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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]:28460033
[Au] Autor:Ram S; Shaughnessy J; de Oliveira RB; Lewis LA; Gulati S; Rice PA
[Ad] Endereço:Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
[Ti] Título:Gonococcal lipooligosaccharide sialylation: virulence factor and target for novel immunotherapeutics.
[So] Source:Pathog Dis;75(4), 2017 Jun 01.
[Is] ISSN:2049-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gonorrhea has become resistant to most conventional antimicrobials used in clinical practice. The global spread of multidrug-resistant isolates of Neisseria gonorrhoeae could lead to an era of untreatable gonorrhea. New therapeutic modalities with novel mechanisms of action that do not lend themselves to the development of resistance are urgently needed. Gonococcal lipooligosaccharide (LOS) sialylation is critical for complement resistance and for establishing infection in humans and experimental mouse models. Here we describe two immunotherapeutic approaches that target LOS sialic acid: (i) a fusion protein that comprises the region in the complement inhibitor factor H (FH) that binds to sialylated gonococci and IgG Fc (FH/Fc fusion protein) and (ii) analogs of sialic acid that are incorporated into LOS but fail to protect the bacterium against killing. Both molecules showed efficacy in the mouse vaginal colonization model of gonorrhea and may represent promising immunotherapeutic approaches to target multidrug-resistant isolates. Disabling key gonococcal virulence mechanisms is an effective therapeutic strategy because the reduction of virulence is likely to be accompanied by a loss of fitness, rapid elimination by host immunity and consequently, decreased transmission.
[Mh] Termos MeSH primário: Gonorreia/prevenção & controle
Lipopolissacarídeos/metabolismo
Neisseria gonorrhoeae/fisiologia
Ácidos Siálicos/metabolismo
Fatores de Virulência/metabolismo
[Mh] Termos MeSH secundário: Animais
Fator H do Complemento/genética
Fator H do Complemento/metabolismo
Modelos Animais de Doenças
Feminino
Fragmentos Fc das Imunoglobulinas/genética
Fragmentos Fc das Imunoglobulinas/metabolismo
Camundongos
Neisseria gonorrhoeae/efeitos dos fármacos
Ligação Proteica
Proteínas Recombinantes de Fusão/metabolismo
Vagina/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin Fc Fragments); 0 (Lipopolysaccharides); 0 (Recombinant Fusion Proteins); 0 (Sialic Acids); 0 (Virulence Factors); 0 (lipid-linked oligosaccharides); 80295-65-4 (Complement Factor H)
[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:170502
[St] Status:MEDLINE
[do] DOI:10.1093/femspd/ftx049


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[PMID]:28745640
[Au] Autor:Cao C; Wang WJ; Huang YY; Yao HL; Conway LP; Liu L; Voglmeir J
[Ad] Endereço:Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University.
[Ti] Título:Determination of Sialic Acids in Liver and Milk Samples of Wild-type and CMAH Knock-out Mice.
[So] Source:J Vis Exp;(125), 2017 Jul 14.
[Is] ISSN:1940-087X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CMAH (cytidine monophosphate-N-acetylneuraminic acid hydroxylase) is responsible for the oxidation of cytidine monophosphate-N-acetylneuraminic acids in mammals. However, humans cannot oxidize cytidine monophosphate-N-acetylneuraminic acid to cytidine monophosphate-N-glycolylneuraminic acid due to a primary exon deletion of the CMAH gene. To understand the effects and implications of the lack of CMAH activity in more detail, a Cmah knock-out model in mice is of keen interest in basic and applied research. The analysis method to determine the phenotype of this mouse model is herein described in detail, and is based on the detection of both N-acetylneuraminic acid and N-glycolylenuraminic acid in the liver and milk of wild-type and Cmah knock-out mice. Endogenous sialic acids are released and derivatized with o-phenylenediamine to generate fluorogenic derivatives, which can be subsequently analyzed by HPLC. The presented protocol can be also applied for the analysis of milk and tissue samples from various other origins, and may be of use to investigate the nutritional and health effects of N-glycolylneuraminic acid.
[Mh] Termos MeSH primário: Cromatografia Líquida de Alta Pressão
Fígado/química
Leite/química
Oxigenases de Função Mista/genética
Ácidos Siálicos/análise
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas/genética
Fígado/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Oxigenases de Função Mista/deficiência
Ácidos Siálicos/isolamento & purificação
Gravação em Vídeo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sialic Acids); EC 1.- (Mixed Function Oxygenases); EC 1.14.18.2 (CMPacetylneuraminate monooxygenase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.3791/56030


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[PMID]:29235834
[Au] Autor:Holota YV; Olefir YA; Dovbynchuk TV; Tolstanova GM
[Ti] Título:Carbohydrate composition of rat intestine surface mucus layer after ceftriaxone treatment.
[So] Source:Ukr Biochem J;88(6):35-44, 2016 Nov-Dec.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The epidemiological studies have shown that antibiotic treatment increases the susceptibility to inflammatory bowel disease development. The disturbance of mucus layer integrity might be one of the possible mechanisms. The aim of the present study was to investigate the effect of antibiotic ceftriaxone treatment on glycoproteins level and its carbohydrate composition in surface mucus layer of rat intestine. The study was done on male Wistar rats (140-160 g). Ceftriaxone (300 mg/kg, i.m.) was administered once a day for 14 days. The surface mucus from terminal ileum and colon were collected on the 15th, 29th and 72nd days of the experiment. Total level of mucus glycoproteins, hexoses, hexosamines, fucose and sialic acids were measured. Ceftriaxone administration did not affect the levels of glycoproteins in rat ileum. In the colon, the levels of glycoprotein were 1.3-fold decreased (Р < 0.05) on the 72nd day of the experiment. These changes were accompanied by the 1.2-fold decrease of hexoses (Р < 0.05) and 3.1-fold (Р < 0.05) decrease of fucose level and 1.5-fold (Р < 0.05) increase of the levels of sialic acids in the surface mucus of the rat colon. Thus, ceftriaxone administration induces the long-term changes in the levels of glycoproteins and carbohydrates composition in the rat colon surface mucus. This could potentially explain the susceptibility to inflammatory bowel disea­ses development.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Ceftriaxona/farmacologia
Colo/efeitos dos fármacos
Íleo/efeitos dos fármacos
Muco/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Colo/química
Colo/metabolismo
Esquema de Medicação
Fucose/metabolismo
Glicoproteínas/metabolismo
Hexosaminas/metabolismo
Hexoses/metabolismo
Íleo/química
Íleo/metabolismo
Injeções Intramusculares
Masculino
Muco/química
Muco/metabolismo
Ratos
Ratos Wistar
Ácidos Siálicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Glycoproteins); 0 (Hexosamines); 0 (Hexoses); 0 (Sialic Acids); 28RYY2IV3F (Fucose); 75J73V1629 (Ceftriaxone)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.06.035


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[PMID]:28863277
[Au] Autor:Naguib MM; Arafa AS; Parvin R; Beer M; Vahlenkamp T; Harder TC
[Ad] Endereço:Institute of Diagnostic Virology, Friedrich-Loeffler-Institut, Suedufer 10, Greifswald Insel-Riems 17493, Germany; National Laboratory for Veterinary Quality Control on Poultry Production, Animal Health Research Institute, Giza 12618, Egypt.
[Ti] Título:Insights into genetic diversity and biological propensities of potentially zoonotic avian influenza H9N2 viruses circulating in Egypt.
[So] Source:Virology;511:165-174, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Low pathogenic avian influenza (LPAI) H9N2 viruses have established endemic status in Egyptian poultry populations since 2012. Recently, four cases of human H9N2 virus infections in Egypt demonstrated the zoonotic potential of these viruses. Egyptian H9N2 viruses obtained from 2011 to 2014 phylogenetically grouped into three clusters (1-3) within subclade B of the G1 lineage. Antigenically, a close clustering of the Egyptian H9N2 viruses with other recent G1-B like H9N2 strains and a significant antigenic distance from viruses outside the G1-B lineage was evident. Recent Egyptian LPAIV H9N2 showed a tendency to increased binding with erythrocytes expressing α 2,6-linked sialic acid which correlated with the Q226L amino acid substitution at the receptor binding unit of the hemagglutinin (Q234L, H9 numbering). Sequence analyses of the N2 neuraminidase (NA) revealed substitutions in the NA hemadsorption site similar to the N2 of prepandemic H3N2/1968, but no distinct antigenic or functional characteristics of the H9N2 NA associated with increased zoonotic potential could be identified.
[Mh] Termos MeSH primário: Variação Genética
Vírus da Influenza A Subtipo H9N2/classificação
Vírus da Influenza A Subtipo H9N2/genética
Influenza Aviária/virologia
Influenza Humana/virologia
Zoonoses/virologia
[Mh] Termos MeSH secundário: Animais
Análise por Conglomerados
Egito
Genótipo
Glicoproteínas de Hemaglutininação de Vírus da Influenza/genética
Seres Humanos
Vírus da Influenza A Subtipo H9N2/isolamento & purificação
Vírus da Influenza A Subtipo H9N2/fisiologia
Neuraminidase/genética
Filogenia
Aves Domésticas
Receptores Virais/metabolismo
Sorogrupo
Ácidos Siálicos/metabolismo
Proteínas Virais/genética
Ligação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Receptors, Virus); 0 (Sialic Acids); 0 (Viral Proteins); EC 3.2.1.18 (NA protein, influenza A virus); EC 3.2.1.18 (Neuraminidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE


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[PMID]:28760868
[Au] Autor:Werneburg S; Fuchs HLS; Albers I; Burkhardt H; Gudi V; Skripuletz T; Stangel M; Gerardy-Schahn R; Hildebrandt H
[Ad] Endereço:Institute of Clinical Biochemistry, and.
[Ti] Título:Polysialylation at Early Stages of Oligodendrocyte Differentiation Promotes Myelin Repair.
[So] Source:J Neurosci;37(34):8131-8141, 2017 Aug 23.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polysialic acid is a glycan modification of the neural cell adhesion molecule (NCAM) produced by the polysialyltransferases ST8SIA2 and ST8SIA4. Polysialic acid has been detected in multiple sclerosis plaques, but its beneficial or adverse role in remyelination is elusive. Here, we show that, despite a developmental delay, myelination at the onset and during cuprizone-induced demyelination was unaffected in male or mice. However, remyelination, restoration of oligodendrocyte densities, and motor recovery after the cessation of cuprizone treatment were compromised. Impaired differentiation of NCAM- or ST8SIA2-negative oligodendrocyte precursors suggested an underlying cell-autonomous mechanism. In contrast, premature differentiation in ST8SIA4-negative cultures explained the accelerated remyelination previously observed in mice. mRNA profiling during differentiation of human stem cell-derived and primary murine oligodendrocytes indicated that the opposing roles of ST8SIA2 and ST8SIA4 arise from sequential expression. We also provide evidence that potentiation of ST8SIA2 by 9- retinoic acid and artificial polysialylation of oligodendrocyte precursors by a bacterial polysialyltransferase are mechanisms to promote oligodendrocytic differentiation. Thus, differential targeting of polysialyltransferases and polysialic acid engineering are promising strategies to advance the treatment of demyelinating diseases. The beneficial or adverse role of polysialic acid (polySia) in myelin repair is a long-standing question. As a modification of the neural cell adhesion molecule (NCAM), polySia is produced by the polysialyltransferases ST8SIA2 and ST8SIA4. Here we demonstrate that NCAM and ST8SIA2 promote oligodendrocyte differentiation and myelin repair as well as motor recovery after cuprizone-induced demyelination. In contrast, ST8SIA4 delays oligodendrocyte differentiation, explaining its adverse role in remyelination. These opposing roles of the polysialyltransferases are based on different expression profiles. 9- retinoic acid enhances ST8SIA2 expression, providing a mechanism for understanding how it supports oligodendrocyte differentiation and remyelination. Furthermore, artificial polysialylation of the cell surface promotes oligodendrocyte differentiation. Thus, boosting ST8SIA2 and engineering of polySia are promising strategies for improving myelin repair.
[Mh] Termos MeSH primário: Antígeno CD56/biossíntese
Diferenciação Celular/fisiologia
Bainha de Mielina/metabolismo
Oligodendroglia/metabolismo
Sialiltransferases/biossíntese
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Doenças Desmielinizantes/metabolismo
Células-Tronco Embrionárias/metabolismo
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Atividade Motora/fisiologia
Molécula L1 de Adesão de Célula Nervosa
Distribuição Aleatória
Ácidos Siálicos/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD56 Antigen); 0 (Ncam1 protein, mouse); 0 (Neural Cell Adhesion Molecule L1); 0 (Sialic Acids); 0 (polysialic acid); 0 (polysialyl neural cell adhesion molecule); EC 2.4.99.- (CMP-N-acetylneuraminate-poly-alpha-2,8-sialosyl sialyltransferase); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.8 (ST8SiaIV protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1147-17.2017


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[PMID]:28678638
[Au] Autor:Zhang T; Zhou S; Liu Y; Luo X; Di D; Song Y; Liu X; Deng Y
[Ad] Endereço:a College of Pharmacy , Shenyang Pharmaceutical University , Shenyang , P.R. China.
[Ti] Título:Polysialic acid and pluronic F127 mixed polymeric micelles of docetaxel as new approach for enhanced antitumor efficacy.
[So] Source:Drug Dev Ind Pharm;43(11):1827-1835, 2017 Nov.
[Is] ISSN:1520-5762
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In our previous study, polysialic acid-octadecyl dimethyl betaine (PSA-BS18) was synthesized and modified to liposomal EPI. Preliminary experiments revealed that the PSA-BS18 was a potential material for targeting tumor site with superior curative effects. In this study, PSA-BS18 and Pluronic F127 (F127) mixed polymeric micelles encapsulated docetaxel (DTX) (FP/DTX) were prepared by a self-assembly method. The FP/DTX was found to have a diameter of 34.83 ± 0.50 nm with a narrow polydispersity, the entrapment efficiency was 99.12 ± 1.17%, and the drug loading efficiency of 1.40 ± 0.01%. The storage and dilution stability of FP/DTX was fine. In vitro release studies demonstrated that FP/DTX had delayed the drug release from the micelles. In vitro cytotoxicity assay on B16 cells presented that FP/DTX led to a stronger cytotoxic activity in comparison to F127 micelles based DTX (F127/DTX) and Tween80-based DTX (Taxotere ). The in vivo imaging study showed that the accumulation of FP/DTX at tumor sites was more than F127/DTX. The in vivo antitumor activity of FP/DTX against B16 tumor xenograft model showed a significant higher inhibition and a lower toxicity compared with F127/DTX and Taxotere . Taken together, the results obtained above showed that PSA-BS18 and F127 mixed polymeric micelles may be a promising strategy for antitumor delivery of DTX.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Poloxâmero/química
Polietilenoglicóis/química
Ácidos Siálicos/química
[Mh] Termos MeSH secundário: Antineoplásicos/química
Portadores de Fármacos
Sistemas de Liberação de Medicamentos
Lipossomos
Micelas
Taxoides
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Drug Carriers); 0 (Liposomes); 0 (Micelles); 0 (Sialic Acids); 0 (Taxoids); 0 (polysialic acid); 106392-12-5 (Poloxamer); 15H5577CQD (docetaxel); 30IQX730WE (Polyethylene Glycols)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1080/03639045.2017.1349784


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[PMID]:28652312
[Au] Autor:Li J; Evans DR; Freedman JC; McClane BA
[Ad] Endereço:Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
[Ti] Título:NanR Regulates Sialidase Expression by Clostridium perfringens F4969, a Human Enteropathogenic Strain.
[So] Source:Infect Immun;85(9), 2017 Sep.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:can produce up to three different sialidases, including NanI, its major exosialidase. The current study first showed that human intestinal strains of can grow by utilizing either glucose or sialic acids, such as -acetylneuraminic acid (Neu5Ac), which are the end products of sialidase activity. For the human enteropathogenic strain F4969, it was then determined that culture supernatant sialidase activity and expression of exosialidase genes, particularly , are influenced by the presence of Neu5Ac or glucose. Low Neu5Ac concentrations increased culture supernatant sialidase activity, largely by stimulating transcription. In contrast, low glucose concentrations did not affect exosialidase activity or transcription. However, either high Neu5Ac or high glucose concentrations repressed F4969 culture supernatant sialidase activity and transcription levels. Furthermore, high glucose levels repressed F4969 culture sialidase activity and expression even in the presence of low Neu5AC concentrations. To begin to evaluate the mechanistic basis for expression, a null mutant was used to demonstrate that NanR, a member of the RpiR family of regulatory proteins, decreases exosialidase activity and transcription in the absence of sialic acid. The ability of to regulate its exosialidase activity, largely by controlling expression, may affect intestinal pathogenesis by affecting the production of NanI, which may affect growth, adhesion, and toxin binding .
[Mh] Termos MeSH primário: Clostridium perfringens/genética
Proteínas de Ligação a DNA/metabolismo
Regulação Bacteriana da Expressão Gênica
Neuraminidase/biossíntese
[Mh] Termos MeSH secundário: Clostridium perfringens/crescimento & desenvolvimento
Clostridium perfringens/metabolismo
Perfilação da Expressão Gênica
Glucose/metabolismo
Seres Humanos
Ácidos Siálicos/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Sialic Acids); EC 3.2.1.18 (Neuraminidase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


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[PMID]:28635265
[Au] Autor:Heise T; Büll C; Beurskens DM; Rossing E; de Jonge MI; Adema GJ; Boltje TJ; Langereis JD
[Ad] Endereço:Institute for Molecules and Materials, Radboud University Nijmegen , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
[Ti] Título:Metabolic Oligosaccharide Engineering with Alkyne Sialic Acids Confers Neuraminidase Resistance and Inhibits Influenza Reproduction.
[So] Source:Bioconjug Chem;28(7):1811-1815, 2017 Jul 19.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metabolic incorporation of azide- or alkyne-modified sialic acids into the cellular glycosylation pathway enables the study of sialoglycan expression, localization, and trafficking via bioorthogonal chemistry. Herein, we report that such modifications of the sialic acid sugar can have a profound influence on their hydrolysis by neuraminidases (sialidase). Azidoacetyl (Az)-modified sialic acids were prone to neuraminidase cleavage, whereas propargyloxycarbonyl (Poc)-modified sialic acids were largely resistant to cleavage. Because the influenza virus infection cycle depends on the hydrolysis of host-cell-surface sialic acids, influenza cell-to-cell transmission was strongly reduced in Poc sialic acid glycoengineered host cells. The use of Poc sialic acids may disturb biological processes involving neuraminidase cleavage but also provides perspective for use in applications in which sialic acid hydrolysis is not desired, such as antibody modification, viral infection, etc.
[Mh] Termos MeSH primário: Alquinos/química
Neuraminidase/metabolismo
Oligossacarídeos/metabolismo
Orthomyxoviridae/fisiologia
Ácidos Siálicos/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
Hidrólise
Engenharia Metabólica/métodos
Oligossacarídeos/química
Ácidos Siálicos/química
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkynes); 0 (Oligosaccharides); 0 (Sialic Acids); EC 3.2.1.18 (Neuraminidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00224


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[PMID]:28621497
[Au] Autor:Hinderlich S; Tauber R; Bertozzi CR; Hackenberger CPR
[Ad] Endereço:Beuth Hochschule für Technik Berlin, Fachbereich Life Sciences and Technology, Seestrasse 64, 13347, Berlin, Germany.
[Ti] Título:Werner Reutter: A Visionary Pioneer in Molecular Glycobiology.
[So] Source:Chembiochem;18(13):1141-1145, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A creative pioneer: Werner Reutter (1937-2016) was a scientist who both made fundamental discoveries in glycobiology and reached out to disciplines beyond his core field. Many of his former colleagues and students will remember his desire to exchange research ideas, which ultimately contributed to the birth of new research fields.
[Mh] Termos MeSH primário: Glicômica/recursos humanos
Biologia Molecular/recursos humanos
[Mh] Termos MeSH secundário: Metabolismo dos Carboidratos/genética
Glicômica/história
Glicômica/métodos
História do Século XX
História do Século XXI
Seres Humanos
Engenharia Metabólica/história
Engenharia Metabólica/métodos
Biologia Molecular/história
Biologia Molecular/métodos
Ácidos Siálicos/genética
Ácidos Siálicos/metabolismo
[Pt] Tipo de publicação:BIOGRAPHY; EDITORIAL; HISTORICAL ARTICLE; PORTRAITS
[Ps] Nome de pessoa como assunto:Reutter W
[Nm] Nome de substância:
0 (Sialic Acids)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700277



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