerase chain reaction (qRT-PCR) is a most frequently used method to identify the target molecules regulated by certain compound. However, this method needs stable internal reference genes to analyze the expression change of the targets. In this study, the transcriptional stabilities of several traditional reference genes were evaluated in colon cancer cells treated with aspirin, and also, the suitable internal reference genes were screened by using a microarray and were further identified by using the geNorm and NormFinder softwares, and then were validated in more cell lines and xenografts. We have showed that three traditional internal reference genes, ß-actin, GAPDH and α-tubulin, are not suitable for studying gene transcription in colon cancer cells treated with aspirin, and we have identified and validated TMEM208 and PQLC2 as the ideal internal reference genes for detecting the molecular targets of aspirin in colon cancer in vitro and in vivo. This study reveals stable internal reference genes for studying the target genes of aspirin in colon cancer, which will contribute to identify the molecular mechanism behind aspirin preventing colon cancer. [Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/genética Anti-Inflamatórios não Esteroides/farmacologia Aspirina/farmacologia Neoplasias Colorretais/genética Perfilação da Expressão Gênica/normas Proteínas de Membrana/genética RNA Mensageiro/metabolismo [Mh] Termos MeSH secundário: Actinas/genética Actinas/metabolismo Sistemas de Transporte de Aminoácidos Básicos/metabolismo Animais Apoptose/efeitos dos fármacos Proliferação Celular/efeitos dos fármacos Neoplasias Colorretais/tratamento farmacológico Neoplasias Colorretais/patologia Seres Humanos Masculino Proteínas de Membrana/metabolismo Camundongos Camundongos Nus RNA Mensageiro/genética Reação em Cadeia da Polimerase em Tempo Real Padrões de Referência Reação em Cadeia da Polimerase Via Transcriptase Reversa Tubulina (Proteína)/genética Tubulina (Proteína)/metabolismo Células Tumorais Cultivadas Ensaios Antitumorais Modelo de Xenoenxerto [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Actins); 0 (Amino Acid Transport Systems, Basic); 0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Membrane Proteins); 0 (PQLC2 protein, human); 0 (RNA, Messenger); 0 (TMEM208 protein, human); 0 (Tubulin); R16CO5Y76E (Aspirin) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171013 [Lr] Data última revisão: 171013 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170211 [St] Status: MEDLINE [do] DOI: 10.18632/oncotarget.15191

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[PMID]: 28165480 [Au] Autor: Zee T; Bose N; Zee J; Beck JN; Yang S; Parihar J; Yang M; Damodar S; Hall D; O'Leary MN; Ramanathan A; Gerona RR; Killilea DW; Chi T; Tischfield J; Sahota A; Kahn A; Stoller ML; Kapahi P [Ad] Endereço: Department of Urology, University of California, San Francisco, San Francisco, California, USA. [Ti] Título: α-Lipoic acid treatment prevents cystine urolithiasis in a mouse model of cystinuria. [So] Source: Nat Med;23(3):288-290, 2017 Mar. [Is] ISSN: 1546-170X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Cystinuria is an incompletely dominant disorder characterized by defective urinary cystine reabsorption that results in the formation of cystine-based urinary stones. Current treatment options are limited in their effectiveness at preventing stone recurrence and are often poorly tolerated. We report that the nutritional supplement α-lipoic acid inhibits cystine stone formation in the Slc3a1 mouse model of cystinuria by increasing the solubility of urinary cystine. These findings identify a novel therapeutic strategy for the clinical treatment of cystinuria. [Mh] Termos MeSH primário: Cistina/efeitos dos fármacos Cistinúria/metabolismo Rim/efeitos dos fármacos Ácido Tióctico/farmacologia Urolitíase/metabolismo [Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/genética Sistemas de Transporte de Aminoácidos Neutros/genética Animais Cistina/metabolismo Modelos Animais de Doenças Rim/diagnóstico por imagem Rim/metabolismo Camundongos Camundongos Knockout Solubilidade/efeitos dos fármacos Urolitíase/diagnóstico por imagem Microtomografia por Raio-X [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Amino Acid Transport Systems, Basic); 0 (Amino Acid Transport Systems, Neutral); 0 (Slc3a1 protein, mouse); 48TCX9A1VT (Cystine); 73Y7P0K73Y (Thioctic Acid) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 171027 [Lr] Data última revisão: 171027 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170207 [St] Status: MEDLINE [do] DOI: 10.1038/nm.4280

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