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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]:28751193
[Au] Autor:Shan Y; Liu Y; Zhao L; Liu B; Li Y; Jia L
[Ad] Endereço:College of Laboratory Medicine, Dalian Medical University, Dalian 116044, Liaoning Province, China.
[Ti] Título:MicroRNA-33a and let-7e inhibit human colorectal cancer progression by targeting ST8SIA1.
[So] Source:Int J Biochem Cell Biol;90:48-58, 2017 Sep.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Colorectal cancer (CRC) is one of the leading causes of cancer mortality worldwide. Aberrant sialylation is crucially involved in the progression of various types of cancer. MicroRNAs (miRNAs) have been broadly studied in cancer. MicroRNA-33a (miR-33a) and Has-let-7e (let-7e) are non-coding RNA that can reduce cell motility and viability in cancer. In this study, miR-33a and let-7e levels were confirmed to be significantly down-regulated in CRC samples (n=32) and drug resistant cell line (HCT-8/5-FU) compared with those in the matched adjacent tissues and drug sensitivity cell line (HCT-8). ST8SIA1 was highly expressed in CRC tissues and HCT-8/5-FU cells, which was negatively correlated with miR-33a/let-7e expression. Luciferase reporter assays confirmed that both miR-33a and let-7e bound to the 3'-untranslated (3'-UTR) region of ST8SIA1. Inhibiting miR-33a/let-7e expression in CRC cells increased endogenous ST8SIA1 mRNA and protein levels. MiR-33a/let-7e knockdown promoted chemoresistance, proliferation, invasion, angiogenesis in vitro, and tumor growth in vivo. Whereas, ectopic expression of miR-33a/let-7e suppressed chemoresistance, proliferation, invasion and angiogenesis in CRC cell lines. ST8SIA1 knockdown mimicked the tumor suppressive effect of miR-33a/let-7e on CRC cells, while restoration of ST8SIA1 abolished the tumor suppressive effect of miR-33a/let-7e on CRC cells. Taken together, altered expression of miR-33a/let-7e was correlated with ST8SIA1 level, which might contribute to CRC progression. The miR-33a/let-7e-ST8SIA1 axis could be a therapeutic target for CRC patients.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
Neoplasias Colorretais/patologia
Progressão da Doença
MicroRNAs/genética
Sialiltransferases/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Proliferação Celular/genética
Transformação Celular Neoplásica
Neoplasias Colorretais/tratamento farmacológico
Resistência a Medicamentos Antineoplásicos/genética
Seres Humanos
Camundongos
Invasividade Neoplásica/genética
Neovascularização Patológica/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MicroRNAs); 0 (mirnlet7 microRNA, human); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.8 (alpha-N-acetylneuraminate alpha-2,8-sialyltransferase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170729
[St] Status:MEDLINE


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[PMID]:28717006
[Au] Autor:Manhardt CT; Punch PR; Dougher CWL; Lau JTY
[Ad] Endereço:From the Departments of Molecular and Cellular Biology and.
[Ti] Título:Extrinsic sialylation is dynamically regulated by systemic triggers .
[So] Source:J Biol Chem;292(33):13514-13520, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent reports have documented that extracellular sialyltransferases can remodel both cell-surface and secreted glycans by a process other than the canonical cell-autonomous glycosylation that occurs within the intracellular secretory apparatus. Despite association of the abundance of these extracellular sialyltransferases, particularly ST6Gal-1, with disease states such as cancer and a variety of inflammatory conditions, the prevalence of this extrinsic glycosylation pathway remains unknown. Here we observed no significant extrinsic sialylation in resting mice, suggesting that extrinsic sialylation is not a constitutive process. However, extrinsic sialylation in the periphery could be triggered by inflammatory challenges, such as exposure to ionizing radiation or to bacterial lipopolysaccharides. Sialic acids from circulating platelets were used to remodel target cell surfaces. Platelet activation was minimally sufficient to elicit extrinsic sialylation, as demonstrated with the FeCl model of mesenteric artery thrombosis. Although extracellular ST6Gal-1 supports extrinsic sialylation, other sialyltransferases are present in systemic circulation. We also observed extrinsic sialylation in animals deficient in ST6Gal-1, demonstrating that extrinsic sialylation is not mediated exclusively by ST6Gal-1. Together, these observations form an emerging picture of glycans biosynthesized by the canonical cell-autonomous glycosylation pathway, but subjected to remodeling by extracellular glycan-modifying enzymes.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Modelos Animais de Doenças
Oxigenases de Função Mista/metabolismo
Processamento de Proteína Pós-Traducional
Sialiltransferases/metabolismo
Síndrome de Resposta Inflamatória Sistêmica/metabolismo
Trombose/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/sangue
Biomarcadores/metabolismo
Plaquetas/imunologia
Plaquetas/patologia
Células da Medula Óssea/imunologia
Células da Medula Óssea/metabolismo
Células da Medula Óssea/patologia
Artérias Mesentéricas
Camundongos Endogâmicos C57BL
Camundongos Knockout
Oxigenases de Função Mista/genética
Ativação Plaquetária
Sialiltransferases/sangue
Sialiltransferases/genética
Síndrome de Resposta Inflamatória Sistêmica/sangue
Síndrome de Resposta Inflamatória Sistêmica/imunologia
Síndrome de Resposta Inflamatória Sistêmica/patologia
Trombose/sangue
Trombose/imunologia
Trombose/patologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); EC 1.- (Mixed Function Oxygenases); EC 1.14.18.2 (CMPacetylneuraminate monooxygenase); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.1 (beta-D-galactoside alpha 2-6-sialyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.C117.795138


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[PMID]:28707750
[Au] Autor:Cameron SA; White SM; Arrollo D; Shulman ST; Rowley AH
[Ad] Endereço:Department of Pediatrics/Cardiology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
[Ti] Título:Arterial immune protein expression demonstrates the complexity of immune responses in Kawasaki disease arteritis.
[So] Source:Clin Exp Immunol;190(2):244-250, 2017 Nov.
[Is] ISSN:1365-2249
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A more complete understanding of immune-mediated damage to the coronary arteries in children with Kawasaki disease (KD) is required for improvements in patient treatment and outcomes. We recently reported the transcriptional profile of KD coronary arteritis, and in this study sought to determine protein expression of transcriptionally up-regulated immune genes in KD coronary arteries from the first 2 months after disease onset. We examined the coronary arteries of 12 fatal KD cases and 13 childhood controls for expression of a set of proteins whose genes were highly up-regulated in the KD coronary artery transcriptome: allograft inflammatory factor 1 (AIF1), interleukin 18 (IL-18), CD74, CD1c, CD20 (MS4A1), Toll-like receptor 7 (TLR-7) and Z-DNA binding protein 1 (ZBP1). Immunohistochemistry and immunofluorescence studies were performed to evaluate protein expression and co-localization, respectively. AIF1 was expressed transmurally in KD arteritis and localized to macrophages and myeloid dendritic cells. CD74, which interacts with major histocompatibility complex (MHC) class II on antigen-presenting cells, localized to the intima-media. CD1c, a marker of myeloid dendritic cells, was expressed in a transmural pattern, as were IL-18 and CD20. ZBP1 and TLR-7 were up-regulated compared to controls, but less highly compared to the other proteins. These findings provide evidence of antigen presentation and interferon response in KD arteritis. In combination with prior studies demonstrating T lymphocyte activation, these results demonstrate the complexity of the KD arterial immune response.
[Mh] Termos MeSH primário: Arterite/imunologia
Vasos Coronários/imunologia
Expressão Gênica
Síndrome de Linfonodos Mucocutâneos/imunologia
Síndrome de Linfonodos Mucocutâneos/metabolismo
[Mh] Termos MeSH secundário: Apresentação do Antígeno
Antígenos CD/genética
Antígenos CD1/genética
Antígenos CD20/genética
Arterite/fisiopatologia
Aneurisma Coronário/imunologia
Vasos Coronários/fisiopatologia
Proteínas de Ligação a DNA/genética
Feminino
Imunofluorescência
Perfilação da Expressão Gênica
Glicoproteínas/genética
Seres Humanos
Imuno-Histoquímica
Lactente
Interleucina-18/genética
Masculino
Síndrome de Linfonodos Mucocutâneos/complicações
Síndrome de Linfonodos Mucocutâneos/mortalidade
Sialiltransferases/genética
Receptor 7 Toll-Like/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AIF1 protein, human); 0 (Antigens, CD); 0 (Antigens, CD1); 0 (Antigens, CD20); 0 (CD1C protein, human); 0 (DNA-Binding Proteins); 0 (Glycoproteins); 0 (Interleukin-18); 0 (TLR7 protein, human); 0 (Toll-Like Receptor 7); 0 (ZBP1 protein, human); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.1 (ST6GAL1 protein, human)
[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:170715
[St] Status:MEDLINE
[do] DOI:10.1111/cei.13010


  5 / 2543 MEDLINE  
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[PMID]:28698248
[Au] Autor:Chumpen Ramirez S; Ruggiero FM; Daniotti JL; Valdez Taubas J
[Ad] Endereço:Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), CONICET, Universidad Nacional de Córdoba, Córdoba, Argentina jvaldezt@dqb.fcq.unc.edu.ar.
[Ti] Título:Ganglioside glycosyltransferases are S-acylated at conserved cysteine residues involved in homodimerisation.
[So] Source:Biochem J;474(16):2803-2816, 2017 Aug 07.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ganglioside glycosyltransferases (GGTs) are type II membrane proteins bearing a short N-terminal cytoplasmic tail, a transmembrane domain (TMD), and a lumenal catalytic domain. The expression and activity of these enzymes largely determine the quality of the glycolipids that decorate mammalian cell membranes. Many glycosyltransferases (GTs) are themselves glycosylated, and this is important for their proper localisation, but few if any other post-translational modifications of these proteins have been reported. Here, we show that the GGTs, ST3Gal-V, ST8Sia-I, and ß4GalNAcT-I are S-acylated at conserved cysteine residues located close to the cytoplasmic border of their TMDs. ST3Gal-II, a GT that sialylates glycolipids and glycoproteins, is also S-acylated at a conserved cysteine located in the N-terminal cytoplasmic tail. Many other GTs also possess cysteine residues in their cytoplasmic regions, suggesting that this modification occurs also on these GTs. S-acylation, commonly known as palmitoylation, is catalysed by a family of palmitoyltransferases (PATs) that are mostly localised at the Golgi complex but also at the endoplasmic reticulum (ER) and the plasma membrane. Using GT ER retention mutants, we found that S-acylation of ß4GalNAcT-I and ST3Gal-II takes place at different compartments, suggesting that these enzymes are not substrates of the same PAT. Finally, we found that cysteines that are the target of S-acylation on ß4GalNAcT-I and ST3Gal-II are involved in the formation of homodimers through disulphide bonds. We observed an increase in ST3Gal-II dimers in the presence of the PAT inhibitor 2-bromopalmitate, suggesting that GT homodimerisation may be regulating S-acylation.
[Mh] Termos MeSH primário: N-Acetilgalactosaminiltransferases/metabolismo
Processamento de Proteína Pós-Traducional
Sialiltransferases/metabolismo
[Mh] Termos MeSH secundário: Acilação
Sequência de Aminoácidos
Animais
Células CHO
Linhagem Celular
Sequência Conservada
Cricetulus
Cisteína/metabolismo
Dimerização
Seres Humanos
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Microscopia de Fluorescência
Mutação
N-Acetilgalactosaminiltransferases/química
N-Acetilgalactosaminiltransferases/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Filogenia
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Sialiltransferases/química
Sialiltransferases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Luminescent Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); EC 2.4.1.- (N-Acetylgalactosaminyltransferases); EC 2.4.1.165 (beta-1,4-N-acetyl-galactosaminyl transferase 1, human); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase); EC 2.4.99.8 (alpha-N-acetylneuraminate alpha-2,8-sialyltransferase); EC 2.4.99.9 (haematoside synthetase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170124


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[PMID]:28687873
[Au] Autor:Li Q; Wei D; Feng F; Wang XL; Li C; Chen ZN; Bian H
[Ad] Endereço:Department of Cell Biology, National Translational Science Center for Molecular Medicine, Fourth Military Medical University, No. 169, Changle West Road, Xi'an, 710032, China.
[Ti] Título:α2,6-linked sialic acid serves as a high-affinity receptor for cancer oncolytic virotherapy with Newcastle disease virus.
[So] Source:J Cancer Res Clin Oncol;143(11):2171-2181, 2017 Nov.
[Is] ISSN:1432-1335
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Newcastle disease virus (NDV) has been applied to oncolytic virotherapy for decades due to its naturally oncolytic property. In spite of the substantiation of the sialic acid receptors of NDV on host cells, knowledge of preference of sialic acid linkage in viral attachment and oncolytic effect is lacking and imperative to be elucidated. METHODS: Surface plasmon resonance analysis and competitive inhibition with sialylated glycan receptor analogues were used to determine the affinity and the preference of sialic acid receptor. Treatments of sialyltransferase inhibitors and linkage-specific sialidases and transfection with sialyltransferase expression vector were performed to regulate sialic acids levels. RESULTS: We demonstrated that sialic acid was essential for NDV binding and infection of tumor cells. α2,6-linked sialic acid served as a high-affinity receptor for NDV and the ST6Gal I sialyltransferase that synthesizes α2-6 linkage of sialylated N-linked glycans in CHO-K1 cells promoted NDV binding and cytopathic effect. More importantly, an enhanced antitumor effect of NDV on aggressive SW620 colorectal carcinoma cells with high-level of cell surface α2,6-sialylation, but not SW480 cells with relative low-level of α2,6-sialylation, was observed both in vitro and in vivo. CONCLUSIONS: The study provides evidence of optimized therapeutic strategy in oncolytic virotherapy via partly defining α2,6-sialylated receptor as a "cellular marker" for NDV.
[Mh] Termos MeSH primário: Neoplasias do Colo/terapia
Ácido N-Acetilneuramínico/metabolismo
Vírus da Doença de Newcastle/genética
Terapia Viral Oncolítica
Sialiltransferases/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Células CHO
Proliferação Celular
Neoplasias do Colo/metabolismo
Neoplasias do Colo/patologia
Cricetinae
Cricetulus
Seres Humanos
Camundongos
Camundongos Nus
Células Tumorais Cultivadas
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.4.99.- (Sialyltransferases); EC 2.4.99.1 (beta-D-galactoside alpha 2-6-sialyltransferase); EC 2.4.99.6 (N-acetyllactosaminide alpha-2,3-sialyltransferase); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170709
[St] Status:MEDLINE
[do] DOI:10.1007/s00432-017-2470-y


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[PMID]:28632300
[Au] Autor:Richard E; Pifferi C; Fiore M; Samain E; Le Gouëllec A; Fort S; Renaudet O; Priem B
[Ad] Endereço:Université Grenoble Alpes and CNRS, CERMAV, 601, rue de la chimie, 38000, Grenoble, France.
[Ti] Título:Chemobacterial Synthesis of a Sialyl-Tn Cyclopeptide Vaccine Candidate.
[So] Source:Chembiochem;18(17):1730-1734, 2017 Sep 05.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A conjugatable form of the tumour-associated carbohydrate antigen sialyl-Tn (Neu5Ac-α-2,6-GalNAc) was efficiently produced in Escherichia coli. Metabolically engineered E. coli strains overexpressing the 6-sialyltransferase gene of Photobacterium sp. and CMP-Neu5Ac synthetase genes of Neisseria meningitidis were cultivated at high density in the presence of GalNAc-α-propargyl as the exogenous acceptor. The target disaccharides, which were produced on the scale of several hundreds of milligrams, were then conjugated by using copper(I)-catalysed azide-alkyne cycloaddition click chemistry to a fully synthetic and immunogenic scaffold with the aim to create a candidate anticancer vaccine. Four sialyl-Tn epitopes were introduced on the upper face of an azido-functionalised multivalent cyclopeptide scaffold, the lower face of which was previously modified by an immunogenic polypeptide, PADRE. The ability of the resulting glycoconjugate to interact with oncofoetal sialyl-Tn monoclonal antibodies was confirmed in ELISA assays.
[Mh] Termos MeSH primário: Antígenos Glicosídicos Associados a Tumores/metabolismo
Escherichia coli/metabolismo
Vacinas Sintéticas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Anticorpos Monoclonais/imunologia
Reações Antígeno-Anticorpo
Antígenos Glicosídicos Associados a Tumores/química
Antígenos Glicosídicos Associados a Tumores/genética
Antígenos Glicosídicos Associados a Tumores/imunologia
Vacinas Anticâncer/genética
Vacinas Anticâncer/imunologia
Vacinas Anticâncer/metabolismo
Cromatografia em Camada Delgada
Química Click
Ensaio de Imunoadsorção Enzimática
Epitopos/química
Epitopos/genética
Epitopos/imunologia
Epitopos/metabolismo
Engenharia Metabólica
Neisseria/enzimologia
Peptídeos Cíclicos/genética
Peptídeos Cíclicos/imunologia
Peptídeos Cíclicos/metabolismo
Photobacterium/enzimologia
Sialiltransferases/genética
Sialiltransferases/metabolismo
Vacinas Sintéticas/genética
Vacinas Sintéticas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antigens, Tumor-Associated, Carbohydrate); 0 (Cancer Vaccines); 0 (Epitopes); 0 (Peptides, Cyclic); 0 (Vaccines, Synthetic); 0 (sialosyl-Tn antigen); EC 2.4.99.- (Sialyltransferases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700240


  8 / 2543 MEDLINE  
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[PMID]:28586101
[Au] Autor:Huang X; Schurman N; Handa K; Hakomori S
[Ad] Endereço:Division of Biomembrane Research, Pacific Northwest Research Institute, Seattle, WA, USA.
[Ti] Título:Functional role of glycosphingolipids in contact inhibition of growth in a human mammary epithelial cell line.
[So] Source:FEBS Lett;591(13):1918-1928, 2017 Jul.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have demonstrated previously the involvement of certain glycosphingolipids (GSLs) in 'contact inhibition' (dependent on cell-to-cell contact) of cell growth. Here, we examined the roles of specific GSLs in contact inhibition of the human epithelial cell line MCF10A. Contact-inhibited cells show increased expression of the ganglioside GD3 and the globo-series GSL Gb3, and of the mRNAs for the corresponding sialyltransferases ST8SIA1 (GD3 synthase) and galactosyltransferase A4GALT (Gb3 synthase). siRNA knockdown (KD) of ST8SIA1 and/or A4GALT significantly suppresses contact inhibition. Exogenous addition of GD3 or Gb3 inhibits proliferation of low-density cells. Our findings suggest that GSLs play functional roles in contact inhibition of these cells and that Merlin/NF2, a tumor suppressor protein, is involved in the GSL function.
[Mh] Termos MeSH primário: Inibição de Contato
Glicoesfingolipídeos/metabolismo
Glândulas Mamárias Humanas/citologia
[Mh] Termos MeSH secundário: Contagem de Células
Linhagem Celular Tumoral
Proliferação Celular
Galactosiltransferases/deficiência
Galactosiltransferases/genética
Regulação da Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/genética
Sialiltransferases/deficiência
Sialiltransferases/genética
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Glycosphingolipids); 0 (RNA, Messenger); 0 (RNA, Small Interfering); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.- (UDP-galactose-lactosylceramide alpha 1-4-galactosyltransferase); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.8 (alpha-N-acetylneuraminate alpha-2,8-sialyltransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170607
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12709


  9 / 2543 MEDLINE  
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[PMID]:28550122
[Au] Autor:Dougher CWL; Buffone A; Nemeth MJ; Nasirikenari M; Irons EE; Bogner PN; Lau JTY
[Ad] Endereço:Department of Immunology, Roswell Park Cancer Institute, Buffalo, New York, USA.
[Ti] Título:The blood-borne sialyltransferase ST6Gal-1 is a negative systemic regulator of granulopoiesis.
[So] Source:J Leukoc Biol;102(2):507-516, 2017 Aug.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Responding to systemic demands in producing and replenishing end-effector blood cells is predicated on the appropriate delivery and interpretation of extrinsic signals to the HSPCs. The data presented herein implicate the systemic, extracellular form of the glycosyltransferase ST6Gal-1 in the regulation of late-stage neutrophil development. ST6Gal-1 is typically a membrane-bound enzyme sequestered within the intracellular secretory apparatus, but an extracellular form is released into the blood from the liver. Both human and murine HSPCs, upon exposure to extracellular ST6Gal-1 ex vivo, exhibited decreased proliferation, diminished expression of the neutrophilic primary granule protein MPO, and decreased appearance of CD11b cells. HSPC suppression was preceded by decreased STAT-3 phosphorylation and diminished C/EBPα expression, without increased apoptosis, indicating attenuated G-CSF receptor signaling. A murine model to raise systemic ST6Gal-1 level was developed to examine the role of the circulatory enzyme in vivo. Our results show that systemic ST6Gal-1 modified the cell surface of the GMP subset of HSPCs and decreased marrow neutrophil reserves. Acute airway neutrophilic inflammation by LPS challenge was used to drive demand for new neutrophil production. Reduced neutrophil infiltration into the airway was observed in mice with elevated circulatory ST6Gal-1 levels. The blunted transition of GMPs into GPs in vitro is consistent with ST6Gal-1-attenuated granulopoiesis. The data confirm that circulatory ST6Gal-1 is a negative systemic regulator of granulopoiesis and moreover suggest a clinical potential to limit the number of inflammatory cells by manipulating blood ST6Gal-1 levels.
[Mh] Termos MeSH primário: Hematopoese/imunologia
Neutrófilos/citologia
Sialiltransferases/imunologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Diferenciação Celular/imunologia
Citometria de Fluxo
Imunofluorescência
Células-Tronco Hematopoéticas/citologia
Seres Humanos
Camundongos Endogâmicos C57BL
Neutrófilos/metabolismo
Sialiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.4.99.- (Sialyltransferases); EC 2.4.99.1 (beta-D-galactoside alpha 2-6-sialyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170528
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.3A1216-538RR


  10 / 2543 MEDLINE  
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[PMID]:28521605
[Au] Autor:Ogata M; Koizumi A; Otsubo T; Ikeda K; Sakamoto M; Aita R; Kato T; Park EY; Yamanaka T; Hidari KIPJ
[Ad] Endereço:a Department of Chemistry and Biochemistry, National Institute of Technology , Fukushima College , Iwaki , Japan.
[Ti] Título:Chemoenzymatic synthesis and characterization of N-glycolylneuraminic acid-carrying sialoglycopolypeptides as effective inhibitors against equine influenza virus hemagglutination.
[So] Source:Biosci Biotechnol Biochem;81(8):1520-1528, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A series of novel sialoglycopolypeptides carrying N-glycolylneuraminic acid (Neu5Gc)-containing trisaccharides having α(2 â†’ 3)- and α(2 â†’ 6)-linkages in the side chains of γ-polyglutamic acid (γ-PGA) were designed as competitive inhibitors against equine influenza viruses (EIV), which critically recognize the Neu5Gc residue for receptor binding. Using horse red blood cells (HRBC) we successfully evaluated the binding activity of the multivalent Neu5Gc ligands to both equine and canine influenza viruses in the hemagglutination inhibition (HI) assay. Our findings show the multivalent α2,3-linked Neu5Gc-ligands (3a-c and 7) selectively inhibit hemagglutination mediated by both influenza viruses and display a strong inhibitory activity. Our results indicate that the multivalent Neu5Gc-ligands can be used as novel probes to elucidate the mechanism of infection/adhesion of Neu5Gc-binding influenza viruses.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Hemaglutinação/efeitos dos fármacos
Orthomyxoviridae/efeitos dos fármacos
Sialoglicoproteínas/farmacologia
Sialiltransferases/química
[Mh] Termos MeSH secundário: Animais
Antivirais/química
Antivirais/metabolismo
Ligação Competitiva
Bombyx
Sequência de Carboidratos
Clonagem Molecular
Cães
Eritrócitos/efeitos dos fármacos
Eritrócitos/virologia
Expressão Gênica
Testes de Inibição da Hemaglutinação
Hemolinfa/química
Cavalos
Seres Humanos
Ácidos Neuramínicos/química
Nucleopolyhedrovirus/genética
Nucleopolyhedrovirus/metabolismo
Ácido Poliglutâmico/análogos & derivados
Ácido Poliglutâmico/química
Ácido Poliglutâmico/metabolismo
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sialoglicoproteínas/biossíntese
Sialoglicoproteínas/química
Sialiltransferases/genética
Sialiltransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Neuraminic Acids); 0 (Recombinant Proteins); 0 (Sialoglycoproteins); 0 (poly(gamma-glutamic acid)); 1113-83-3 (N-glycolylneuraminic acid); 25513-46-6 (Polyglutamic Acid); EC 2.4.99.- (Sialyltransferases); EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1325315



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