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[PMID]:29072708
[Au] Autor:Hjuler CT; Maolanon NN; Sauer J; Stougaard J; Thygesen MB; Jensen KJ
[Ad] Endereço:Centre for Carbohydrate Recognition and Signaling, Copenhagen University, Frederiksberg, Denmark.
[Ti] Título:Preparation of glycoconjugates from unprotected carbohydrates for protein-binding studies.
[So] Source:Nat Protoc;12(11):2411-2422, 2017 Nov.
[Is] ISSN:1750-2799
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycobiology, in particular the study of carbohydrate-protein interactions and the events that follow, has become an important research focus in recent decades. To study these interactions, many assays require homogeneous glycoconjugates in suitable amounts. Their synthesis is one of the methodological challenges of glycobiology. Here, we describe a versatile, three-stage protocol for the formation of glycoconjugates from unprotected carbohydrates, including those purified from natural sources, as exemplified here by rhizobial Nod factors and exopolysaccharide fragments. The first stage is to add an oligo(ethylene glycol) linker (OEG-linker) that has a terminal triphenylmethanethiol group to the reducing end of the oligosaccharide by oxime formation catalyzed by aniline. The triphenylmethyl (trityl) tag is then removed from the linker to expose a thiol (stage 2) to allow a conjugation reaction at the thiol group (stage 3). There are many possible conjugation reactions, depending on the desired application. Examples shown in this protocol are as follows: (i) coupling of the oligosaccharide to a support for surface plasmon resonance (SPR) studies, (ii) fluorescence labeling for microscale thermophoresis (MST) or bioimaging, and (iii) biotinylation for biolayer interferometry (BLI) studies. This protocol starts from unprotected carbohydrates and provides glycoconjugates in milligram amounts in just 2 d.
[Mh] Termos MeSH primário: Técnicas de Química Sintética
Glicoconjugados/síntese química
Glicômica/métodos
Lipopolissacarídeos/química
Compostos de Sulfidrila/química
Compostos de Tritil/química
[Mh] Termos MeSH secundário: Compostos de Anilina/química
Biotinilação
Catálise
Interferometria
Imagem Óptica
Oximas/química
Polietilenoglicóis/química
Ligação Proteica
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aniline Compounds); 0 (Glycoconjugates); 0 (Lipopolysaccharides); 0 (Nod factor IV, Rhizobium meliloti); 0 (Oximes); 0 (Sulfhydryl Compounds); 0 (Trityl Compounds); 30IQX730WE (Polyethylene Glycols); SIR7XX2F1K (aniline)
[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:171027
[St] Status:MEDLINE
[do] DOI:10.1038/nprot.2017.109


  2 / 872 MEDLINE  
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[PMID]:28683920
[Au] Autor:Montgomery AP; Xiao K; Wang X; Skropeta D; Yu H
[Ad] Endereço:School of Chemistry, Faculty of Science, Medicine and Health, University of Wollongong, Wollongong, NSW, Australia.
[Ti] Título:Computational Glycobiology: Mechanistic Studies of Carbohydrate-Active Enzymes and Implication for Inhibitor Design.
[So] Source:Adv Protein Chem Struct Biol;109:25-76, 2017.
[Is] ISSN:1876-1623
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Carbohydrate-active enzymes (CAZymes) are families of essential and structurally related enzymes, which catalyze the creation, modification, and degradation of glycosidic bonds in carbohydrates to maintain essentially all kingdoms of life. CAZymes play a key role in many biological processes underpinning human health and diseases (e.g., cancer, diabetes, Alzheimer's diseases, AIDS) and have thus emerged as important drug targets in the fight against pathogenesis. The realization of the full potential of CAZymes remains a significant challenge, relying on a deeper understanding of the molecular mechanisms of catalysis. Considering numerous unsettled questions in the literature, while with a large amount of structural, kinetic, and mutagenesis data available for CAZymes, there is a pressing need and an abundant opportunity for collaborative computational and experimental investigations with the aim to unlock the secrets of CAZyme catalysis at an atomic level. In this review, we briefly survey key methodology development in computational studies of CAZyme catalysis. This is complemented by selected case studies highlighting mechanistic insights provided by computational glycobiology. Implication for inhibitor design by mimicking the transition state is also illustrated for both glycoside hydrolases and glycosyltransferases. The challenges for such studies will be noted and finally an outlook for future directions will be provided.
[Mh] Termos MeSH primário: Projeto Auxiliado por Computador
Descoberta de Drogas/métodos
Inibidores Enzimáticos/farmacologia
Glicômica/métodos
Glicosídeo Hidrolases/antagonistas & inibidores
Glicosiltransferases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Metabolismo dos Carboidratos/efeitos dos fármacos
Carboidratos/química
Inibidores Enzimáticos/química
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/metabolismo
Glicosiltransferases/química
Glicosiltransferases/metabolismo
Seres Humanos
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Carbohydrates); 0 (Enzyme Inhibitors); EC 2.4.- (Glycosyltransferases); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE


  3 / 872 MEDLINE  
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[PMID]:28681696
[Au] Autor:Chen H; Deng Z; Huang C; Wu H; Zhao X; Li Y
[Ad] Endereço:1 Key Laboratory of Marine Drugs, Ministry of Education, Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, School of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
[Ti] Título:Mass spectrometric profiling reveals association of N-glycan patterns with epithelial ovarian cancer progression.
[So] Source:Tumour Biol;39(7):1010428317716249, 2017 Jul.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aberrant changes of N-glycan modifications on proteins have been linked to various diseases including different cancers, suggesting possible avenue for exploring their etiologies based on N-glycomic analysis. Changes in N-glycan patterns during epithelial ovarian cancer development have so far been investigated mainly using serum, plasma, ascites, and cell lines. However, changes in patterns of N-glycans in tumor tissues during epithelial ovarian cancer progression have remained largely undefined. To investigate whether changes in N-glycan patterns correlate with oncogenesis and progression of epithelial ovarian cancer, we profiled N-glycans from formalin-fixed paraffin-embedded tissue slides using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and quantitatively compared among different pathological grades of epithelial ovarian cancer and healthy controls. Our results show that among the 80 compositions of N-glycan detected, expression levels of high-mannose type were higher in epithelial ovarian cancer samples than that observed in healthy controls, accompanied by reduced levels of hybrid-type glycans. By applying receiver operating characteristic analysis, we show that a combined panel composed of four high-mannose and three fucosylated neutral complex N-glycans allows for good discrimination of epithelial ovarian cancer from healthy controls. Furthermore, using a statistical analysis of variance assay, we found that different N-glycan patterns, including 2 high-mannose-type, 2 fucosylated and sialylated complex structures, and 10 fucosylated neutral complex N-glycans, exhibited specific changes in N-glycan abundance across epithelial ovarian cancer grades. Together, our results provide strong evidence that N-glycomic changes are a strong indicator for epithelial ovarian cancer pathological grades and should provide avenues to identify novel biomarkers for epithelial ovarian cancer diagnosis and monitoring.
[Mh] Termos MeSH primário: Carcinogênese/genética
Glicômica
Neoplasias Epiteliais e Glandulares/genética
Neoplasias Ovarianas/genética
Polissacarídeos/genética
[Mh] Termos MeSH secundário: Idoso
Linhagem Celular Tumoral
Progressão da Doença
Feminino
Seres Humanos
Meia-Idade
Neoplasias Epiteliais e Glandulares/metabolismo
Neoplasias Epiteliais e Glandulares/patologia
Neoplasias Ovarianas/metabolismo
Neoplasias Ovarianas/patologia
Polissacarídeos/isolamento & purificação
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polysaccharides)
[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:170707
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317716249


  4 / 872 MEDLINE  
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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


  5 / 872 MEDLINE  
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[PMID]:28556908
[Au] Autor:Hykollari A; Malzl D; Yan S; Wilson IBH; Paschinger K
[Ad] Endereço:Department für Chemie, Universität für Bodenkultur, Wien, Austria.
[Ti] Título:Hydrophilic interaction anion exchange for separation of multiply modified neutral and anionic Dictyostelium N-glycans.
[So] Source:Electrophoresis;38(17):2175-2183, 2017 09.
[Is] ISSN:1522-2683
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The unusual nature of the N-glycans of the cellular slime mould Dictyostelium discoideum has been revealed by a number of studies, primarily based on examination of radiolabeled glycopeptides but more recently also by MS. The complexity of the N-glycomes of even glycosylation mutants is compounded by the occurrence of anionic modifications, which also present an analytical challenge. In this study, we have employed hydrophilic interaction anion exchange (HIAX) HPLC in combination with MALDI-TOF MS/MS to explore the anionic N-glycome of the M31 (modA) strain, which lacks endoplasmic reticulum α-glucosidase II, an enzyme conserved in most eukaryotes including Homo sapiens. Prefractionation with HIAX chromatography enabled the identification of N-glycans with unusual oligo-α1,2-mannose extensions as well as others with up to four anionic modifications. Due to the use of hydrofluoric acid treatment, we were able to discriminate isobaric glycans differing in the presence of sulphate or phosphate on intersected structures as opposed to those carrying GlcNAc-phosphodiesters. The latter represent biosynthetic intermediates during the pathway leading to formation of the methylphosphorylated mannose epitope, which may have a similar function in intracellular targeting of hydrolases as the mannose-6-phosphate modification of lysosomal enzymes in mammals. In conclusion, HIAX in combination with MS is a highly sensitive approach for both fine separation and definition of neutral and anionic N-glycan structures.
[Mh] Termos MeSH primário: Cromatografia por Troca Iônica/métodos
Dictyostelium/química
Glicômica/métodos
Polissacarídeos/análise
Polissacarídeos/química
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão/métodos
Dictyostelium/metabolismo
Hexoses/análise
Hexoses/química
Interações Hidrofóbicas e Hidrofílicas
Manose/análise
Manose/química
Fosfatos/análise
Fosfatos/química
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos
Sulfatos/análise
Sulfatos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hexoses); 0 (Phosphates); 0 (Polysaccharides); 0 (Sulfates); PHA4727WTP (Mannose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE
[do] DOI:10.1002/elps.201700073


  6 / 872 MEDLINE  
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[PMID]:28509371
[Au] Autor:Konze SA; Cajic S; Oberbeck A; Hennig R; Pich A; Rapp E; Buettner FFR
[Ad] Endereço:Institute of Clinical Biochemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625, Hannover, Germany.
[Ti] Título:Quantitative Assessment of Sialo-Glycoproteins and N-Glycans during Cardiomyogenic Differentiation of Human Induced Pluripotent Stem Cells.
[So] Source:Chembiochem;18(13):1317-1331, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human induced pluripotent stem-cell-derived cardiomyocytes (hiPSC CMs) may be used in regenerative medicine for individualized tissue transplants in the future. For application in patients, the generated CMs have to be highly pure and well characterized. In order to overcome the prevalent scarcity of CM-specific markers, we quantitatively assessed cell-surface-exposed sialo-glycoproteins and N-glycans of hiPSCs, CM progenitors, and CMs. Applying a combination of metabolic labeling and specific sialo-glycoprotein capture, we could highly enrich and quantify membrane proteins during cardiomyogenic differentiation. Among them we identified a number of novel, putative biomarkers for hiPSC CMs. Analysis of the N-glycome by capillary gel electrophoresis revealed three novel structures comprising ß1,3-linked galactose, α2,6-linked sialic acid and complex fucosylation; these were highly specific for hiPSCs. Bisecting GlcNAc structures strongly increased during differentiation, and we propose that they are characteristic of early, immature CMs.
[Mh] Termos MeSH primário: Membrana Celular/química
Glicômica/métodos
Células-Tronco Pluripotentes Induzidas/química
Miócitos Cardíacos/química
Polissacarídeos/química
[Mh] Termos MeSH secundário: Acetilglucosamina/química
Acetilglucosamina/metabolismo
Sequência de Carboidratos
Diferenciação Celular
Membrana Celular/metabolismo
Subunidade alfa do Receptor do Fator Neutrófico Ciliar/genética
Subunidade alfa do Receptor do Fator Neutrófico Ciliar/metabolismo
Fucose/química
Fucose/metabolismo
Galactose/química
Galactose/metabolismo
Gastrinas/genética
Gastrinas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Células-Tronco Pluripotentes Induzidas/citologia
Células-Tronco Pluripotentes Induzidas/metabolismo
Laminina/genética
Laminina/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Miócitos Cardíacos/citologia
Miócitos Cardíacos/metabolismo
Polissacarídeos/metabolismo
Receptor EphA7/genética
Receptor EphA7/metabolismo
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores/metabolismo
Receptores Acoplados a Proteínas-G/genética
Receptores Acoplados a Proteínas-G/metabolismo
Ácidos Siálicos/química
Ácidos Siálicos/metabolismo
Coloração e Rotulagem/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CNTFR protein, human); 0 (Ciliary Neurotrophic Factor Receptor alpha Subunit); 0 (Gastrins); 0 (HEPH protein, human); 0 (LGR4 protein, human); 0 (Laminin); 0 (Membrane Proteins); 0 (Polysaccharides); 0 (Receptors, G-Protein-Coupled); 0 (Sialic Acids); 151186-83-3 (laminin A); 28RYY2IV3F (Fucose); EC 2.7.10.1 (Receptor, EphA7); EC 3.1.3.48 (PTPRD protein, human); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2); V956696549 (Acetylglucosamine); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700100


  7 / 872 MEDLINE  
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[PMID]:28388299
[Au] Autor:Adua E; Russell A; Roberts P; Wang Y; Song M; Wang W
[Ad] Endereço:1 School of Medical and Health Sciences, Edith Cowan University , Perth, Australia .
[Ti] Título:Innovation Analysis on Postgenomic Biomarkers: Glycomics for Chronic Diseases.
[So] Source:OMICS;21(4):183-196, 2017 Apr.
[Is] ISSN:1557-8100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite decades of investment in biomarker research, we still do not have robust and field-tested biomarkers for many chronic diseases so as to anticipate clinical outcomes and thus move toward personalized medicine. Biomarker innovations have tended to focus on genomics, but next-generation biomarkers from the nascent field of glycomics now offer fresh vistas for innovation in chronic disease biomarkers and systems diagnostics. Glycosylation, regarded as a complex enzymatic process where sugars (glycans) bind to proteins and lipids, affects many human biological functions, including cell signaling, adhesion, and motility. Notably, and contrary to proteins, glycan biosynthesis does not require a template; rather its final structure is catalyzed by a repertoire of enzymes that attach or detach monosaccharides in the glycosylation pathway, making glycomics research more challenging than proteomics or genomics. Yet, given glycans' biological significance, alterations in their processing may be detrimental to human health and also offer insights for preventive medicine and wellness interventions. Therefore, studying glycans' structure and understanding their function and molecular interactions in the emerging field of glycomics are key to unraveling the pathogenesis of various common chronic diseases. This review summarizes the major concepts in glycomics, including glycan release methods, techniques for large-scale glycan analysis, and glycoinformatic tools for data handling and storage. In all, this analysis on glycomics offers strategies to build a robust postgenomic innovation roadmap for glycan-driven biomarkers as the field is anticipated to mature further and gain greater prominence in the near future.
[Mh] Termos MeSH primário: Biomarcadores/análise
Glicômica/métodos
[Mh] Termos MeSH secundário: Doença Crônica
Glicosilação
Medicina de Precisão
Proteômica/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.1089/omi.2017.0035


  8 / 872 MEDLINE  
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[PMID]:28383803
[Au] Autor:Zhu Y; Chen X
[Ad] Endereço:College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China.
[Ti] Título:Expanding the Scope of Metabolic Glycan Labeling in Arabidopsis thaliana.
[So] Source:Chembiochem;18(13):1286-1296, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Metabolic glycan labeling (MGL) has gained wide utility and has become a useful tool for probing glycosylation in living systems. For the past three decades, the development and application of MGL have mostly focused on animal glycosylation. Recently, exploiting MGL for studying plant glycosylation has gained interest. Here, we describe a systematic evaluation of MGL for fluorescence imaging of root glycans in Arabidopsis thaliana. Nineteen monosaccharide analogues containing a bioorthogonal group (azide, alkyne, or cyclopropene) were synthesized and evaluated for metabolic incorporation into root glycans. Among these unnatural sugars, 14 (including three new compounds) were evaluated in plants for the first time. Our results showed that five unnatural sugars metabolically labeled root glycans efficiently, and enabled fluorescence imaging by bioorthogonal conjugation with fluorophores. We optimized the experimental procedures for MGL in Arabidopsis. Finally, distinct distribution patterns of the newly synthesized glycans were observed along the root developmental zones, thus indicating regulated biosynthesis of glycans during root development. We envision that MGL will find broad applications in plant glycobiology.
[Mh] Termos MeSH primário: Alquinos/química
Arabidopsis/metabolismo
Azidas/química
Materiais Biomiméticos/química
Ciclopropanos/química
Raízes de Plantas/metabolismo
Polissacarídeos/química
[Mh] Termos MeSH secundário: Alquinos/metabolismo
Arabidopsis/química
Arabidopsis/ultraestrutura
Azidas/metabolismo
Materiais Biomiméticos/metabolismo
Carbocianinas/química
Configuração de Carboidratos
Sequência de Carboidratos
Ciclopropanos/metabolismo
Corantes Fluorescentes/química
Glicoconjugados/química
Glicoconjugados/metabolismo
Glicômica/métodos
Glicosilação
Monossacarídeos/química
Monossacarídeos/metabolismo
Raízes de Plantas/química
Raízes de Plantas/ultraestrutura
Polissacarídeos/metabolismo
Coloração e Rotulagem/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkynes); 0 (Azides); 0 (Carbocyanines); 0 (Cyclopropanes); 0 (Fluorescent Dyes); 0 (Glycoconjugates); 0 (Monosaccharides); 0 (Polysaccharides); 0 (cyanine dye 5); 7B8994OHJ0 (cyclopropene)
[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:170407
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700069


  9 / 872 MEDLINE  
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[PMID]:28370937
[Au] Autor:Montacir H; Freyer N; Knöspel F; Urbaniak T; Dedova T; Berger M; Damm G; Tauber R; Zeilinger K; Blanchard V
[Ad] Endereço:Institute of Laboratory Medicine, Clinical Chemistry and Pathobiochemistry, Charité-Universitätsmedizin Berlin, Augustenburger Platz 1, 13353, Berlin, Germany.
[Ti] Título:The Cell-Surface N-Glycome of Human Embryonic Stem Cells and Differentiated Hepatic Cells thereof.
[So] Source:Chembiochem;18(13):1234-1241, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human embryonic stem cells (hESCs) are pluripotent stem cells that offer a wide range of applications in regenerative medicine. In addition, they have been proposed as an appropriate alternative source of hepatocytes. In this work, hESCs were differentiated into definitive endodermal cells (DECs), followed by maturation into hepatocyte-like cells (HLCs). Their cell-surface N-glycome was profiled and also compared with that of primary human hepatocytes (PHHs). Undifferentiated hESCs contained large amounts of high-mannose N-glycans. In contrast, complex-type N-glycans such as asialylated or monosialylated biantennary and triantennary N-glycans were dominant in HLCs, and fully galactosylated structures were significantly more abundant than in undifferentiated hESCs. The cell-surface N-glycosylation of PHHs was more biologically processed than that of HLCs, with bisialylated biantennary and trisialylated triantennary structures predominant. This is the first report of the cell surface N-glycome of PHHs and of HLCs being directly generated from hESCs without embryoid body formation.
[Mh] Termos MeSH primário: Membrana Celular/química
Glicômica
Hepatócitos/química
Células-Tronco Embrionárias Humanas/química
Polissacarídeos/química
[Mh] Termos MeSH secundário: Biomarcadores/metabolismo
Configuração de Carboidratos
Sequência de Carboidratos
Diferenciação Celular
Membrana Celular/metabolismo
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Metabolismo Energético
Expressão Gênica
Glicosilação
Hepatócitos/citologia
Hepatócitos/metabolismo
Células-Tronco Embrionárias Humanas/citologia
Células-Tronco Embrionárias Humanas/metabolismo
Seres Humanos
Manose/química
Manose/metabolismo
Polissacarídeos/metabolismo
Cultura Primária de Células
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Polysaccharides); 0 (Transcription Factors); 9035-51-2 (Cytochrome P-450 Enzyme System); PHA4727WTP (Mannose)
[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:170404
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700001


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[PMID]:28334832
[Au] Autor:Russell AC; Simurina M; Garcia MT; Novokmet M; Wang Y; Rudan I; Campbell H; Lauc G; Thomas MG; Wang W
[Ad] Endereço:School of Medical and Health Sciences, Edith Cowan University, 270 Joondalup Drive, Joondalup, WA 6027, Australia.
[Ti] Título:The N-glycosylation of immunoglobulin G as a novel biomarker of Parkinson's disease.
[So] Source:Glycobiology;27(5):501-510, 2017 May 01.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The use of the emerging "omics" technologies for large scale population screening is promising in terms of predictive, preventive and personalized medicine. For Parkinson's disease, it is essential that an accurate diagnosis is obtained and disease progression can be monitored. Immunoglobulin G (IgG) has the ability to exert both anti-inflammatory and pro-inflammatory effects, and the N-glycosylation of the fragment crystallizable portion of IgG is involved in this process. This study aimed to determine whether the IgG glycome could be a candidate biomarker for Parkinson's disease. Ninety-four community-based individuals with Parkinson's disease and a sex-, age- and ethnically-matched cohort of 102 individuals with mixed phenotypes, representative of a "normally" aged Caucasian controls, were investigated. Plasma IgG glycans were analyzed by ultra-performance liquid chromatography. Overall, seven glycan peaks and 11 derived traits had statistically significant differences (P < 8.06 × 10-4) between Parkinson's disease cases and healthy controls. Out of the seven significantly different glycan peaks, four were selected by Akaike's Information Criterion to be included in the logistic regression model, with a sensitivity of 87.2% and a specificity of 92.2%. The study suggested that there may be a reduced capacity for the IgG to inhibit Fcγ-RIIIa binding, which would allow an increased ability for the IgG to cause antibody-dependent cell cytotoxicity and a possible state of low-grade inflammation in individuals with Parkinson's disease.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Imunoglobulina G/sangue
Doença de Parkinson/sangue
Polissacarídeos/sangue
[Mh] Termos MeSH secundário: Idoso
Citotoxicidade Celular Dependente de Anticorpos/genética
Progressão da Doença
Feminino
Glicômica
Glicosilação
Seres Humanos
Masculino
Meia-Idade
Doença de Parkinson/genética
Doença de Parkinson/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Immunoglobulin G); 0 (Polysaccharides)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwx022



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