Base de dados : MEDLINE
Pesquisa : D09.254.488 [Categoria DeCS]
Referências encontradas : 4806 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 481 ir para página                         

  1 / 4806 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  2 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29176671
[Au] Autor:Schneider M; Kumar V; Nordstrøm LU; Feng L; Takeuchi H; Hao H; Luca VC; Garcia KC; Stanley P; Wu P; Haltiwanger RS
[Ad] Endereço:Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA.
[Ti] Título:Inhibition of Delta-induced Notch signaling using fucose analogs.
[So] Source:Nat Chem Biol;14(1):65-71, 2018 Jan.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Notch is a cell-surface receptor that controls cell-fate decisions and is regulated by O-glycans attached to epidermal growth factor-like (EGF) repeats in its extracellular domain. Protein O-fucosyltransferase 1 (Pofut1) modifies EGF repeats with O-fucose and is essential for Notch signaling. Constitutive activation of Notch signaling has been associated with a variety of human malignancies. Therefore, tools that inhibit Notch activity are being developed as cancer therapeutics. To this end, we screened L-fucose analogs for their effects on Notch signaling. Two analogs, 6-alkynyl and 6-alkenyl fucose, were substrates of Pofut1 and were incorporated directly into Notch EGF repeats in cells. Both analogs were potent inhibitors of binding to and activation of Notch1 by Notch ligands Dll1 and Dll4, but not by Jag1. Mutagenesis and modeling studies suggest that incorporation of the analogs into EGF8 of Notch1 markedly reduces the ability of Delta ligands to bind and activate Notch1.
[Mh] Termos MeSH primário: Família de Proteínas EGF/metabolismo
Fucose/análogos & derivados
Fucose/farmacologia
Fucosiltransferases/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas de Membrana/metabolismo
Receptores Notch/antagonistas & inibidores
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Fucose/química
Fucose/genética
Fucosiltransferases/genética
Células HEK293
Seres Humanos
Ligantes
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EGF Family of Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Ligands); 0 (Membrane Proteins); 0 (Receptors, Notch); 0 (delta protein); 28RYY2IV3F (Fucose); EC 2.4.1.- (Fucosyltransferases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2520


  3 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28450116
[Au] Autor:Shida M; Mikami T; Tamura JI; Kitagawa H
[Ad] Endereço:Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan.
[Ti] Título:A characteristic chondroitin sulfate trisaccharide unit with a sulfated fucose branch exhibits neurite outgrowth-promoting activity: Novel biological roles of fucosylated chondroitin sulfates isolated from the sea cucumber Apostichopus japonicus.
[So] Source:Biochem Biophys Res Commun;487(3):678-683, 2017 06 03.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chondroitin sulfate (CS) is a class of sulfated glycosaminoglycan (GAG) chains that consist of repeating disaccharide unit composed of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc). CS chains are found throughout the pericellular and extracellular spaces and contribute to the formation of functional microenvironments for numerous biological events. However, their structure-function relations remain to be fully characterized. Here, a fucosylated CS (FCS) was isolated from the body wall of the sea cucumber Apostichopus japonicus. Its promotional effects on neurite outgrowth were assessed by using isolated polysaccharides and the chemically synthesized FCS trisaccharide ß-D-GalNAc(4,6-O-disulfate) (1-4)[α-l-fucose (2,4-O-disulfate) (1-3)]-ß-D-GlcA. FCS polysaccharides contained the E-type disaccharide unit GlcA-GalNAc(4,6-O-disulfate) as a CS major backbone structure and carried distinct sulfated fucose branches. Despite their relatively lower abundance of E unit, FCS polysaccharides exhibited neurite outgrowth-promoting activity comparable to squid cartilage-derived CS-E polysaccharides, which are characterized by their predominant E units, suggesting potential roles of the fucose branch in neurite outgrowth. Indeed, the chemically synthesized FCS trisaccharide was as effective as CS-E tetrasaccharide in stimulating neurite elongation in vitro. In conclusion, FCS trisaccharide units with 2,4-O-disulfated fucose branches may provide new insights into understanding the structure-function relations of CS chains.
[Mh] Termos MeSH primário: Sulfatos de Condroitina/administração & dosagem
Neuritos/efeitos dos fármacos
Neuritos/fisiologia
Neurogênese/efeitos dos fármacos
Neurogênese/fisiologia
Pepinos-do-Mar/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Sulfatos de Condroitina/química
Relação Dose-Resposta a Droga
Fucose/química
Camundongos
Neuritos/ultraestrutura
Trissacarídeos/administração & dosagem
Trissacarídeos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Trisaccharides); 0 (fucosylated chondroitin sulfate); 28RYY2IV3F (Fucose); 9007-28-7 (Chondroitin Sulfates)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  4 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28465102
[Au] Autor:Zong G; Hirsch M; Mondrik C; Hu Z; Shi WQ
[Ad] Endereço:Department of Chemistry and Biochemistry, J. William Fulbright College of Arts & Science, University of Arkansas, Fayetteville, AR 72701, USA.
[Ti] Título:Design, synthesis and biological evaluation of fucose-truncated monosaccharide analogues of ipomoeassin F.
[So] Source:Bioorg Med Chem Lett;27(12):2752-2756, 2017 06 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ipomoeassin F is a plant-derived macrocyclic glycolipid with single-digit nanomolar IC values against cancer cell growth. In previous structure-activity relationship studies, we have demonstrated that certain modifications around the fucoside moiety did not cause significant cytotoxicity loss. To further elucidate the effect of the fucoside moiety on the biological activity, we describe here the design and synthesis of several fucose-truncated monosaccharide analogues of ipomoeassin F. Subsequent biological evaluation strongly suggests that the 6-membered ring of the fucoside moiety is essential to the overall conformation of the molecule, thereby influencing bioactivity.
[Mh] Termos MeSH primário: Antineoplásicos Fitogênicos/farmacologia
Desenho de Drogas
Fucose/farmacologia
Glicoconjugados/farmacologia
[Mh] Termos MeSH secundário: Antineoplásicos Fitogênicos/síntese química
Antineoplásicos Fitogênicos/química
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Ensaios de Seleção de Medicamentos Antitumorais
Fucose/química
Glicoconjugados/síntese química
Glicoconjugados/química
Seres Humanos
Estrutura Molecular
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:
0 (Antineoplastic Agents, Phytogenic); 0 (Glycoconjugates); 0 (ipomoeassin F); 28RYY2IV3F (Fucose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  5 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28988527
[Au] Autor:Kononova SV
[Ad] Endereço:Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. skonon23@gmail.com.
[Ti] Título:How Fucose of Blood Group Glycotopes Programs Human Gut Microbiota.
[So] Source:Biochemistry (Mosc);82(9):973-989, 2017 Sep.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Formation of appropriate gut microbiota is essential for human health. The first two years of life is the critical period for this process. Selection of mutualistic microorganisms of the intestinal microbiota is controlled by the FUT2 and FUT3 genes that encode fucosyltransferases, enzymes responsible for the synthesis of fucosylated glycan structures of mucins and milk oligosaccharides. In this review, the mechanisms of the selection and maintenance of intestinal microorganisms that involve fucosylated oligosaccharides of breast milk and mucins of the newborn's intestine are described. Possible reasons for the use of fucose, and not sialic acid, as the major biological signal for the selection are also discussed.
[Mh] Termos MeSH primário: Antígenos de Grupos Sanguíneos
Fucose
Microbioma Gastrointestinal
Leite Humano/química
[Mh] Termos MeSH secundário: Feminino
Fucosiltransferases/fisiologia
Seres Humanos
Lactente
Recém-Nascido
Leite Humano/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Blood Group Antigens); 28RYY2IV3F (Fucose); EC 2.4.1.- (Fucosyltransferases); EC 2.4.1.65 (3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase); EC 2.4.1.69 (galactoside 2-alpha-L-fucosyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171010
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917090012


  6 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28880909
[Au] Autor:Mastrangeli R; Satwekar A; Cutillo F; Ciampolillo C; Palinsky W; Longobardi S
[Ad] Endereço:Biotech Development Programme, Merck Serono S.p.A. (an affiliate of Merck KGaA, Darmstadt, Germany), Guidonia Montecelio, Rome, Italy.
[Ti] Título:In-vivo biological activity and glycosylation analysis of a biosimilar recombinant human follicle-stimulating hormone product (Bemfola) compared with its reference medicinal product (GONAL-f).
[So] Source:PLoS One;12(9):e0184139, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recombinant human follicle-stimulating hormone (r-hFSH) is widely used in fertility treatment. Although biosimilar versions of r-hFSH (follitropin alfa) are currently on the market, given their structural complexity and manufacturing process, it is important to thoroughly evaluate them in comparison with the reference product. This evaluation should focus on how they differ (e.g., active component molecular characteristics, impurities and potency), as this could be associated with clinical outcome. This study compared the site-specific glycosylation profile and batch-to-batch variability of the in-vivo bioactivity of Bemfola, a biosimilar follitropin alfa, with its reference medicinal product GONAL-f. The focus of this analysis was the site-specific glycosylation at asparagine (Asn) 52 of the α-subunit of FSH, owing to the pivotal role of Asn52 glycosylation in FSH receptor (FSHR) activation/signalling. Overall, Bemfola had bulkier glycan structures and greater sialylation than GONAL-f. The nominal specific activity for both Bemfola and GONAL-f is 13,636 IU/mg. Taking into account both the determined potency and the nominal amount the average specific activity of Bemfola was 14,522 IU/mg (105.6% of the nominal value), which was greater than the average specific activity observed for GONAL-f (13,159 IU/mg; 97.3% of the nominal value; p = 0.0048), although this was within the range stated in the product label. A higher batch-to-batch variability was also observed for Bemfola versus GONAL-f (coefficient of variation: 8.3% vs 5.8%). A different glycan profile was observed at Asn52 in Bemfola compared with GONAL-f (a lower proportion of bi-antennary structures [~53% vs ~77%], and a higher proportion of tri-antennary [~41% vs ~23%] and tetra-antennary structures [~5% vs <1%]). These differences in the Asn52 glycan profile might potentially lead to differences in FSHR activation. This, together with the greater bioactivity and higher batch-to-batch variability of Bemfola, could partly explain the reported differences in clinical outcomes. The clinical relevance of the differences observed between GONAL-f and Bemfola should be further investigated.
[Mh] Termos MeSH primário: Medicamentos Biossimilares/farmacologia
Hormônio Foliculoestimulante Humano/farmacologia
Hormônio Foliculoestimulante/farmacologia
Proteínas Recombinantes/farmacologia
[Mh] Termos MeSH secundário: Asparagina/metabolismo
Fucose/metabolismo
Glicopeptídeos/química
Glicosilação/efeitos dos fármacos
Seres Humanos
Ácido N-Acetilneuramínico/metabolismo
Mapeamento de Peptídeos
Polissacarídeos/metabolismo
Subunidades Proteicas/metabolismo
Padrões de Referência
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biosimilar Pharmaceuticals); 0 (Follicle Stimulating Hormone, Human); 0 (Glycopeptides); 0 (Polysaccharides); 0 (Protein Subunits); 0 (Recombinant Proteins); 0 (follitropin alfa); 28RYY2IV3F (Fucose); 7006-34-0 (Asparagine); 9002-68-0 (Follicle Stimulating Hormone); GZP2782OP0 (N-Acetylneuraminic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184139


  7 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28609653
[Au] Autor:Magalhães A; Duarte HO; Reis CA
[Ad] Endereço:Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal; Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), 4200-135 Porto, Portugal.
[Ti] Título:Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis.
[So] Source:Cancer Cell;31(6):733-735, 2017 06 12.
[Is] ISSN:1878-3686
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycosylation alterations are involved in several steps of human cancer pathogenesis. In this issue of Cancer Cell, Agrawal et al. identified the glycosyltransferase FUT8 as a previously unrecognized mediator of melanoma metastasis, establishing core fucosylation as a potential therapeutic target for prevention and treatment of metastatic tumors.
[Mh] Termos MeSH primário: Fucose
Fucosiltransferases
Melanoma
Metástase Neoplásica
Neoplasias Cutâneas
[Mh] Termos MeSH secundário: Glicosilação
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
28RYY2IV3F (Fucose); EC 2.4.1.- (Fucosyltransferases)
[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:170614
[St] Status:MEDLINE


  8 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28566370
[Au] Autor:Bruggeman CW; Dekkers G; Bentlage AEH; Treffers LW; Nagelkerke SQ; Lissenberg-Thunnissen S; Koeleman CAM; Wuhrer M; van den Berg TK; Rispens T; Vidarsson G; Kuijpers TW
[Ad] Endereço:Department of Blood Cell Research, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, 1066 CX Amsterdam, the Netherlands; c.bruggeman@sanquin.nl.
[Ti] Título:Enhanced Effector Functions Due to Antibody Defucosylation Depend on the Effector Cell Fcγ Receptor Profile.
[So] Source:J Immunol;199(1):204-211, 2017 Jul 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Abs of the IgG isotype are glycosylated in their Fc domain at a conserved asparagine at position 297. Removal of the core fucose of this glycan greatly increases the affinity for FcγRIII, resulting in enhanced FcγRIII-mediated effector functions. Normal plasma IgG contains ∼94% fucosylated Abs, but alloantibodies against, for example, Rhesus D (RhD) and platelet Ags frequently have reduced fucosylation that enhances their pathogenicity. The increased FcγRIII-mediated effector functions have been put to use in various afucosylated therapeutic Abs in anticancer treatment. To test the functional consequences of Ab fucosylation, we produced V-gene-matched recombinant anti-RhD IgG Abs of the four different subclasses (IgG1-4) with and without core fucose (i.e., 20% fucose remaining). Binding to all human FcγR types and their functional isoforms was assessed with surface plasmon resonance. All hypofucosylated anti-RhD IgGs of all IgG subclasses indeed showed enhanced binding affinity for isolated FcγRIII isoforms, without affecting binding affinity to other FcγRs. In contrast, when testing hypofucosylated anti-RhD Abs with FcγRIIIa-expressing NK cells, a 12- and 7-fold increased erythrocyte lysis was observed with the IgG1 and IgG3, respectively, but no increase with IgG2 and IgG4 anti-RhD Abs. Notably, none of the hypofucosylated IgGs enhanced effector function of macrophages, which, in contrast to NK cells, express a complex set of FcγRs, including FcγRIIIa. Our data suggest that the beneficial effects of afucosylated biologicals for clinical use can be particularly anticipated when there is a substantial involvement of FcγRIIIa-expressing cells, such as NK cells.
[Mh] Termos MeSH primário: Fucose/química
Imunoglobulina G/química
Imunoglobulina G/imunologia
Receptores de IgG/imunologia
[Mh] Termos MeSH secundário: Citotoxicidade Celular Dependente de Anticorpos
Fucose/imunologia
Fucose/metabolismo
Proteínas Ligadas por GPI/química
Proteínas Ligadas por GPI/genética
Proteínas Ligadas por GPI/imunologia
Glicosilação
Seres Humanos
Fragmentos Fc das Imunoglobulinas/química
Fragmentos Fc das Imunoglobulinas/imunologia
Imunoglobulina G/isolamento & purificação
Imunoglobulina G/metabolismo
Células Matadoras Naturais/imunologia
Macrófagos/imunologia
Ligação Proteica
Receptores de IgG/química
Receptores de IgG/genética
Sistema do Grupo Sanguíneo Rh-Hr/imunologia
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FCGR3A protein, human); 0 (FCGR3B protein, human); 0 (GPI-Linked Proteins); 0 (Immunoglobulin Fc Fragments); 0 (Immunoglobulin G); 0 (Receptors, IgG); 0 (Rh-Hr Blood-Group System); 0 (Rho(D) antigen); 28RYY2IV3F (Fucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700116


  9 / 4806 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  10 / 4806 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28509333
[Au] Autor:Stümer J; Biermann MHC; Knopf J; Magorivska I; Kastbom A; Svärd A; Janko C; Bilyy R; Schett G; Sjöwall C; Herrmann M; Muñoz LE
[Ad] Endereço:Friedrich-Alexander-University Erlangen-Nürnberg (FAU), Department of Internal Medicine 3, Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.
[Ti] Título:Altered glycan accessibility on native immunoglobulin G complexes in early rheumatoid arthritis and its changes during therapy.
[So] Source:Clin Exp Immunol;189(3):372-382, 2017 Sep.
[Is] ISSN:1365-2249
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The goal of this study was to investigate the glycosylation profile of native immunoglobulin (Ig)G present in serum immune complexes in patients with rheumatoid arthritis (RA). To accomplish this, lectin binding assays, detecting the accessibility of glycans present on IgG-containing immune complexes by biotinylated lectins, were employed. Lectins capturing fucosyl residues (AAL), fucosylated tri-mannose N-glycan core sites (LCA), terminal sialic acid residues (SNA) and O-glycosidically linked galactose/N-acetylgalactosamine (GalNac-L) were used. Patients with recent-onset RA at baseline and after 3-year follow-up were investigated. We found that native IgG was complexed significantly more often with IgM, C1q, C3c and C-reactive protein (CRP) in RA patients, suggesting alterations of the native structure of IgG. The total accessibility of fucose residues on captured immune complexes to the respective lectin was significantly higher in patients with RA. Moreover, fucose accessibility on IgG-containing immune complexes correlated positively with the levels of antibodies to cyclic citrullinated peptides (anti-CCP). We also observed a significantly higher accessibility to sialic acid residues and galactose/GalNAc glyco-epitopes in native complexed IgG of patients with RA at baseline. While sialic acid accessibility increased during treatment, the accessibility of galactose/GalNAc decreased. Hence, successful treatment of RA was associated with an increase in the SNA/GalNAc-L ratio. Interestingly, the SNA/GalNAc-L ratio in particular rises after glucocorticoid treatment. In summary, this study shows the exposure of glycans in native complexed IgG of patients with early RA, revealing particular glycosylation patterns and its changes following pharmaceutical treatment.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/imunologia
Artrite Reumatoide/imunologia
Imunoglobulina G/imunologia
Imunoglobulina M/imunologia
Polissacarídeos/química
Polissacarídeos/imunologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Complexo Antígeno-Anticorpo/química
Artrite Reumatoide/terapia
Proteína C-Reativa/imunologia
Proteína C-Reativa/metabolismo
Complemento C1q/imunologia
Complemento C1q/metabolismo
Complemento C3c/imunologia
Complemento C3c/metabolismo
Feminino
Fucose/metabolismo
Galactose/metabolismo
Glicosilação
Seres Humanos
Imunoglobulina A/imunologia
Imunoglobulina A/metabolismo
Imunoglobulina G/química
Imunoglobulina G/metabolismo
Imunoglobulina M/metabolismo
Lectinas/metabolismo
Masculino
Meia-Idade
Polissacarídeos/metabolismo
Sambucus nigra
Ácidos Siálicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Immunoglobulin A); 0 (Immunoglobulin G); 0 (Immunoglobulin M); 0 (Lectins); 0 (Polysaccharides); 0 (Sialic Acids); 0 (lectin, Aleuria aurantia); 28RYY2IV3F (Fucose); 80295-33-6 (Complement C1q); 80295-44-9 (Complement C3c); 9007-41-4 (C-Reactive Protein); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1710
[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:10.1111/cei.12987



página 1 de 481 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde