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  1 / 8632 MEDLINE  
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[PMID]:28453664
[Au] Autor:Krag TO; Ruiz-Ruiz C; Vissing J
[Ad] Endereço:Copenhagen Neuromuscular Center, Department of Neurology, Rigshospitalet, University of Copenhagen, 2100 Copenhagen, Denmark.
[Ti] Título:Glycogen Synthesis in Glycogenin 1-Deficient Patients: A Role for Glycogenin 2 in Muscle.
[So] Source:J Clin Endocrinol Metab;102(8):2690-2700, 2017 Aug 01.
[Is] ISSN:1945-7197
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Context: Glycogen storage disease (GSD) type XV is a rare disease caused by mutations in the GYG1 gene that codes for the core molecule of muscle glycogen, glycogenin 1. Nonetheless, glycogen is present in muscles of glycogenin 1-deficient patients, suggesting an alternative for glycogen buildup. A likely candidate is glycogenin 2, an isoform expressed in the liver and heart but not in healthy skeletal muscle. Objective: We wanted to investigate the formation of glycogen and changes in glycogen metabolism in patients with GSD type XV. Design, Setting, and Patients: Two patients with mutations in the GYG1 gene were investigated for histopathology, ultrastructure, and expression of proteins involved in glycogen synthesis and metabolism. Results: Apart from occurrence of polyglucosan (PG) bodies in few fibers, glycogen appeared normal in most cells, and the concentration was normal in patients with GSD type XV. We found that glycogenin 1 was absent, but glycogenin 2 was present in the patients, whereas the opposite was the case in healthy controls. Electron microscopy revealed that glycogen was present between and not inside myofibrils in type II fibers, compromising the ultrastructure of these fibers, and only type I fibers contained PG bodies. We also found significant changes to the expression levels of several enzymes directly involved in glycogen and glucose metabolism. Conclusions: To our knowledge, this is the first report demonstrating expression of glycogenin 2 in glycogenin 1-deficient patients, suggesting that glycogenin 2 rescues the formation of glycogen in patients with glycogenin 1 deficiency.
[Mh] Termos MeSH primário: Glucosiltransferases/genética
Glucosiltransferases/metabolismo
Glicogênio/biossíntese
Glicoproteínas/genética
Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: Idoso
Metabolismo dos Carboidratos
Estudos de Casos e Controles
Feminino
Glucanos/metabolismo
Glucose/metabolismo
Glicogênio/metabolismo
Glicogênio/ultraestrutura
Doença de Depósito de Glicogênio/genética
Glicoproteínas/metabolismo
Seres Humanos
Microscopia Eletrônica
Meia-Idade
Fibras Musculares de Contração Rápida/ultraestrutura
Músculo Esquelético/patologia
Músculo Esquelético/ultraestrutura
Miofibrilas/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (Glycoproteins); 0 (glycogenin); 9005-79-2 (Glycogen); 9012-72-0 (polyglucosan); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.186 (GYG2 protein, human); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1210/jc.2017-00399


  2 / 8632 MEDLINE  
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[PMID]:29278771
[Au] Autor:Zou X; Zhen Z; Ge Q; Fan S; Liu A; Gong W; Li J; Gong J; Shi Y; Wang Y; Liu R; Duan L; Lei K; Zhang Q; Jiang X; Zhang S; Jia T; Zhang L; Shang H; Yuan Y
[Ad] Endereço:State Key Laboratory of Cotton Biology, Key Laboratory of Biological and Genetic Breeding of Cotton, The Ministry of Agriculture, Institute of Cotton Research, Chinese Academy of Agricultural Sciences, Anyang 455000, Henan, China.
[Ti] Título:Genome-wide identification and analysis of the evolution and expression patterns of the cellulose synthase gene superfamily in Gossypium species.
[So] Source:Gene;646:28-38, 2018 Mar 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The cellulose synthase gene superfamily, which includes the cellulose synthase (Ces) and cellulose synthase-like (Csl) families, is involved in the synthesis of cellulose and hemicellulose. This superfamily is critical for cotton fiber development in Gossypium species. Applying a series of bioinformatic methods, we identified 228 Ces/Csl genes from four Gossypium species (G. hirsutum, G. barbadense, G. arboreum, and G. raimondii). These genes were then grouped into 11 subfamilies based on phylogenetic relationships. A subsequent analysis of gene evolution revealed sites in CSLG and CSLJ genes that were under long-term positive selection pressure, with a posterior probability >0.95. Moreover, the d :d value for the CSLJ clade was 1.305, suggesting this subfamily was under positive selection pressure. Our data indicated that the d :d value ranged from 0.0084 to 0.9693 among the homologous Ces/Csl genes, implying they were under purifying selection pressure. Our transcriptome and qRT-PCR analyses revealed that CesA genes were more highly expressed in tetraploids than in diploids. However, the Csl expression levels exhibited the opposite trend. Furthermore, changes to promoter sequences may have influenced the expression of homologous Ces/Csl genes. Our findings may provide novel insights into the evolutionary relationships and expression patterns of the Ces/Csl genes in Gossypium species.
[Mh] Termos MeSH primário: Perfilação da Expressão Gênica/métodos
Glucosiltransferases/genética
Gossypium/crescimento & desenvolvimento
Família Multigênica
[Mh] Termos MeSH secundário: Mapeamento Cromossômico
Evolução Molecular
Regulação Enzimológica da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Gossypium/enzimologia
Gossypium/genética
Filogenia
Proteínas de Plantas/genética
Seleção Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (cellulose synthase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


  3 / 8632 MEDLINE  
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[PMID]:29240782
[Au] Autor:Mishra BP; Kumar R; Mohan A; Gill KS
[Ad] Endereço:Department of Agricultural Biotechnology and Molecular Biology, Dr. Rajendra Prasad Central Agricultural University, Pusa, Bihar, India.
[Ti] Título:Conservation and divergence of Starch Synthase III genes of monocots and dicots.
[So] Source:PLoS One;12(12):e0189303, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Starch Synthase (SS) plays an important role in extending the α-1,4 glucan chains during starch biosynthesis by catalyzing the transfer of the glucosyl moiety from ADP-glucose to the non-reducing end of a pre-existing glucan chain. SS has five distinct isoforms of which SSIII is involved in the formation of longer glucan chain length. Here we report identification and detailed characterization of 'true' orthologs of the well-characterized maize SSIII (ZmSSIII), among six monocots and two dicot species. ZmSSIII orthologs have nucleotide sequence similarity ranging from 56-81%. Variation in gene size among various orthologs ranged from 5.49 kb in Arabidopsis to 11.62 kb in Brachypodium and the variation was mainly due to intron size and indels present in the exons 1 and 3. Number of exons and introns were highly conserved among all orthologs however. While the intron number was conserved, intron phase showed variation at group, genera and species level except for intron 1 and 5. Several species, genera, and class specific cis-acting regulatory elements were identified in the promoter region. The predicted protein size of the SSIII orthologs ranged from 1094 amino acid (aa) in Arabidopsis to 1688 aa in Brachypodium with sequence identity ranging from 60%-89%. The N-terminal region of the protein was highly variable whereas the C-terminal region containing the Glycosyltransferase domain was conserved with >80% sequence similarity among the orthologs. In addition to confirming the known motifs, eleven novel motifs possibly providing species, genera and group specific functions, were identified in the three carbohydrate binding domains. Despite of significant sequence variation among orthologs, most of the motifs and their relative distances are highly conserved among the orthologs. The 3-D structure of catalytic region of SSIII orthologs superimposed with higher confidence confirming the presence of similar binding sites with five unidentified conserved regions in the catalytic (glycosyltransferase) domain including the pockets involved in catalysis and binding of ligands. Homeologs of wheat SSIII gene showed tissue and developmental stage specific expression pattern with the highest expression recorded in developing grains.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Brachypodium/genética
Genes de Plantas
Glucosiltransferases/genética
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Brachypodium/enzimologia
Domínio Catalítico
Éxons
Íntrons
Filogenia
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (starch synthase III, Arabidopsis)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189303


  4 / 8632 MEDLINE  
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[PMID]:28465351
[Au] Autor:Morimoto A; Kannari M; Tsuchida Y; Sasaki S; Saito C; Matsuta T; Maeda T; Akiyama M; Nakamura T; Sakaguchi M; Nameki N; Gonzalez FJ; Inoue Y
[Ad] Endereço:From the Laboratory of Molecular Life Science, Division of Molecular Science, Faculty of Science and Technology, Gunma University, Kiryu, Gunma 376-8515, Japan.
[Ti] Título:An HNF4α-microRNA-194/192 signaling axis maintains hepatic cell function.
[So] Source:J Biol Chem;292(25):10574-10585, 2017 06 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatocyte nuclear factor 4α (HNF4α) controls the expression of liver-specific protein-coding genes. However, some microRNAs are also modulated by HNF4α, and it is not known whether they are direct targets of HNF4α and whether they influence hepatic function. In this study, we found that HNF4α regulates microRNAs, indicated by marked down-regulation of miR-194 and miR-192 (miR-194/192) in liver-specific -null ( ) mice. Transactivation of the shared miR-194/192 promoter was dependent on HNF4α expression, indicating that miR-194/192 is a target gene of HNF4α. Screening of potential mRNAs targeted by miR-194/192 revealed that expression of genes involved in glucose metabolism (glycogenin 1 ( )), cell adhesion and migration (activated leukocyte cell adhesion molecule ( )), tumorigenesis and tumor progression ( and epiregulin ( )), protein SUMOylation ( ), epigenetic regulation ( and Cullin 4B ( )), and the epithelial-mesenchymal transition (moesin ( )) was up-regulated in mice. Moreover, we also found that miR-194/192 binds the 3'-UTR of these mRNAs. siRNA knockdown of HNF4α suppressed miR-194/192 expression in human hepatocellular carcinoma (HCC) cells and resulted in up-regulation of their mRNA targets. Inhibition and overexpression experiments with miR-194/192 revealed that , , , , and are miR-194 targets, whereas , , and are miR-192 targets. These findings reveal a novel HNF4α network controlled by miR-194/192 that may play a critical role in maintaining the hepatocyte-differentiated state by inhibiting expression of genes involved in dedifferentiation and tumorigenesis. These insights may contribute to the development of diagnostic markers for early HCC detection, and targeting of the miR-194/192 pathway could be useful for managing HCC.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/fisiologia
Fator 4 Nuclear de Hepatócito/metabolismo
Hepatócitos/metabolismo
MicroRNAs/metabolismo
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas/fisiologia
Molécula de Adesão de Leucócito Ativado/biossíntese
Molécula de Adesão de Leucócito Ativado/genética
Animais
Transformação Celular Neoplásica/genética
Transformação Celular Neoplásica/metabolismo
Epirregulina/biossíntese
Epirregulina/genética
Glucosiltransferases/biossíntese
Glucosiltransferases/genética
Glicoproteínas/biossíntese
Glicoproteínas/genética
Fator 4 Nuclear de Hepatócito/genética
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/metabolismo
Camundongos
Camundongos Mutantes
MicroRNAs/genética
Proteínas dos Microfilamentos/biossíntese
Proteínas dos Microfilamentos/genética
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/biossíntese
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Activated-Leukocyte Cell Adhesion Molecule); 0 (Epiregulin); 0 (Ereg protein, mouse); 0 (Glycoproteins); 0 (Hepatocyte Nuclear Factor 4); 0 (Hnf4a protein, mouse); 0 (MIRN194 microRNA, mouse); 0 (MicroRNAs); 0 (Microfilament Proteins); 0 (Mirn192 microRNA, mouse); 0 (SUMO2 protein, mouse); 0 (Small Ubiquitin-Related Modifier Proteins); 0 (glycogenin); 144131-77-1 (moesin); EC 2.4.1.- (Glucosyltransferases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785592


  5 / 8632 MEDLINE  
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[PMID]:27775150
[Au] Autor:Schmölzer K; Lemmerer M; Gutmann A; Nidetzky B
[Ad] Endereço:Austrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
[Ti] Título:Integrated process design for biocatalytic synthesis by a Leloir Glycosyltransferase: UDP-glucose production with sucrose synthase.
[So] Source:Biotechnol Bioeng;114(4):924-928, 2017 04.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nucleotide sugar-dependent ("Leloir") glycosyltransferases (GTs), represent a new paradigm for the application of biocatalytic glycosylations to the production of fine chemicals. However, it remains to be shown that GT processes meet the high efficiency targets of industrial biotransformations. We demonstrate in this study of uridine-5'-diphosphate glucose (UDP-glc) production by sucrose synthase (from Acidithiobacillus caldus) that a holistic process design, involving coordinated development of biocatalyst production, biotransformation, and downstream processing (DSP) was vital for target achievement at ∼100 g scale synthesis. Constitutive expression in Escherichia coli shifted the recombinant protein production mainly to the stationary phase and enhanced the specific enzyme activity to a level (∼480 U/g ) suitable for whole-cell biotransformation. The UDP-glc production had excellent performance metrics of ∼100 g /L, 86% yield (based on UDP), and a total turnover number of 103 g /g at a space-time yield of 10 g/L/h. Using efficient chromatography-free DSP, the UDP-glc was isolated in a single batch with ≥90% purity and in 73% isolated yield. Overall, the process would allow production of ∼0.7 kg of isolated product/L E. coli bioreactor culture, thus demonstrating how integrated process design promotes the practical use of a GT conversion. Biotechnol. Bioeng. 2017;114: 924-928. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Glucosiltransferases/metabolismo
Glicosiltransferases/metabolismo
Uridina Difosfato Glucose/análise
Uridina Difosfato Glucose/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Escherichia coli/metabolismo
Glicosilação
Nucleotídeos
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Nucleotides); 0 (Recombinant Proteins); EC 2.4.- (Glycosyltransferases); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.13 (sucrose synthase); V50K1D7P4Y (Uridine Diphosphate Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171216
[Lr] Data última revisão:
171216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26204


  6 / 8632 MEDLINE  
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[PMID]:29036229
[Au] Autor:Wang J; Du J; Mu X; Wang P
[Ad] Endereço:Department of Pomology, College of Horticulture, Shanxi Agricultural University, Taigu, China.
[Ti] Título:Cloning and characterization of the Cerasus humilis sucrose phosphate synthase gene (ChSPS1).
[So] Source:PLoS One;12(10):e0186650, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sucrose is crucial to the growth and development of plants, and sucrose phosphate synthase (SPS) plays a key role in sucrose synthesis. To understand the genetic and molecular mechanisms of sucrose synthesis in Cerasus humilis, ChSPS1, a homologue of SPS, was cloned using RT-PCR. Sequence analysis showed that the open reading frame (ORF) sequence of ChSPS1 is 3174 bp in length, encoding a predicted protein of 1057 amino acids. The predicted protein showed a high degree of sequence identity with SPS homologues from other species. Real-time RT-PCR analysis showed that ChSPS1 mRNA was detected in all tissues and the transcription level was the highest in mature fruit. There is a significant positive correlation between expression of ChSPS1 and sucrose content. Prokaryotic expression of ChSPS1 indicated that ChSPS1 protein was expressed in E. coli and it had the SPS activity. Overexpression of ChSPS1 in tobacco led to upregulation of enzyme activity and increased sucrose contents in transgenic plants. Real-time RT-PCR analysis showed that the expression of ChSPS1 in transgenic tobacco was significantly higher than in wild type plants. These results suggested that ChSPS1 plays an important role in sucrose synthesis in Cerasus humilis.
[Mh] Termos MeSH primário: Glucosiltransferases/genética
Prunus/enzimologia
Prunus/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Clonagem Molecular
Regulação da Expressão Gênica de Plantas
Glucosiltransferases/química
Glucosiltransferases/metabolismo
Análise de Sequência
Sacarose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
57-50-1 (Sucrose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.14 (sucrose-phosphate synthase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186650


  7 / 8632 MEDLINE  
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[PMID]:28951248
[Au] Autor:Li R; Zhu LN; Ren LQ; Weng JY; Sun JS
[Ad] Endereço:Tianjin Key Laboratory of Animal and Plant Resistance, College of Life Science, Tianjin Normal University, Tianjin, People's Republic of China.
[Ti] Título:Molecular cloning and characterization of glycogen synthase in Eriocheir sinensis.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;214:47-56, 2017 Dec.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycogen plays an important role in glucose and energy homeostasis at cellular and organismal levels. In glycogen synthesis, glycogen synthase (GS) is a rate-limiting enzyme catalysing the addition of α-1,4-linked glucose units from (UDP) -glucose to a nascent glycogen chain using glycogenin (GN) as a primer. While studies on mammalian liver GS (GYS2) are numerous, enzymes from crustaceans, which also use glycogen and glucose as their main energy source, have received less attention. In the present study, we amplified full-length GS cDNA from Eriocheir sinensis. Tissue expression profiling revealed the highest expression of GS in the hepatopancreas. During moulting, GS expression and activity declined, and glycogen levels in the hepatopancreas were reduced. Recombinant GS was expressed in Escherichia coli Rosetta (DE3), and induction at 37°C or 16°C yielded EsGS in insoluble inclusion bodies (EsGS-I) or in soluble form (EsGS-S), respectively. Enzyme activity was measured in a cell-free system containing glucose-6-phosphate (G6P), and both forms possessed glycosyltransferase activity, but refolded EsGS-I was more active. Enzyme activity of both GS and EsGS-I in the hepatopancreas was optimum at 25°C, which is coincident with the optimum growth temperature of Chinese mitten crab, and higher (37°C) or lower (16°C) temperatures resulted in lower enzyme activity. Taken together, the results suggest that GS may be important for maintaining normal physiological functions such as growth and reproduction.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/genética
Braquiúros/enzimologia
Glicogênio Sintase/genética
Glicogênio/biossíntese
Hepatopâncreas/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas de Artrópodes/metabolismo
Sítios de Ligação
Braquiúros/genética
Braquiúros/crescimento & desenvolvimento
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glucose-6-Fosfato/metabolismo
Glucosiltransferases/metabolismo
Glicogênio Sintase/metabolismo
Glicoproteínas/metabolismo
Hepatopâncreas/crescimento & desenvolvimento
Corpos de Inclusão/química
Cinética
Muda/genética
Especificidade de Órgãos
Filogenia
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Glycoproteins); 0 (Recombinant Proteins); 0 (glycogenin); 56-73-5 (Glucose-6-Phosphate); 9005-79-2 (Glycogen); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.11 (Glycogen Synthase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE


  8 / 8632 MEDLINE  
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[PMID]:28926587
[Au] Autor:Weh E; Takeuchi H; Muheisen S; Haltiwanger RS; Semina EV
[Ad] Endereço:Department of Pediatrics and Children's Research Institute at the Medical College of Wisconsin, Milwaukee, Wisconsin, United States of America.
[Ti] Título:Functional characterization of zebrafish orthologs of the human Beta 3-Glucosyltransferase B3GLCT gene mutated in Peters Plus Syndrome.
[So] Source:PLoS One;12(9):e0184903, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Peters Plus Syndrome (PPS) is a rare autosomal recessive disease characterized by ocular defects, short stature, brachydactyly, characteristic facial features, developmental delay and other highly variable systemic defects. Classic PPS is caused by loss-of-function mutations in the B3GLCT gene encoding for a ß3-glucosyltransferase that catalyzes the attachment of glucose via a ß1-3 glycosidic linkage to O-linked fucose on thrombospondin type 1 repeats (TSRs). B3GLCT was shown to participate in a non-canonical ER quality control mechanism; however, the exact molecular processes affected in PPS are not well understood. Here we report the identification and characterization of two zebrafish orthologs of the human B3GLCT gene, b3glcta and b3glctb. The b3glcta and b3glctb genes encode for 496-aa and 493-aa proteins with 65% and 57% identity to human B3GLCT, respectively. Expression studies demonstrate that both orthologs are widely expressed with strong presence in embryonic tissues affected in PPS. In vitro glucosylation assays demonstrated that extracts from wildtype embryos contain active b3glct enzyme capable of transferring glucose from UDP-glucose to an O-fucosylated TSR, indicating functional conservation with human B3GLCT. To determine the developmental role of the zebrafish genes, single and double b3glct knockouts were generated using TALEN-induced genome editing. Extracts from double homozygous b3glct-/- embryos demonstrated complete loss of in vitro b3glct activity. Surprisingly, b3glct-/- homozygous fish developed normally. Transcriptome analyses of head and trunk tissues of b3glct-/- 24-hpf embryos identified 483 shared differentially regulated transcripts that may be involved in compensation for b3glct function in these embryos. The presented data show that both sequence and function of B3GLCT/b3glct genes is conserved in vertebrates. At the same time, complete b3glct deficiency in zebrafish appears to be inconsequential and possibly compensated for by a yet unknown mechanism.
[Mh] Termos MeSH primário: Glucosiltransferases/metabolismo
Proteínas de Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Fenda Labial/genética
Fenda Labial/patologia
Córnea/anormalidades
Córnea/patologia
Embrião não Mamífero/metabolismo
Edição de Genes
Perfilação da Expressão Gênica
Técnicas de Inativação de Genes
Glucosiltransferases/deficiência
Glucosiltransferases/genética
Transtornos do Crescimento/genética
Transtornos do Crescimento/patologia
Seres Humanos
Hibridização In Situ
Deformidades Congênitas dos Membros/genética
Deformidades Congênitas dos Membros/patologia
Dados de Sequência Molecular
Mutação
Alinhamento de Sequência
Nucleases dos Efetores Semelhantes a Ativadores de Transcrição/genética
Peixe-Zebra
Proteínas de Peixe-Zebra/deficiência
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Zebrafish Proteins); EC 2.4.1.- (1,3-alpha-D-glucan synthase); EC 2.4.1.- (Glucosyltransferases); EC 3.1.- (Transcription Activator-Like Effector Nucleases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184903


  9 / 8632 MEDLINE  
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[PMID]:28878084
[Au] Autor:Chen D; Xiang Q; Nicholas J
[Ad] Endereço:Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
[Ti] Título:Human Herpesvirus 8 Interleukin-6 Interacts with Calnexin Cycle Components and Promotes Protein Folding.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Viral interleukin-6 (vIL-6) encoded by human herpesvirus 8 (HHV-8) is believed to contribute via mitogenic, survival, and angiogenic activities to HHV-8-associated Kaposi's sarcoma, primary effusion lymphoma (PEL), and multicentric Castleman's disease through autocrine or paracrine mechanisms during latency or productive replication. There is direct evidence that vIL-6 promotes latently infected PEL cell viability and proliferation and also viral productive replication in PEL and endothelial cells. These activities are mediated largely through endoplasmic reticulum (ER)-localized vIL-6, which can induce signal transduction via the gp130 signaling receptor, activating mitogen-activated protein kinase and signal transducer and activator of transcription signaling, and interactions of vIL-6 with the ER membrane protein vitamin K epoxide reductase complex subunit 1 variant 2 (VKORC1v2). The latter functional axis involves suppression of proapoptotic lysosomal protein cathepsin D by promotion of the ER-associated degradation of ER-transiting, preproteolytically processed procathepsin D. Other interactions of VKORC1v2 and activities of vIL-6 via the receptor have not been reported. We show here that both vIL-6 and VKORC1v2 interact with calnexin cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), which catalyzes monoglucosylation of N-glycans, and oppositely acting glucosidase II (GlucII), and that vIL-6 can promote protein folding. This activity was found to require VKORC1v2 and UGGT1, to involve vIL-6 associations with VKORC1v2, UGGT1, and GlucII, and to operate in the context of productively infected cells. These findings document new VKORC1v2-associated interactions and activities of vIL-6, revealing novel mechanisms of vIL-6 function within the ER compartment. HHV-8 vIL-6 prosurvival (latent) and proreplication functions are mediated from the ER compartment through both gp130 receptor-mediated signal transduction and interaction of vIL-6 with the ER membrane protein VKORC1v2. This report identifies interactions of vIL-6 and VKORC1v2 with calnexin cycle enzymes GlucII and UGGT1, which are involved in glycan processing and nascent protein folding. The presented data show that vIL-6 and VKORC1v2 can cocomplex with GlucII and UGGT1, that vIL-6 promotes protein folding, and that VKORC1v2, UGGT1, and vIL-6 interactions with GlucII and UGGT1 are important for the profolding activity of vIL-6, which can be detected in the context of infected cells. This newly identified ER activity of vIL-6 involving VKORC1v2 may promote viral latency (in PEL cells) and productive replication by limiting the damaging effects of unfolded protein response signaling in addition to enhancing viral protein folding. This is the first report of such a function for a cytokine.
[Mh] Termos MeSH primário: Retículo Endoplasmático/metabolismo
Glucosiltransferases/metabolismo
Herpesvirus Humano 8/metabolismo
Interleucina-6/metabolismo
Sarcoma de Kaposi/metabolismo
Proteínas Virais/metabolismo
Vitamina K Epóxido Redutases/metabolismo
[Mh] Termos MeSH secundário: Receptor gp130 de Citocina/genética
Receptor gp130 de Citocina/metabolismo
Retículo Endoplasmático/genética
Retículo Endoplasmático/virologia
Glucosiltransferases/genética
Células HEK293
Herpesvirus Humano 8/genética
Seres Humanos
Interleucina-6/genética
Dobramento de Proteína
Sarcoma de Kaposi/genética
Proteínas Virais/genética
Vitamina K Epóxido Redutases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-6); 0 (Viral Proteins); 133483-10-0 (Cytokine Receptor gp130); EC 1.17.4.4 (VKORC1 protein, human); EC 1.17.4.4 (Vitamin K Epoxide Reductases); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (UGGT1 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE


  10 / 8632 MEDLINE  
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[PMID]:28842504
[Au] Autor:Gupta P; Zhang Z; Sugiman-Marangos SN; Tam J; Raman S; Julien JP; Kroh HK; Lacy DB; Murgolo N; Bekkari K; Therien AG; Hernandez LD; Melnyk RA
[Ad] Endereço:From Merck & Co., Inc., Kenilworth, New Jersey 07033.
[Ti] Título:Functional defects in TcdB toxin uptake identify CSPG4 receptor-binding determinants.
[So] Source:J Biol Chem;292(42):17290-17301, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is a major nosocomial pathogen that produces two exotoxins, TcdA and TcdB, with TcdB thought to be the primary determinant in human disease. TcdA and TcdB are large, multidomain proteins, each harboring a cytotoxic glucosyltransferase domain that is delivered into the cytosol from endosomes via a translocation domain after receptor-mediated endocytosis of toxins from the cell surface. Although there are currently no known host cell receptors for TcdA, three cell-surface receptors for TcdB have been identified: CSPG4, NECTIN3, and FZD1/2/7. The sites on TcdB that mediate binding to each receptor are not defined. Furthermore, it is not known whether the combined repetitive oligopeptide (CROP) domain is involved in or required for receptor binding. Here, in a screen designed to identify sites in TcdB that are essential for target cell intoxication, we identified a region at the junction of the translocation and the CROP domains that is implicated in CSPG4 binding. Using a series of C-terminal truncations, we show that the CSPG4-binding site on TcdB extends into the CROP domain, requiring three short repeats for binding and for full toxicity on CSPG4-expressing cells. Consistent with the location of the CSPG4-binding site on TcdB, we show that the anti-TcdB antibody bezlotoxumab, which binds partially within the first three short repeats, prevents CSPG4 binding to TcdB. In addition to establishing the binding region for CSPG4, this work ascribes for the first time a role in TcdB CROPs in receptor binding and further clarifies the relative roles of host receptors in TcdB pathogenesis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/metabolismo
Proteoglicanas de Sulfatos de Condroitina/metabolismo
Clostridium difficile/enzimologia
Glucosiltransferases/metabolismo
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/química
Anticorpos Neutralizantes/química
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/genética
Toxinas Bacterianas/antagonistas & inibidores
Toxinas Bacterianas/genética
Células CHO
Células CACO-2
Cercopithecus aethiops
Proteoglicanas de Sulfatos de Condroitina/genética
Clostridium difficile/genética
Clostridium difficile/patogenicidade
Cricetinae
Cricetulus
Glucosiltransferases/antagonistas & inibidores
Glucosiltransferases/genética
Células HEK293
Seres Humanos
Proteínas de Membrana/genética
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (CSPG4 protein, human); 0 (Chondroitin Sulfate Proteoglycans); 0 (Membrane Proteins); 0 (bezlotoxumab); 0 (toxB protein, Clostridium difficile); EC 2.4.1.- (Glucosyltransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.806687



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