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Pesquisa : D09.067.342.531.050 [Categoria DeCS]
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[PMID]:29335469
[Au] Autor:Aunkham A; Zahn M; Kesireddy A; Pothula KR; Schulte A; Baslé A; Kleinekathöfer U; Suginta W; van den Berg B
[Ad] Endereço:Biochemistry-Electrochemistry Research Unit, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
[Ti] Título:Structural basis for chitin acquisition by marine Vibrio species.
[So] Source:Nat Commun;9(1):220, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chitin, an insoluble polymer of N-acetylglucosamine, is one of the most abundant biopolymers on Earth. By degrading chitin, chitinolytic bacteria such as Vibrio harveyi are critical for chitin recycling and maintenance of carbon and nitrogen cycles in the world's oceans. A decisive step in chitin degradation is the uptake of chito-oligosaccharides by an outer membrane protein channel named chitoporin (ChiP). Here, we report X-ray crystal structures of ChiP from V. harveyi in the presence and absence of chito-oligosaccharides. Structures without bound sugar reveal a trimeric assembly with an unprecedented closing of the transport pore by the N-terminus of a neighboring subunit. Substrate binding ejects the pore plug to open the transport channel. Together with molecular dynamics simulations, electrophysiology and in vitro transport assays our data provide an explanation for the exceptional affinity of ChiP for chito-oligosaccharides and point to an important role of the N-terminal gate in substrate transport.
[Mh] Termos MeSH primário: Carbono/metabolismo
Quitina/metabolismo
Nitrogênio/metabolismo
Vibrio/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Proteínas da Membrana Bacteriana Externa/química
Proteínas da Membrana Bacteriana Externa/genética
Proteínas da Membrana Bacteriana Externa/metabolismo
Ciclo do Carbono
Cristalografia por Raios X
Modelos Moleculares
Ciclo do Nitrogênio
Oceanos e Mares
Oligossacarídeos/metabolismo
Porinas/química
Porinas/genética
Porinas/metabolismo
Conformação Proteica
Água do Mar/química
Água do Mar/microbiologia
Vibrio/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Oligosaccharides); 0 (Porins); 1398-61-4 (Chitin); 7440-44-0 (Carbon); N762921K75 (Nitrogen); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02523-y


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[PMID]:28742884
[Au] Autor:Borzym-Kluczyk M; Radziejewska I; Cechowska-Pasko M; Darewicz B
[Ad] Endereço:Department of Pharmaceutical Biochemistry, Medical University of Bialystok, Bialystok, Poland.
[Ti] Título:Reduced expression of E-cadherin and increased sialylation level in clear cell renal cell carcinoma.
[So] Source:Acta Biochim Pol;64(3):465-470, 2017.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Cancer cells are characterized by an aberrant increase in protein N-glycosylation and by disruption of E-cadherin-mediated adherens junctions. However, the relationship between alterations in N-glycosylation process and loss of E-cadherin adhesion in cancer remains unclear. The mechanisms of altered expression of adhesive glycoproteins in cancer cells have not been fully elucidated. Thus, the aim of this study was to examine the expression of E-cadherin and sialyl Lewis / , NeuAcα2-3Gal, NeuAcα2-6Gal/GalNAc structures in the normal renal tissue and intermediate and cancerous tissues from patients with clear cell RCC. Moreover, we attempted to correlate the E-cadherin expression with some specific sugar residues of renal cancer tissue glycoproteins. The expression of E-cadherin was analysed using ELISA test and immunoblotting. Oligosaccharide structures and sialylation level were detected with ELISA test using specific biotinylated lectins or antibodies. A significant decrease of E-cadherin expression as well as a significant increase in sialylated oligosaccharides level in intermediate zone and renal cancer tissue in comparison to normal renal tissue are reported. Significant decrease in expression of cadherins and increase in sialylation of oligosaccharide structures in renal cancer tissue in comparison to normal renal tissue, and in renal cancer tissue in comparison to intermediate zone of renal tissue, are important for the future research concerning detection and quantification of cadherins and sialylated oligosaccharide structures in urine and cells of urinary sediment as possible non-invasive marker of early RCC.
[Mh] Termos MeSH primário: Caderinas/metabolismo
Carcinoma de Células Renais/metabolismo
Neoplasias Renais/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Idoso
Carcinoma de Células Renais/patologia
Feminino
Glicoconjugados/metabolismo
Glicoproteínas/metabolismo
Seres Humanos
Rim/metabolismo
Neoplasias Renais/patologia
Antígeno Lewis X/metabolismo
Masculino
Meia-Idade
Valores de Referência
Ácidos Siálicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDH1 protein, human); 0 (Cadherins); 0 (Glycoconjugates); 0 (Glycoproteins); 0 (Lewis X Antigen); 0 (Sialic Acids); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2015_1215


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[PMID]:29196265
[Au] Autor:Inoue Y; Moriwaki K; Ueda Y; Takeuchi T; Higuchi K; Asahi M
[Ad] Endereço:Department of Internal Medicine II, Faculty of Medicine, Osaka Medical College, Osaka 569-8686, Japan.
[Ti] Título:Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3ß inactivation in a human gastric carcinoma cell line, MKN45 cells.
[So] Source:Biochem Biophys Res Commun;495(2):1681-1687, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling. Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients. However, the role of O-GlcNAcylation in tumor progression is not fully elucidated. Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors. Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated. To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells. As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment. However, the O-GlcNAcylation was not detected on FOXM1 but not on GSK-3ß. High glucose and TMG treatment increased phospho-serine 9 GSK-3ß, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3ß inhibitors in MKN45 cells. Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3ß inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
[Mh] Termos MeSH primário: Proteína Forkhead Box M1/metabolismo
Glicogênio Sintase Quinase 3 beta/metabolismo
Neoplasias Gástricas/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Acilação
Linhagem Celular Tumoral
Proliferação Celular
Complicações do Diabetes/etiologia
Complicações do Diabetes/metabolismo
Complicações do Diabetes/patologia
Inibidores Enzimáticos/farmacologia
Proteína Forkhead Box M1/química
Glucose/metabolismo
Glicogênio Sintase Quinase 3 beta/antagonistas & inibidores
Glicogênio Sintase Quinase 3 beta/química
Seres Humanos
Processamento de Proteína Pós-Traducional
Estabilidade Proteica/efeitos dos fármacos
Proteólise/efeitos dos fármacos
Piranos/farmacologia
Neoplasias Gástricas/etiologia
Neoplasias Gástricas/patologia
Tiazóis/farmacologia
Ubiquitinação/efeitos dos fármacos
Regulação para Cima/efeitos dos fármacos
beta-N-Acetil-Hexosaminidases/antagonistas & inibidores
beta-N-Acetil-Hexosaminidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (FOXM1 protein, human); 0 (Forkhead Box Protein M1); 0 (Pyrans); 0 (Thiazoles); 0 (thiamet G); EC 2.7.11.1 (GSK3B protein, human); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta); EC 3.2.1.50 (hexosaminidase C); EC 3.2.1.52 (beta-N-Acetylhexosaminidases); IY9XDZ35W2 (Glucose); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE


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[PMID]:29371602
[Au] Autor:Gélinas R; Mailleux F; Dontaine J; Bultot L; Demeulder B; Ginion A; Daskalopoulos EP; Esfahani H; Dubois-Deruy E; Lauzier B; Gauthier C; Olson AK; Bouchard B; Des Rosiers C; Viollet B; Sakamoto K; Balligand JL; Vanoverschelde JL; Beauloye C; Horman S; Bertrand L
[Ad] Endereço:Pole of Cardiovascular Research, Institut de Recherche Expérimentale et Clinique, Université catholique de Louvain, Brussels, 1200, Belgium.
[Ti] Título:AMPK activation counteracts cardiac hypertrophy by reducing O-GlcNAcylation.
[So] Source:Nat Commun;9(1):374, 2018 01 25.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AMP-activated protein kinase (AMPK) has been shown to inhibit cardiac hypertrophy. Here, we show that submaximal AMPK activation blocks cardiomyocyte hypertrophy without affecting downstream targets previously suggested to be involved, such as p70 ribosomal S6 protein kinase, calcineurin/nuclear factor of activated T cells (NFAT) and extracellular signal-regulated kinases. Instead, cardiomyocyte hypertrophy is accompanied by increased protein O-GlcNAcylation, which is reversed by AMPK activation. Decreasing O-GlcNAcylation by inhibitors of the glutamine:fructose-6-phosphate aminotransferase (GFAT), blocks cardiomyocyte hypertrophy, mimicking AMPK activation. Conversely, O-GlcNAcylation-inducing agents counteract the anti-hypertrophic effect of AMPK. In vivo, AMPK activation prevents myocardial hypertrophy and the concomitant rise of O-GlcNAcylation in wild-type but not in AMPKα2-deficient mice. Treatment of wild-type mice with O-GlcNAcylation-inducing agents reverses AMPK action. Finally, we demonstrate that AMPK inhibits O-GlcNAcylation by mainly controlling GFAT phosphorylation, thereby reducing O-GlcNAcylation of proteins such as troponin T. We conclude that AMPK activation prevents cardiac hypertrophy predominantly by inhibiting O-GlcNAcylation.
[Mh] Termos MeSH primário: Proteínas Quinases Ativadas por AMP/genética
Acetilglucosamina/metabolismo
Cardiomegalia/genética
Miocárdio/metabolismo
Miócitos Cardíacos/metabolismo
Transferases de Grupos Nitrogenados/genética
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/deficiência
Acetilglucosamina/farmacologia
Acilação/efeitos dos fármacos
Animais
Animais Recém-Nascidos
Azasserina/farmacologia
Compostos Azo/farmacologia
Cardiomegalia/metabolismo
Cardiomegalia/patologia
Ativação Enzimática/efeitos dos fármacos
Ativadores de Enzimas/farmacologia
Regulação da Expressão Gênica
Glicosilação/efeitos dos fármacos
Ventrículos do Coração/efeitos dos fármacos
Ventrículos do Coração/metabolismo
Ventrículos do Coração/patologia
Masculino
Camundongos
Camundongos Knockout
Miocárdio/patologia
Miócitos Cardíacos/efeitos dos fármacos
Miócitos Cardíacos/patologia
Transferases de Grupos Nitrogenados/antagonistas & inibidores
Transferases de Grupos Nitrogenados/metabolismo
Norleucina/análogos & derivados
Norleucina/farmacologia
Fosforilação/efeitos dos fármacos
Cultura Primária de Células
Pironas/farmacologia
Ratos
Ratos Wistar
Transdução de Sinais
Tiofenos/farmacologia
Troponina T/genética
Troponina T/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (6-diazo-5-oxonorleucine); 0 (A 769662); 0 (Azo Compounds); 0 (Enzyme Activators); 0 (Pyrones); 0 (Thiophenes); 0 (Troponin T); 832C8OV84S (Norleucine); 87299V3Q9W (Azaserine); EC 2.6.- (Nitrogenous Group Transferases); EC 2.6.1.16 (Gfpt1 protein, mouse); EC 2.7.11.1 (AMPK alpha2 subunit, mouse); EC 2.7.11.31 (AMP-Activated Protein Kinases); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02795-4


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[PMID]:29320565
[Au] Autor:Brauge T; Faille C; Sadovskaya I; Charbit A; Benezech T; Shen Y; Loessner MJ; Bautista JR; Midelet-Bourdin G
[Ad] Endereço:ANSES, Laboratory for food safety, Boulogne sur Mer, France.
[Ti] Título:The absence of N-acetylglucosamine in wall teichoic acids of Listeria monocytogenes modifies biofilm architecture and tolerance to rinsing and cleaning procedures.
[So] Source:PLoS One;13(1):e0190879, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The wall teichoic acid (WTA) is the major carbohydrate found within the extracellular matrix of the Listeria monocytogenes biofilm. We first addressed the frequency of spontaneous mutations in two genes (lmo2549 and lmo2550) responsible for the GlcNAcylation in 93 serotype 1/2a strains that were mainly isolated from seafood industries. We studied the impact of mutations in lmo2549 or lmo2550 genes on biofilm formation by using one mutant carrying a natural mutation inactivating the lmo2550 gene (DSS 1130 BFA2 strain) and two EGD-e mutants that lack respective genes by in-frame deletion of lmo2549 or lmo2550 using splicing-by-overlap-extension PCR, followed by allelic exchange mutagenesis. The lmo2550 gene mutation, occurring in around 50% isolates, caused a decrease in bacterial adhesion to stainless steel compared to wild-type EGD-e strain during the adhesion step. On the other hand, bacterial population weren't significantly different after 24h-biofilm formation. The biofilm architecture was different between the wild-type strain and the two mutants inactivated for lmo2549 or lmo2550 genes respectively with the presence of bacterial micro-colonies for mutants which were not observed in the wild-type EGD-e strain biofilm. These differences might account for the stronger hydrophilic surface exhibited by the mutant cells. Upon a water flow or to a cleaning procedure at a shear stress of 0.16 Pa, the mutant biofilms showed the higher detachment rate compared to wild-type strain. Meanwhile, an increase in the amount of residual viable but non-culturable population on stainless steel was recorded in two mutants. Our data suggests that the GlcNAc residue of WTA played a role in adhesion and biofilm formation of Listeria monocyctogenes.
[Mh] Termos MeSH primário: Acetilglucosamina/metabolismo
Aderência Bacteriana/fisiologia
Biofilmes
Parede Celular/metabolismo
Listeria monocytogenes/fisiologia
Ácidos Teicoicos/metabolismo
[Mh] Termos MeSH secundário: Aderência Bacteriana/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Parede Celular/genética
Parede Celular/ultraestrutura
Interações Hidrofóbicas e Hidrofílicas
Listeria monocytogenes/genética
Listeria monocytogenes/ultraestrutura
Microscopia Eletrônica de Transmissão
Mutação
Fenótipo
Aço Inoxidável
Estresse Mecânico
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Teichoic Acids); 059QF0KO0R (Water); 12597-68-1 (Stainless Steel); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190879


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[PMID]:29211815
[Au] Autor:Berger AK; Yi H; Kearns DB; Mainou BA
[Ad] Endereço:Department of Pediatrics, Emory University School of Medicine, Atlanta, Georgia, United States of America.
[Ti] Título:Bacteria and bacterial envelope components enhance mammalian reovirus thermostability.
[So] Source:PLoS Pathog;13(12):e1006768, 2017 Dec.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enteric viruses encounter diverse environments as they migrate through the gastrointestinal tract to infect their hosts. The interaction of eukaryotic viruses with members of the host microbiota can greatly impact various aspects of virus biology, including the efficiency with which viruses can infect their hosts. Mammalian orthoreovirus, a human enteric virus that infects most humans during childhood, is negatively affected by antibiotic treatment prior to infection. However, it is not known how components of the host microbiota affect reovirus infectivity. In this study, we show that reovirus virions directly interact with Gram positive and Gram negative bacteria. Reovirus interaction with bacterial cells conveys enhanced virion thermostability that translates into enhanced attachment and infection of cells following an environmental insult. Enhanced virion thermostability was also conveyed by bacterial envelope components lipopolysaccharide (LPS) and peptidoglycan (PG). Lipoteichoic acid and N-acetylglucosamine-containing polysaccharides enhanced virion stability in a serotype-dependent manner. LPS and PG also enhanced the thermostability of an intermediate reovirus particle (ISVP) that is associated with primary infection in the gut. Although LPS and PG alter reovirus thermostability, these bacterial envelope components did not affect reovirus utilization of its proteinaceous cellular receptor junctional adhesion molecule-A or cell entry kinetics. LPS and PG also did not affect the overall number of reovirus capsid proteins σ1 and σ3, suggesting their effect on virion thermostability is not mediated through altering the overall number of major capsid proteins on the virus. Incubation of reovirus with LPS and PG did not significantly affect the neutralizing efficiency of reovirus-specific antibodies. These data suggest that bacteria enhance reovirus infection of the intestinal tract by enhancing the thermal stability of the reovirus particle at a variety of temperatures through interactions between the viral particle and bacterial envelope components.
[Mh] Termos MeSH primário: Bacillus subtilis/fisiologia
Enterócitos/virologia
Escherichia coli K12/fisiologia
Infecções por Reoviridae/virologia
Reoviridae/fisiologia
[Mh] Termos MeSH secundário: Acetilglucosamina/análogos & derivados
Acetilglucosamina/metabolismo
Acetilglucosamina/toxicidade
Bacillus subtilis/metabolismo
Bacillus subtilis/ultraestrutura
Bacillus subtilis/virologia
Células CACO-2
Endotoxinas/metabolismo
Endotoxinas/toxicidade
Enterócitos/efeitos dos fármacos
Enterócitos/microbiologia
Enterócitos/patologia
Escherichia coli K12/metabolismo
Escherichia coli K12/ultraestrutura
Escherichia coli K12/virologia
Microbioma Gastrointestinal
Células HeLa
Temperatura Alta
Seres Humanos
Lipopolissacarídeos/metabolismo
Lipopolissacarídeos/toxicidade
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Microscopia Eletrônica de Transmissão
Peptidoglicano/metabolismo
Peptidoglicano/toxicidade
RNA/metabolismo
Estabilidade de RNA/efeitos dos fármacos
Proteínas Recombinantes/metabolismo
Reoviridae/química
Reoviridae/efeitos dos fármacos
Reoviridae/patogenicidade
Infecções por Reoviridae/metabolismo
Infecções por Reoviridae/microbiologia
Infecções por Reoviridae/patologia
Ácidos Teicoicos/metabolismo
Ácidos Teicoicos/toxicidade
Vírion/química
Vírion/patogenicidade
Vírion/fisiologia
Ligação Viral/efeitos dos fármacos
Internalização do Vírus/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endotoxins); 0 (Lipopolysaccharides); 0 (Luminescent Proteins); 0 (Peptidoglycan); 0 (RNA, recombinant); 0 (Recombinant Proteins); 0 (Teichoic Acids); 0 (red fluorescent protein); 56411-57-5 (lipoteichoic acid); 63231-63-0 (RNA); 67924-63-4 (endotoxin, Escherichia coli); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006768


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[PMID]:28745862
[Au] Autor:Zhang X; Chen X; Zhao W; Zeng C; Luo X; Li W; Li B; Jiang J; Dong Y
[Ad] Endereço:Division of Pharmaceutics & Pharmaceutical Chemistry, College of Pharmacy, ‡Department of Biomedical Engineering, §The Center for Clinical and Translational Science, ∥The Comprehensive Cancer Center, ⊥Dorothy M. Davis Heart & Lung Research Institute, and ¶Department of Radiation Oncology
[Ti] Título:GlcNAc Conjugated Atorvastatin with Enhanced Water Solubility and Cellular Internalization.
[So] Source:Bioconjug Chem;28(8):2109-2113, 2017 08 16.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Targeting ligands facilitate cell specific drug delivery and improve pharmaceutical properties. Herein, we designed two ligand drug conjugates by conjugating GlcNAc (N-acetylglucosamine) with atorvastatin. These two conjugates, termed G-AT and G-K-AT, exhibited enhanced water solubility and cellular uptake. Moreover, both G-AT and G-K-AT were able to release atorvastatin and consequently achieve significant inhibition against 3-hydroxy-3-methyl-glutaryl-coenzyme A (HMG-CoA) reductase.
[Mh] Termos MeSH primário: Acetilglucosamina/química
Atorvastatina Cálcica/química
Atorvastatina Cálcica/metabolismo
Água/química
[Mh] Termos MeSH secundário: Transporte Biológico
Linhagem Celular
Seres Humanos
Solubilidade
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
059QF0KO0R (Water); 48A5M73Z4Q (Atorvastatin Calcium); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00295


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[PMID]:28742148
[Au] Autor:Groussaud D; Khair M; Tollenaere AI; Waast L; Kuo MS; Mangeney M; Martella C; Fardini Y; Coste S; Souidi M; Benit L; Pique C; Issad T
[Ad] Endereço:INSERM, U1016, Institut Cochin, Paris, France.
[Ti] Título:Hijacking of the O-GlcNAcZYME complex by the HTLV-1 Tax oncoprotein facilitates viral transcription.
[So] Source:PLoS Pathog;13(7):e1006518, 2017 Jul.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The viral Tax oncoprotein plays a key role in both Human T-cell lymphotropic virus type 1 (HTLV-1)-replication and HTLV-1-associated pathologies, notably adult T-cell leukemia. Tax governs the transcription from the viral 5'LTR, enhancing thereby its own expression, via the recruitment of dimers of phosphorylated CREB to cAMP-response elements located within the U3 region (vCRE). In addition to phosphorylation, CREB is also the target of O-GlcNAcylation, another reversible post-translational modification involved in a wide range of diseases, including cancers. O-GlcNAcylation consists in the addition of O-linked-N-acetylglucosamine (O-GlcNAc) on Serine or Threonine residues, a process controlled by two enzymes: O-GlcNAc transferase (OGT), which transfers O-GlcNAc on proteins, and O-GlcNAcase (OGA), which removes it. In this study, we investigated the status of O-GlcNAcylation enzymes in HTLV-1-transformed T cells. We found that OGA mRNA and protein expression levels are increased in HTLV-1-transformed T cells as compared to control T cell lines while OGT expression is unchanged. However, higher OGA production coincides with a reduction in OGA specific activity, showing that HTLV-1-transformed T cells produce high level of a less active form of OGA. Introducing Tax into HEK-293T cells or Tax-negative HTLV-1-transformed TL-om1 T cells is sufficient to inhibit OGA activity and increase total O-GlcNAcylation, without any change in OGT activity. Furthermore, Tax interacts with the OGT/OGA complex and inhibits the activity of OGT-bound OGA. Pharmacological inhibition of OGA increases CREB O-GlcNAcylation as well as HTLV-1-LTR transactivation by Tax and CREB recruitment to the LTR. Moreover, overexpression of wild-type CREB but not a CREB protein mutated on a previously described O-GlcNAcylation site enhances Tax-mediated LTR transactivation. Finally, both OGT and OGA are recruited to the LTR. These findings reveal the interplay between Tax and the O-GlcNAcylation pathway and identify new key molecular actors involved in the assembly of the Tax-dependent transactivation complex.
[Mh] Termos MeSH primário: Produtos do Gene tax/metabolismo
Infecções por HTLV-I/virologia
Vírus 1 Linfotrópico T Humano/metabolismo
N-Acetilglucosaminiltransferases/metabolismo
Linfócitos T/virologia
beta-N-Acetil-Hexosaminidases/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/metabolismo
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/genética
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
Regulação Viral da Expressão Gênica
Produtos do Gene tax/genética
Infecções por HTLV-I/enzimologia
Infecções por HTLV-I/genética
Infecções por HTLV-I/metabolismo
Interações Hospedeiro-Patógeno
Vírus 1 Linfotrópico T Humano/genética
Seres Humanos
N-Acetilglucosaminiltransferases/genética
Processamento de Proteína Pós-Traducional
Linfócitos T/enzimologia
Linfócitos T/metabolismo
Transcrição Genética
beta-N-Acetil-Hexosaminidases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclic AMP Response Element-Binding Protein); 0 (Gene Products, tax); 0 (tax protein, Human T-lymphotrophic virus 1); EC 2.4.1.- (N-Acetylglucosaminyltransferases); EC 2.4.1.- (O-GlcNAc transferase); EC 3.2.1.50 (hexosaminidase C); EC 3.2.1.52 (beta-N-Acetylhexosaminidases); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171213
[Lr] Data última revisão:
171213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006518


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[PMID]:28912268
[Au] Autor:Shen Y; Boulos S; Sumrall E; Gerber B; Julian-Rodero A; Eugster MR; Fieseler L; Nyström L; Ebert MO; Loessner MJ
[Ad] Endereço:From the Laboratory of Food Microbiology, Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, CH-8092 Zurich, yang.shen@hest.ethz.ch.
[Ti] Título:Structural and functional diversity in cell wall teichoic acids.
[So] Source:J Biol Chem;292(43):17832-17844, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Wall teichoic acids (WTAs) are the most abundant glycopolymers found on the cell wall of many Gram-positive bacteria, whose diverse surface structures play key roles in multiple biological processes. Despite recent technological advances in glycan analysis, structural elucidation of WTAs remains challenging due to their complex nature. Here, we employed a combination of ultra-performance liquid chromatography-coupled electrospray ionization tandem-MS/MS and NMR to determine the structural complexity of WTAs from species. We unveiled more than 10 different types of WTA polymers that vary in their linkage and repeating units. Disparity in GlcNAc to ribitol connectivity, as well as variable -acetylation and glycosylation of GlcNAc contribute to the structural diversity of WTAs. Notably, SPR analysis indicated that constitution of WTA determines the recognition by bacteriophage endolysins. Collectively, these findings provide detailed insight into cell wall-associated carbohydrates, and will guide further studies on the structure-function relationship of WTAs.
[Mh] Termos MeSH primário: Parede Celular/química
Parede Celular/metabolismo
Listeria/metabolismo
Ácidos Teicoicos/química
Ácidos Teicoicos/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/química
Acetilglucosamina/metabolismo
Ribitol/química
Ribitol/metabolismo
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Teichoic Acids); 488-81-3 (Ribitol); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.813964


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[PMID]:28886091
[Au] Autor:Britto-Borges T; Barton GJ
[Ad] Endereço:Division of Computational Biology, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
[Ti] Título:A study of the structural properties of sites modified by the O-linked 6-N-acetylglucosamine transferase.
[So] Source:PLoS One;12(9):e0184405, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein O-GlcNAcylation (O-GlcNAc) is an essential post-translational modification (PTM) in higher eukaryotes. The O-linked ß-N-acetylglucosamine transferase (OGT), targets specific Serines and Threonines (S/T) in intracellular proteins. However, unlike phosphorylation, fewer than 25% of known O-GlcNAc sites match a clear sequence pattern. Accordingly, the three-dimensional structures of O-GlcNAc sites were characterised to investigate the role of structure in molecular recognition. From 1,584 O-GlcNAc sites in 620 proteins, 143 were mapped to protein structures determined by X-ray crystallography. The modified S/T were 1.7 times more likely to be annotated in the REM465 field which defines missing residues in a protein structure, while 7 O-GlcNAc sites were solvent inaccessible and unlikely to be targeted by OGT. 132 sites with complete backbone atoms clustered into 10 groups, but these were indistinguishable from clusters from unmodified S/T. This suggests there is no prevalent three-dimensional motif for OGT recognition. Predicted features from the 620 proteins were compared to unmodified S/T in O-GlcNAcylated proteins and globular proteins. The Jpred4 predicted secondary structure shows that modified S/T were more likely to be coils. 5/6 methods to predict intrinsic disorder indicated O-GlcNAcylated S/T to be significantly more disordered than unmodified S/T. Although the analysis did not find a pattern in the site three-dimensional structure, it revealed the residues around the modification site are likely to be disordered and suggests a potential role of secondary structure elements in OGT site recognition.
[Mh] Termos MeSH primário: Modelos Moleculares
N-Acetilglucosaminiltransferases/química
Conformação Proteica
[Mh] Termos MeSH secundário: Acetilglucosamina/genética
Acetilglucosamina/metabolismo
Sítios de Ligação
N-Acetilglucosaminiltransferases/metabolismo
Ligação Proteica
Processamento de Proteína Pós-Traducional
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.4.1.- (N-Acetylglucosaminyltransferases); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184405



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