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Pesquisa : D12.776.157.530.500 [Categoria DeCS]
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[PMID]:28742265
[Au] Autor:Alsubhi S; Alhashem A; Faqeih E; Alfadhel M; Alfaifi A; Altuwaijri W; Alsahli S; Aldhalaan H; Alkuraya FS; Hundallah K; Mahmoud A; Alasmari A; Mutairi FA; Abduraouf H; AlRasheed L; Alshahwan S; Tabarki B
[Ad] Endereço:Division of Pediatric Neurology, Department of Pediatrics, Prince Sultan Military Medical City, Riyadh, Saudi Arabia.
[Ti] Título:Congenital disorders of glycosylation: The Saudi experience.
[So] Source:Am J Med Genet A;173(10):2614-2621, 2017 Oct.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We retrospectively reviewed Saudi patients who had a congenital disorder of glycosylation (CDG). Twenty-seven Saudi patients (14 males, 13 females) from 13 unrelated families were identified. Based on molecular studies, the 27 CDG patients were classified into different subtypes: ALG9-CDG (8 patients, 29.5%), ALG3-CDG (7 patients, 26%), COG6-CDG (7 patients, 26%), MGAT2-CDG (3 patients, 11%), SLC35A2-CDG (1 patient), and PMM2-CDG (1 patient). All the patients had homozygous gene mutations. The combined carrier frequency of CDG for the encountered founder mutations in the Saudi population is 11.5 per 10,000, which translates to a minimum disease burden of 14 patients per 1,000,000. Our study provides comprehensive epidemiologic information and prevalence figures for each of these CDG in a large cohort of congenital disorder of glycosylation patients.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Defeitos Congênitos da Glicosilação/genética
Mutação
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/genética
Adolescente
Criança
Pré-Escolar
Defeitos Congênitos da Glicosilação/epidemiologia
Feminino
Glicosilação
Homozigoto
Seres Humanos
Lactente
Masculino
Manosiltransferases/genética
Proteínas de Membrana/genética
Oxigenases de Função Mista/genética
Proteínas de Transporte de Monossacarídeos/genética
N-Acetilglucosaminiltransferases/genética
Fenótipo
Estudos Retrospectivos
Arábia Saudita/epidemiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Biomarkers, Tumor); 0 (COG6 protein, human); 0 (Membrane Proteins); 0 (Monosaccharide Transport Proteins); 0 (UDP-galactose translocator); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.- (4-coumaroyl-D-glucose hydroxylase); EC 2.4.1.- (ALG3 protein, human); EC 2.4.1.- (ALG9 protein, human); EC 2.4.1.- (Mannosyltransferases); EC 2.4.1.- (N-Acetylglucosaminyltransferases); EC 2.4.1.143 (alpha-1,6-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38358


  2 / 9116 MEDLINE  
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[PMID]:28464256
[Au] Autor:Shin HY; Nijland JG; de Waal PP; Driessen AJM
[Ad] Endereço:Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology, University of Groningen, Zernike Institute for Advanced Materials and Kluyver Centre for Genomics of Industrial Fermentation, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
[Ti] Título:The amino-terminal tail of Hxt11 confers membrane stability to the Hxt2 sugar transporter and improves xylose fermentation in the presence of acetic acid.
[So] Source:Biotechnol Bioeng;114(9):1937-1945, 2017 09.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hxt2 is a glucose repressed, high affinity glucose transporter of the yeast Saccharomyces cerevisiae and is subjected to high glucose induced degradation. Hxt11 is a sugar transporter that is stably expressed at the membrane irrespective the sugar concentration. To transfer this property to Hxt2, the N-terminal tail of Hxt2 was replaced by the corresponding region of Hxt11 yielding a chimeric Hxt11/2 transporter. This resulted in the stable expression of Hxt2 at the membrane and improved the growth on 8% d-glucose and 4% d-xylose. Mutation of N361 of Hxt11/2 into threonine reversed the specificity for d-xylose over d-glucose with high d-xylose transport rates. This mutant supported efficient sugar fermentation of both d-glucose and d-xylose at industrially relevant sugar concentrations even in the presence of the inhibitor acetic acid which is normally present in lignocellulosic hydrolysates. Biotechnol. Bioeng. 2017;114: 1937-1945. © 2017 The Authors. Biotechnology and Bioengineering Published by Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Ácido Acético/metabolismo
Membrana Celular/metabolismo
Melhoramento Genético/métodos
Proteínas Facilitadoras de Transporte de Glucose/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
Xilose/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/genética
Glucose
Proteínas Facilitadoras de Transporte de Glucose/genética
Engenharia Metabólica/métodos
Proteínas de Transporte de Monossacarídeos/genética
Proteínas de Saccharomyces cerevisiae/genética
Relação Estrutura-Atividade
Xilose/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Glucose Transport Proteins, Facilitative); 0 (HXT11 protein, S cerevisiae); 0 (HXT2 protein, S cerevisiae); 0 (Monosaccharide Transport Proteins); 0 (Saccharomyces cerevisiae Proteins); A1TA934AKO (Xylose); IY9XDZ35W2 (Glucose); Q40Q9N063P (Acetic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26322


  3 / 9116 MEDLINE  
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[PMID]:28455339
[Au] Autor:Tanaka M; Hiramoto T; Tada H; Shintani T; Gomi K
[Ad] Endereço:Laboratory of Bioindustrial Genomics, Department of Bioindustrial Informatics and Genomics, Graduate School of Agricultural Science, Tohoku University, Aramaki, Aoba-ku, Sendai, Japan.
[Ti] Título:Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillus oryzae.
[So] Source:Appl Environ Microbiol;83(13), 2017 Jul 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:produces copious amount of amylolytic enzymes, and MalP, a major maltose permease, is required for the expression of amylase-encoding genes. The expression of these genes is strongly repressed by carbon catabolite repression (CCR) in the presence of glucose. MalP is transported from the plasma membrane to the vacuole by endocytosis, which requires the homolog of E6-AP carboxyl terminus ubiquitin ligase HulA, an ortholog of yeast Rsp5. In yeast, arrestin-like proteins mediate endocytosis as adaptors of Rsp5 and transporters. In the present study, we examined the involvement of CreD, an arrestin-like protein, in glucose-induced MalP endocytosis and CCR of amylase-encoding genes. Deletion of inhibited the glucose-induced endocytosis of MalP, and CreD showed physical interaction with HulA. Phosphorylation of CreD was detected by Western blotting, and two serine residues were determined as the putative phosphorylation sites. However, the phosphorylation state of the serine residues did not regulate MalP endocytosis and its interaction with HulA. Although α-amylase production was significantly repressed by deletion, both phosphorylation and dephosphorylation mimics of CreD had a negligible effect on α-amylase activity. Interestingly, dephosphorylation of CreD was required for CCR relief of amylase genes that was triggered by disruption of the deubiquitinating enzyme-encoding gene The α-amylase activity of the mutant was 1.6-fold higher than that of the wild type, and the dephosphorylation mimic of CreD further improved the α-amylase activity by 2.6-fold. These results indicate that a combination of the dephosphorylation mutation of CreD and disruption increased the production of amylolytic enzymes in In eukaryotes, glucose induces carbon catabolite repression (CCR) and proteolytic degradation of plasma membrane transporters via endocytosis. Glucose-induced endocytosis of transporters is mediated by their ubiquitination, and arrestin-like proteins act as adaptors of transporters and ubiquitin ligases. In this study, we showed that CreD, an arrestin-like protein, is involved in glucose-induced endocytosis of maltose permease and carbon catabolite derepression of amylase gene expression in Dephosphorylation of CreD was required for CCR relief triggered by the disruption of , which encodes a deubiquitinating enzyme; a combination of the phosphorylation-defective mutation of CreD and disruption dramatically improved α-amylase production. This study shows the dual function of an arrestin-like protein and provides a novel approach for improving the production of amylolytic enzymes in .
[Mh] Termos MeSH primário: Arrestina/metabolismo
Aspergillus oryzae/metabolismo
Repressão Catabólica
Endocitose
Proteínas Fúngicas/genética
Proteínas de Transporte de Monossacarídeos/genética
alfa-Amilases/genética
[Mh] Termos MeSH secundário: Arrestina/genética
Aspergillus oryzae/enzimologia
Aspergillus oryzae/genética
Carbono/metabolismo
Proteínas Fúngicas/metabolismo
Regulação Fúngica da Expressão Gênica
Glucose/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Mutação
Fosforilação
Transporte Proteico
alfa-Amilases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arrestin); 0 (Fungal Proteins); 0 (Monosaccharide Transport Proteins); 7440-44-0 (Carbon); 9055-23-6 (maltose permease); EC 3.2.1.1 (alpha-Amylases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


  4 / 9116 MEDLINE  
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[PMID]:28468835
[Au] Autor:Hovsepian J; Defenouillère Q; Albanèse V; Váchová L; Garcia C; Palková Z; Léon S
[Ad] Endereço:Institut Jacques Monod, UMR 7592 Centre National de la Recherche Scientifique/Université Paris-Diderot, Sorbonne Paris Cité, 75013 Paris, France.
[Ti] Título:Multilevel regulation of an α-arrestin by glucose depletion controls hexose transporter endocytosis.
[So] Source:J Cell Biol;216(6):1811-1831, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nutrient availability controls the landscape of nutrient transporters present at the plasma membrane, notably by regulating their ubiquitylation and subsequent endocytosis. In yeast, this involves the Nedd4 ubiquitin ligase Rsp5 and arrestin-related trafficking adaptors (ARTs). ARTs are targeted by signaling pathways and warrant that cargo ubiquitylation and endocytosis appropriately respond to nutritional inputs. Here, we show that glucose deprivation regulates the ART protein Csr2/Art8 at multiple levels to trigger high-affinity glucose transporter endocytosis. Csr2 is transcriptionally induced in these conditions through the AMPK orthologue Snf1 and downstream transcriptional repressors. Upon synthesis, Csr2 becomes activated by ubiquitylation. In contrast, glucose replenishment induces transcriptional shutdown and switches Csr2 to an inactive, deubiquitylated form. This glucose-induced deubiquitylation of Csr2 correlates with its phospho-dependent association with 14-3-3 proteins and involves protein kinase A. Thus, two glucose signaling pathways converge onto Csr2 to regulate hexose transporter endocytosis by glucose availability. These data illustrate novel mechanisms by which nutrients modulate ART activity and endocytosis.
[Mh] Termos MeSH primário: Arrestina/metabolismo
Endocitose
Glucose/deficiência
Proteínas de Transporte de Monossacarídeos/metabolismo
Proteínas Nucleares/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas 14-3-3/metabolismo
Arrestina/genética
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Regulação Fúngica da Expressão Gênica
Proteínas de Transporte de Monossacarídeos/genética
Mutação
Proteínas Nucleares/genética
Proteína Fosfatase 1/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Repressoras/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Tempo
Transcrição Genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (14-3-3 Proteins); 0 (Arrestin); 0 (BMH1 protein, S cerevisiae); 0 (BMH2 protein, S cerevisiae); 0 (Csr2 protein, S cerevisiae); 0 (HXT7 protein, S cerevisiae); 0 (Hxt6 protein, S cerevisiae); 0 (MIG1 protein, S cerevisiae); 0 (Mig2 protein, S cerevisiae); 0 (Monosaccharide Transport Proteins); 0 (Nuclear Proteins); 0 (Repressor Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.1.- (SNF1-related protein kinases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 3.1.3.16 (Protein Phosphatase 1); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171205
[Lr] Data última revisão:
171205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610094


  5 / 9116 MEDLINE  
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[PMID]:28961260
[Au] Autor:Cappuccio G; Pinelli M; Alagia M; Donti T; Day-Salvatore DL; Veggiotti P; De Giorgis V; Lunghi S; Vari MS; Striano P; Brunetti-Pierri N; Kennedy AD; Elsea SH
[Ad] Endereço:Department of Translational Medicine, Sector of Pediatrics, Federico II, University, Naples, Italy.
[Ti] Título:Biochemical phenotyping unravels novel metabolic abnormalities and potential biomarkers associated with treatment of GLUT1 deficiency with ketogenic diet.
[So] Source:PLoS One;12(9):e0184022, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Global metabolomic profiling offers novel opportunities for the discovery of biomarkers and for the elucidation of pathogenic mechanisms that might lead to the development of novel therapies. GLUT1 deficiency syndrome (GLUT1-DS) is an inborn error of metabolism due to reduced function of glucose transporter type 1. Clinical presentation of GLUT1-DS is heterogeneous and the disorder mirrors patients with epilepsy, movement disorders, or any paroxysmal events or unexplained neurological manifestation triggered by exercise or fasting. The diagnostic biochemical hallmark of the disease is a reduced cerebrospinal fluid (CSF)/blood glucose ratio and the only available treatment is ketogenic diet. This study aimed at advancing our understanding of the biochemical perturbations in GLUT1-DS pathogenesis through biochemical phenotyping and the treatment of GLUT1-DS with a ketogenic diet. Metabolomic analysis of three CSF samples from GLUT1-DS patients not on ketogenic diet was feasible inasmuch as CSF sampling was used for diagnosis before to start with ketogenic diet. The analysis of plasma and urine samples obtained from GLUT1-DS patients treated with a ketogenic diet showed alterations in lipid and amino acid profiles. While subtle, these were consistent findings across the patients with GLUT1-DS on ketogenic diet, suggesting impacts on mitochondrial physiology. Moreover, low levels of free carnitine were present suggesting its consumption in GLUT1-DS on ketogenic diet. 3-hydroxybutyrate, 3-hydroxybutyrylcarnitine, 3-methyladipate, and N-acetylglycine were identified as potential biomarkers of GLUT1-DS on ketogenic diet. This is the first study to identify CSF, plasma, and urine metabolites associated with GLUT1-DS, as well as biochemical changes impacted by a ketogenic diet. Potential biomarkers and metabolic insights deserve further investigation.
[Mh] Termos MeSH primário: Biomarcadores/metabolismo
Dieta Cetogênica
Proteínas de Transporte de Monossacarídeos/deficiência
[Mh] Termos MeSH secundário: Erros Inatos do Metabolismo dos Carboidratos
Metabolismo Energético
Ácidos Graxos/metabolismo
Seres Humanos
Metabolômica
Proteínas de Transporte de Monossacarídeos/química
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Fatty Acids); 0 (Monosaccharide Transport Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184022


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[PMID]:28931056
[Au] Autor:Tian L; Liu L; Yin Y; Huang M; Chen Y; Xu X; Wu P; Li M; Wu G; Jiang H; Chen Y
[Ad] Endereço:Key Laboratory of Plant Resources Conservation and Sustainable Utilization, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, PR China.
[Ti] Título:Heterogeneity in the expression and subcellular localization of POLYOL/MONOSACCHARIDE TRANSPORTER genes in Lotus japonicus.
[So] Source:PLoS One;12(9):e0185269, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polyols can serve as a means for the translocation of carbon skeletons and energy between source and sink organs as well as being osmoprotective solutes and antioxidants which may be involved in the resistance of some plants to biotic and abiotic stresses. Polyol/Monosaccharide transporter (PLT) proteins previously identified in plants are involved in the loading of polyols into the phloem and are reported to be located in the plasma membrane. The functions of PLT proteins in leguminous plants are not yet clear. In this study, a total of 14 putative PLT genes (LjPLT1-14) were identified in the genome of Lotus japonicus and divided into 4 clades based on phylogenetic analysis. Different patterns of expression of LjPLT genes in various tissues were validated by qRT-PCR analysis. Four genes (LjPLT3, 4, 11, and 14) from clade II were expressed at much higher levels in nodule than in other tissues. Moreover, three of these genes (LjPLT3, 4, and 14) showed significantly increased expression in roots after inoculation with Mesorhizobium loti. Three genes (LjPLT1, 3, and 9) responded when salinity and/or osmotic stresses were applied to L. japonicus. Transient expression of GFP-LjPLT fusion constructs in Arabidopsis and Nicotiana benthamiana protoplasts indicated that the LjPLT1, LjPLT6 and LjPLT7 proteins are localized to the plasma membrane, but LjPLT2 (clade IV), LjPLT3, 4, 5 (clade II) and LjPLT8 (clade III) proteins possibly reside in the Golgi apparatus. The results suggest that members of the LjPLT gene family may be involved in different biological processes, several of which may potentially play roles in nodulation in this nitrogen-fixing legume.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica de Plantas
Loteae/genética
Proteínas de Transporte de Monossacarídeos/genética
Proteínas de Plantas/genética
[Mh] Termos MeSH secundário: Proteínas de Arabidopsis/genética
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Loteae/microbiologia
Mesorhizobium/fisiologia
Proteínas de Transporte de Monossacarídeos/metabolismo
Família Multigênica
Pressão Osmótica
Filogenia
Proteínas de Plantas/metabolismo
Raízes de Plantas/genética
Reação em Cadeia da Polimerase em Tempo Real
Salinidade
Simbiose
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Monosaccharide Transport Proteins); 0 (Plant Proteins); 147336-22-9 (Green Fluorescent Proteins)
[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:170921
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185269


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[PMID]:28692262
[Au] Autor:Mao GL; Yan Y; Chen Y; Wang BF; Xu FF; Zhang ZX; Lin F; Xu HH
[Ad] Endereço:State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources and Key Laboratory of Natural Pesticide and Chemical Biology, Ministry of Education, South China Agricultural University , Guangzhou, Guangdong 510642, People's Republic of China.
[Ti] Título:Family of Ricinus communis Monosaccharide Transporters and RcSTP1 in Promoting the Uptake of a Glucose-Fipronil Conjugate.
[So] Source:J Agric Food Chem;65(30):6169-6178, 2017 Aug 02.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enhancing the systemic distribution of a bioactive compound by exploiting the vascular transport system of a plant presents a means of reducing both the volume and frequency of pesticide/fungicide application. The foliar uptake of the glucose-fipronil conjugate N-[3-cyano-1-[2,6-dichloro-4-(trifluoromethyl)phenyl]-4-[(trifluoromethyl)sulfinyl]-1H-pyrazol-5-yl]-1-(ß-d-glucopyranosyl)-1H-1,2,3-triazole-4-methanamine (GTF) achieved in castor bean (Ricinus communis) and its transport via the phloem are known to be mediated by monosaccharide transporter(s) [MST(s)], although neither the identity of the key MST(s) involved nor the mechanistic basis of its movement have yet to be described. On the basis of homology with Arabidopsis thaliana sugar transporters, the castor bean genome was concluded to harbor 53 genes encoding a sugar transporter, falling into the eight previously defined subfamilies INT, PMT, VGT, STP, ERD6, pGlucT, TMT, and SUT. Transcriptional profiling identified the product of RcSTP1 as a candidate for mediating GTF uptake, because this gene was induced by exposure of the plant to GTF. When RcSTP1 was transiently expressed in onion epidermis cells, the site of RcSTP1 deposition was shown to be the plasma membrane. A functional analysis based on RcSTP1 expression in Xenopus laevis oocytes demonstrated that its product has a high affinity for GTF. The long-distance root-to-shoot transport of GTF was enhanced in a transgenic soybean chimera constitutively expressing RcSTP1.
[Mh] Termos MeSH primário: Glucose/metabolismo
Inseticidas/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Monossacarídeos/metabolismo
Proteínas de Plantas/metabolismo
Pirazóis/metabolismo
Ricinus/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas de Transporte de Monossacarídeos/genética
Floema/metabolismo
Proteínas de Plantas/genética
Ricinus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insecticides); 0 (Monosaccharide Transport Proteins); 0 (Monosaccharides); 0 (Plant Proteins); 0 (Pyrazoles); IY9XDZ35W2 (Glucose); QGH063955F (fipronil)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02044


  8 / 9116 MEDLINE  
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[PMID]:28556183
[Au] Autor:Gras D; Cousin C; Kappeler C; Fung CW; Auvin S; Essid N; Chung BH; Da Costa L; Hainque E; Luton MP; Petit V; Vuillaumier-Barrot S; Boespflug-Tanguy O; Roze E; Mochel F
[Ad] Endereço:APHP, Robert-Debré University Hospital, Department of Paediatric Neurology and Metabolic Diseases, Paris, France.
[Ti] Título:A simple blood test expedites the diagnosis of glucose transporter type 1 deficiency syndrome.
[So] Source:Ann Neurol;82(1):133-138, 2017 Jul.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glucose transporter type 1 (GLUT1) deficiency syndrome (GLUT1-DS) leads to a wide range of neurological symptoms. Ketogenic diets are very efficient to control epilepsy and movement disorders. We tested a novel simple and rapid blood test in 30 patients with GLUT1-DS with predominant movement disorders, 18 patients with movement disorders attributed to other genetic defects, and 346 healthy controls. We detected significantly reduced GLUT1 expression only on red blood cells from patients with GLUT1-DS (23 patients; 78%), including patients with inconclusive genetic analysis. This test opens perspectives for the screening of GLUT1-DS in children and adults with cognitive impairment, movement disorder, or epilepsy. Ann Neurol 2017;82:133-138.
[Mh] Termos MeSH primário: Erros Inatos do Metabolismo dos Carboidratos/diagnóstico
Transportador de Glucose Tipo 1/biossíntese
Testes Hematológicos
Proteínas de Transporte de Monossacarídeos/deficiência
[Mh] Termos MeSH secundário: Adolescente
Adulto
Erros Inatos do Metabolismo dos Carboidratos/sangue
Estudos de Casos e Controles
Criança
Pré-Escolar
Feminino
Seres Humanos
Masculino
Meia-Idade
Proteínas de Transporte de Monossacarídeos/sangue
Transtornos dos Movimentos/sangue
Transtornos dos Movimentos/diagnóstico
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucose Transporter Type 1); 0 (Monosaccharide Transport Proteins); 0 (SLC2A1 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE
[do] DOI:10.1002/ana.24970


  9 / 9116 MEDLINE  
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[PMID]:28535336
[Au] Autor:Bhattacherjee A; Hrynets Y; Betti M
[Ad] Endereço:Department of Agricultural, Food and Nutritional Science, University of Alberta 410 Agriculture/Forestry Centre, Edmonton AB T6G 2P5, Canada.
[Ti] Título:Transport of the Glucosamine-Derived Browning Product Fructosazine (Polyhydroxyalkylpyrazine) Across the Human Intestinal Caco-2 Cell Monolayer: Role of the Hexose Transporters.
[So] Source:J Agric Food Chem;65(23):4642-4650, 2017 Jun 14.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The transport mechanism of fructosazine, a glucosamine self-condensation product, was investigated using a Caco-2 cell model. Fructosazine transport was assessed by measuring the bidirectional permeability coefficient across Caco-2 cells. The mechanism of transport was evaluated using phlorizin, an inhibitor of sodium-dependent glucose cotransporters (SGLT) 1 and 2, phloretin and quercetin, inhibitors of glucose transporters (GLUT) 1 and 2, transcytosis inhibitor wortmannin, and gap junction disruptor cytochalasin D. The role of hexose transporters was further studied using downregulated or overexpressed cell lines. The apparent permeability (P ) of fructosazine was 1.30 ± 0.02 × 10 cm/s. No significant (p > 0.05) effect was observed in fructosazine transport by adding wortmannin and cytochalasin D. The presence of phlorizin, phloretin, and quercetin decreased fructosazine transport. The downregulated GLUT cells line was unable to transport fructosazine. In human intestinal epithelial Caco-2 cells, GLUT1 or GLUT2 and SGLT are mainly responsible for fructosazine transport.
[Mh] Termos MeSH primário: Glucosamina/metabolismo
Intestinos/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Pirazinas/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Células CACO-2
Glucosamina/química
Glucose/metabolismo
Seres Humanos
Proteínas de Transporte de Monossacarídeos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Monosaccharide Transport Proteins); 0 (Pyrazines); 13121-64-7 (tagatosazine); IY9XDZ35W2 (Glucose); N08U5BOQ1K (Glucosamine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01611


  10 / 9116 MEDLINE  
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[PMID]:28511796
[Au] Autor:Hao GJ; Ding YH; Wen H; Li XF; Zhang W; Su HY; Liu DM; Xie NL
[Ad] Endereço:Department of Oncology, First Hospital of Yulin City, Yulin 719000, PR China.
[Ti] Título:Attenuation of deregulated miR-369-3p expression sensitizes non-small cell lung cancer cells to cisplatin via modulation of the nucleotide sugar transporter SLC35F5.
[So] Source:Biochem Biophys Res Commun;488(3):501-508, 2017 Jul 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Deregulation of the microRNAs (miRNAs), a cluster of important posttranscriptional regulators, has been frequently associated with lung cancer (LCa). However, the emerging mechanism for how miRNAs is linked causally in the development of LCa chemoresistance is poorly understood. Herein, we established for the time the up-regulation of miR-369-3p in cisplatin (DDP)-resistant nonsmall cell lung cancer (NSCLC) tissues and cells. Its deregulation was found to be correlated to the magnitude of malignancy in well-characterized LCa cells. Functionally, inhibition of miR-369-3p sensitized LCa cells to DDP and suppressed the invasive capability in the presence of DDP treatment, whereas miR-369-3p overexpression promoted DDP resistance and thereby enhanced LCa cells invasiveness. Mechanistically, bioinformatics coupled with luciferase and gain-of-function, loss-of-function assays revealed that miR-369-3p may regulate DDP chemoresistance by directly targeting the 3' untranslated region (UTR) of human solute carrier 35F5 (SLC35F5), as application of miR-369-3p inhibitors or reintroduction of epigenetically silenced SLC35F5 both individually sensitized LCa cells to DDP, but combined treatment with miR-369-3p inhibitors and SLC35F5 overexpression failed to sensitized LCa cells further to DDP-elicited cell death. Our results provide evidence that the oncomiR effect of miR-369-3p may be mediated through disrupting the nucleotide sugar transportation and that SLC35F5 is a key effector of this chemoresistance-promoting activity.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Carcinoma Pulmonar de Células não Pequenas/tratamento farmacológico
Carcinoma Pulmonar de Células não Pequenas/genética
Cisplatino/farmacologia
Neoplasias Pulmonares/tratamento farmacológico
MicroRNAs/genética
Proteínas de Transporte de Monossacarídeos/metabolismo
[Mh] Termos MeSH secundário: Carcinoma Pulmonar de Células não Pequenas/metabolismo
Carcinoma Pulmonar de Células não Pequenas/patologia
Perfilação da Expressão Gênica
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/metabolismo
Neoplasias Pulmonares/patologia
MicroRNAs/biossíntese
MicroRNAs/metabolismo
Proteínas de Transporte de Monossacarídeos/genética
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (MIRN369 microRNA, human); 0 (MicroRNAs); 0 (Monosaccharide Transport Proteins); 0 (SLC35F5 protein, human); Q20Q21Q62J (Cisplatin)
[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:170518
[St] Status:MEDLINE



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