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[PMID]:28842487
[Au] Autor:Song K; Fu J; Song J; Herzog BH; Bergstrom K; Kondo Y; McDaniel JM; McGee S; Silasi-Mansat R; Lupu F; Chen H; Bagavant H; Xia L
[Ad] Endereço:From the Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104.
[Ti] Título:Loss of mucin-type -glycans impairs the integrity of the glomerular filtration barrier in the mouse kidney.
[So] Source:J Biol Chem;292(40):16491-16497, 2017 Oct 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The kidney's filtration activity is essential for removing toxins and waste products from the body. The vascular endothelial cells of the glomerulus are fenestrated, flattened, and surrounded by podocytes, specialized cells that support glomerular endothelial cells. Mucin-type core 1-derived glycans ( -glycans) are highly expressed on both glomerular capillary endothelial cells and their supporting podocytes, but their biological role is unclear. Biosynthesis of core 1-derived -glycans is catalyzed by the glycosyltransferase core 1 ß1,3-galactosyltransferase (C1galt1). Here we report that neonatal or adult mice with inducible deletion of ( ) exhibit spontaneous proteinuria and rapidly progressing glomerulosclerosis. Ultrastructural analysis of the glomerular filtration barrier components revealed that loss of -glycans results in altered podocyte foot processes. Further analysis indicated that -glycan is essential for the normal signaling function of podocalyxin, a podocyte foot process-associated glycoprotein. Our results reveal a new function of -glycosylation in the integrity of the glomerular filtration barrier.
[Mh] Termos MeSH primário: Galactosiltransferases/metabolismo
Mucinas
Podócitos/metabolismo
Polissacarídeos/metabolismo
Sialoglicoproteínas/metabolismo
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Galactosiltransferases/genética
Camundongos
Camundongos Knockout
Polissacarídeos/genética
Sialoglicoproteínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mucins); 0 (Polysaccharides); 0 (Sialoglycoproteins); 0 (podocalyxin); EC 2.4.1.- (C1galt1 protein, mouse); EC 2.4.1.- (Galactosyltransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798512


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[PMID]:28787006
[Au] Autor:Chen WA; Zhang J; Hall KM; Martin CB; Kisselev S; Dasen EJ; Vahanian NN; Link CJ; Martin BK
[Ad] Endereço:NewLink Genetics Corp., Ames, Iowa, United States of America.
[Ti] Título:Addition of αGal HyperAcute™ technology to recombinant avian influenza vaccines induces strong low-dose antibody responses.
[So] Source:PLoS One;12(8):e0182683, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Highly pathogenic avian influenza represents a severe public health threat. Over the last decade, the demand for highly efficacious vaccines against avian influenza viruses has grown, especially after the 2013 H7N9 outbreak in China that resulted in over 600 human cases with over 200 deaths. Currently, there are several H5N1 and H7N9 influenza vaccines in clinical trials, all of which employ traditional oil-in-water adjuvants due to the poor immunogenicity of avian influenza virus antigens. In this study, we developed potent recombinant avian influenza vaccine candidates using HyperAcute™ Technology, which takes advantage of naturally-acquired anti-αGal immunity in humans. We successfully generated αGal-positive recombinant protein and virus-like particle vaccine candidates of H5N1 and H7N9 influenza strains using either biological or our novel CarboLink chemical αGal modification techniques. Strikingly, two doses of 100 ng αGal-modified vaccine, with no traditional adjuvant, was able to induce a much stronger humoral response in αGT BALB/c knockout mice (the only experimental system readily available for testing αGal in vivo) than unmodified vaccines even at 10-fold higher dose (1000 ng/dose). Our data strongly suggest that αGal modification significantly enhances the humoral immunogenicity of the recombinant influenza vaccine candidates. Use of αGal HyperAcute™ technology allows significant dose-sparing while retaining desired immunogenicity. Our success in the development of highly potent H5N1 and H7N9 vaccine candidates demonstrated the potential of αGal HyperAcute™ technology for the development of vaccines against other infectious diseases.
[Mh] Termos MeSH primário: Anticorpos Antivirais/imunologia
Vírus da Influenza A Subtipo H5N1/imunologia
Vírus da Influenza A Subtipo H7N9/imunologia
Vacinas contra Influenza/genética
Vacinas contra Influenza/imunologia
Vacinas Sintéticas/genética
Vacinas Sintéticas/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Epitopos/imunologia
Feminino
Galactosiltransferases/deficiência
Galactosiltransferases/genética
Técnicas de Inativação de Genes
Imunidade Humoral/imunologia
Vacinas contra Influenza/química
Camundongos
Camundongos Endogâmicos BALB C
Vacinas Sintéticas/química
Vacinas de Partículas Semelhantes a Vírus/genética
Vacinas de Partículas Semelhantes a Vírus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Epitopes); 0 (Influenza Vaccines); 0 (Vaccines, Synthetic); 0 (Vaccines, Virus-Like Particle); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.133 (alpha 1,3 galactosyltransferase, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182683


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[PMID]:28715486
[Au] Autor:Gao B; Long C; Lee W; Zhang Z; Gao X; Landsittel D; Ezzelarab M; Ayares D; Huang Y; Cooper DKC; Wang Y; Hara H
[Ad] Endereço:Thomas E. Starzl Transplantation Institute, University of Pittsburgh, Pittsburgh, PA, United States of America.
[Ti] Título:Anti-Neu5Gc and anti-non-Neu5Gc antibodies in healthy humans.
[So] Source:PLoS One;12(7):e0180768, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Our group previously investigated the levels of anti-Gal and anti-nonGal IgM and IgG in a cohort of 75 healthy humans of various backgrounds, and found some significant differences related to factors such as age, gender, ABO blood group, diet, vaccination history, and geographic location during childhood. We have now expanded our cohort (n = 84) to investigate the levels of anti-Neu5Gc and anti-nonGal/nonNeu5Gc antibodies in healthy humans. Anti-nonGal and anti-nonGal/nonNeu5Gc human IgM and IgG binding to pRBCs and pAECs from GTKO/CD46 and GTKO/CD46/Neu5GcKO pigs were measured by flow cytometry. Anti-Gal and anti-Neu5Gc IgM and IgG levels were measured by ELISA. In summary, (i) the great majority (almost 100%) of humans had anti-Neu5Gc IgM and IgG antibodies that bound to pAECs and approximately 50% had anti-Neu5Gc antibodies that bound to pRBCs, (ii) there was significantly less human antibody binding to pig cells that did not express either Gal or Neu5Gc compared with those that did not express Gal alone, (iii) the levels of both IgM and IgG binding to GTKO/CD46/Neu5GcKO pRBCs and pAECs were low, (iv) the level of anti-Neu5Gc IgG was higher in men than women, (v) the level did not change with age or diet, and there was some variability associated with (vi) previous vaccination history and (vii) the geographic region in which the individual spent his or her childhood. Our study confirms that human antibody binding to RBCs and AECs from GTKO/CD46/Neu5GcKO pigs is greatly reduced compared to binding to GTKO/CD46 cells. However, all humans appear to have a low level of antibody that binds to pAECs that is not directed to either Gal or Neu5Gc. Our findings require consideration in planning clinical trials of xenotransplantation.
[Mh] Termos MeSH primário: Anticorpos/imunologia
Ácidos Neuramínicos/imunologia
[Mh] Termos MeSH secundário: Sistema do Grupo Sanguíneo ABO
Adulto
Idoso
Idoso de 80 Anos ou mais
Animais
Anticorpos/sangue
Células Cultivadas
Dieta
Células Endoteliais/citologia
Células Endoteliais/imunologia
Células Endoteliais/metabolismo
Eritrócitos/citologia
Eritrócitos/imunologia
Eritrócitos/metabolismo
Feminino
Galactose/metabolismo
Galactosiltransferases/deficiência
Galactosiltransferases/genética
Seres Humanos
Imunoglobulina G/sangue
Imunoglobulina G/imunologia
Imunoglobulina M/sangue
Imunoglobulina M/imunologia
Masculino
Proteína Cofatora de Membrana/metabolismo
Meia-Idade
Oxigenases de Função Mista/deficiência
Oxigenases de Função Mista/genética
Suínos
Vacinação
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABO Blood-Group System); 0 (Antibodies); 0 (Immunoglobulin G); 0 (Immunoglobulin M); 0 (Membrane Cofactor Protein); 0 (Neuraminic Acids); 1113-83-3 (N-glycolylneuraminic acid); EC 1.- (Mixed Function Oxygenases); EC 1.14.18.2 (CMPacetylneuraminate monooxygenase); EC 2.4.1.- (Galactosyltransferases); X2RN3Q8DNE (Galactose)
[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:170718
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180768


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[PMID]:28708980
[Au] Autor:Shi C; Xu X; Yu X; Du Z; Luan X; Liu D; Hu T
[Ad] Endereço:Department of Immunology, Binzhou Medical University, Yantai, PR China.
[Ti] Título:CD3/CD28 dynabeads induce expression of tn antigen in human t cells accompanied by hypermethylation of the cosmc promoter.
[So] Source:Mol Immunol;90:98-105, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycosylation is an important protein post-translational modification. In this process, the intermediate product, Tn antigen, arises from somatic mutations in core1ß3-galactosyltransferase-specific molecular chaperone (Cosmc), which is required for the formation of active core1ß3-galactosyltransferase (T-synthase). As a type of tumor-associated carbohydrate antigen, Tn antigen is mainly expressed in many human tumor cells and is absent in normal cells. Surprisingly, it is also expressed in normal activated T cells after in vitro stimulation, but the mechanism underlying its expression remains unclear. This study demonstrated that Tn antigen was expressed in activated T cells and that the percentage of positive (Tn ) cells increased and subsequently decreased within 72h after stimulation with CD3/CD28 Dynabeads, with peak expression occurring at 48h. During activation, interleukin-4 (IL-4) expression in the T-cell supernatant consistently increased with Tn cells, and was inversely correlated with serum interferon gamma (IFN-γ) levels. Compared with unactivated (without CD3/CD28 Dynabead stimulation) T cells, the level of T-synthase transcription in activated T cells did not significantly change, whereas T-synthase activity and Cosmc transcription significantly decreased, accompanied by a further increase in methylation of the Cosmc promoter. The results also showed that Cosmc transcription and translation decreased and then increased, and that Cosmc promoter methylation was a dynamic process during T cell activation. These data suggest that hypermethylation of the Cosmc promoter may induce the expression of Tn antigen in activated T cells.
[Mh] Termos MeSH primário: Antígenos Glicosídicos Associados a Tumores/biossíntese
Chaperonas Moleculares/genética
Regiões Promotoras Genéticas/genética
Fator de Transcrição Sp1/metabolismo
Fator de Transcrição Sp3/metabolismo
Linfócitos T/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Antígenos CD28/imunologia
Complexo CD3/imunologia
Células Cultivadas
Metilação de DNA
Galactosiltransferases/biossíntese
Glicosilação
Seres Humanos
Interferon gama/sangue
Interleucina-4/biossíntese
Ativação Linfocitária/imunologia
Microesferas
Linfócitos T/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Tumor-Associated, Carbohydrate); 0 (C1GALT1C1 protein, human); 0 (CD28 Antigens); 0 (CD3 Complex); 0 (IL4 protein, human); 0 (Molecular Chaperones); 0 (SP3 protein, human); 0 (Sp1 Transcription Factor); 0 (Sp1 protein, human); 0 (Tn antigen); 148710-94-5 (Sp3 Transcription Factor); 207137-56-2 (Interleukin-4); 82115-62-6 (Interferon-gamma); EC 2.4.1.- (C1GALT1 protein, human); EC 2.4.1.- (Galactosyltransferases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE


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[PMID]:28604971
[Au] Autor:Wang B; Shi L; Wang L; Liu Y; Ma L; Zhang R
[Ad] Endereço:The Second Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu 210011, China. lyc60@126.com.
[Ti] Título:[A case of Bw39 subtype caused by 562C to T mutation of exon 7 of α -1,3-D-galactosyltransferase gene].
[So] Source:Zhonghua Yi Xue Yi Chuan Xue Za Zhi;34(3):427-430, 2017 Jun 10.
[Is] ISSN:1003-9406
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To analyze a sample with ABO subgroup using serological and molecular methods. METHODS: The ABO phenotype of the sample was determined with a tube method, and the activity of glycosyltransferases was determined with an uridine diphosphate galactose transferring method. The ABO gene of the propositus was identified by PCR with sequence-specific primers (PCR-SSP). In addition, exons 6 and 7 of the ABO gene were cloned and sequenced. RESULTS: Neither A nor B antigen was identified in the propositus, despite that its anti-B antibody was found to be attenuated. No activity of α -1, 3-D-galactosyltransferase was detected in the serum. The presence of B and O alleles were confirmed by PCR-SSP, and a novel mutation (562C to T) of the exon 7 was confirmed by sequencing, which has led to an amino acid substitution (Arg to Cys) at position 188. The genotype of the propositus was determined as Bnew/O. CONCLUSION: A novel B allele has been identified, which was named as Bw39 by the Blood Group Antigen Gene Mutation Database (BGMUT).
[Mh] Termos MeSH primário: Galactosiltransferases/genética
Mutação Puntual
[Mh] Termos MeSH secundário: Sistema do Grupo Sanguíneo ABO/genética
Adulto
Alelos
Substituição de Aminoácidos
Sequência de Bases
Éxons
Seres Humanos
Masculino
Dados de Sequência Molecular
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABO Blood-Group System); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.87 (N-acetyllactosaminide alpha-1,3-galactosyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1003-9406.2017.03.026


  6 / 3045 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


  7 / 3045 MEDLINE  
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[PMID]:28550913
[Au] Autor:Butler JR; Santos RMN; Martens GR; Ladowski JM; Wang ZY; Li P; Tector M; Tector AJ
[Ad] Endereço:Department of Surgery, Indiana University School of Medicine, Indianapolis, Indiana.
[Ti] Título:Efficient generation of targeted and controlled mutational events in porcine cells using nuclease-directed homologous recombination.
[So] Source:J Surg Res;212:238-245, 2017 May 15.
[Is] ISSN:1095-8673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Nuclease-based genome editing has rapidly sped the creation of new models of human disease. These techniques also hold great promise for the future of clinical xenotransplantation and cell-based therapies for cancer or immunodeficient pathology. However, to fully realize the potential of nuclease editing tools, the efficiency and precision of their application must be optimized. The object of this study was to use nonintegrating selection and nuclease-directed homologous recombination to efficiently control the genetic modification of the porcine genome. METHODS: Clustered randomly integrating spaced palindromic repeats and associated Cas9 protein (CRISPR/Cas9)-directed mutagenesis with a single-guide RNA target was designed to target the alpha-1,3-galactosyltransferase locus (GGTA1) of the porcine genome. A vector expressing a single-guide RNA, Cas9 protein, and green fluorescent protein was used to increase plasmid-delivered mutational efficiency when coupled with fluorescence sorting. Single and double-strand DNA oligonucleotides with a restriction site replacing the start codon were created with variable homology lengths surrounding the mutational event site. Finally, a transgene construct was flanked with 50 base pairs of homology directed immediately 5' to a nuclease cut site. These products were introduced to cells with a constant concentration of CRISPR/cas9 vector. Phenotype-specific mutational efficiency was measured by flow cytometer. Controlled homologous insertion was measured by Sanger sequence, restriction enzyme digest and flow cytometry. RESULTS: Expression of a fluorescence protein on the Cas9 vector functioned as a nonintegrating selection marker. Selection by this marker increased phenotype-silencing mutation rates from 3.5% to 82% (P = 0.0002). Insertion or deletion mutation increased from 11% to 96% (P = 0.0007). Co-transfection with homologous DNA oligonucleotides increased the aggregate phenotype-silencing mutation rates up to 22% and increased biallelic events. Single-strand DNA was twice as efficient as double-strand DNA. Furthermore, nuclease-mediated insertion by homology-directed repair successfully drove locus-specific transgene expression in the porcine genome. CONCLUSIONS: A nonintegrating selection strategy based on fluorescence expression can increase the mutational efficiency of the CRISPR/Cas9 system. The precision of this system can be increased by the addition of a very short homologous template sequence and can serve as a method for locus-specific transgene delivery. Together these strategies may be used to efficiently control mutational events. This system may be used to better use the potential of nuclease-mediated genomic editing.
[Mh] Termos MeSH primário: Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Endonucleases
Galactosiltransferases/genética
Edição de Genes/métodos
Recombinação Homóloga
Mutação
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.- (alpha-1,3-galactosyltransferase 1, porcine); EC 3.1.- (Endonucleases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


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[PMID]:28384485
[Au] Autor:Pastuch-Gawolek G; Plesniak M; Komor R; Byczek-Wyrostek A; Erfurt K; Szeja W
[Ad] Endereço:Department of Organic Chemistry, Bioorganic Chemistry and Biotechnology, Silesian University of Technology, B. Krzywoustego 4, 44-100 Gliwice, Poland; Biotechnology Centre, Silesian University of Technology, Krzywoustego 8, 44-100 Gliwice, Poland. Electronic address: gabriela.pastuch@polsl.pl.
[Ti] Título:Synthesis and preliminary biological assay of uridine glycoconjugate derivatives containing amide and/or 1,2,3-triazole linkers.
[So] Source:Bioorg Chem;72:80-88, 2017 Jun.
[Is] ISSN:1090-2120
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A series of UDP-sugar analogues was synthesized and their preliminary biological activity was evaluated. Glycoconjugates of uridine 1 and 2 were synthesized by condensation of uridine-5'-carboxylic acid and 1-amino sugars derivatives of d-glucose and d-galactose, glycoconjugates 3 and 4 were synthesized by azide-alkyne 1,3-dipolar cycloaddition (CuAAC) of 1-azido sugars and propargylamide derivatives of uridine while glycoconjugates 5 and 6 were synthesized by CuAAC of propargyl ß-O-glycosides and 5'-azido uridine. Evaluation of inhibitory activity of compounds 1-6 against commercially available ß-1,4-galactosyltransferase I (ß4GalT) show that compound 5 inhibited the enzyme in µmolar range. Additionally, the antitumor activity of the obtained glycoconjugates 1-6 were tested using MTT assay.
[Mh] Termos MeSH primário: Amidas/farmacologia
Galactosiltransferases/antagonistas & inibidores
Glicoconjugados/farmacologia
Triazóis/farmacologia
Uridina/farmacologia
[Mh] Termos MeSH secundário: Amidas/química
Animais
Bovinos
Linhagem Celular
Relação Dose-Resposta a Droga
Galactosiltransferases/metabolismo
Glicoconjugados/síntese química
Glicoconjugados/química
Seres Humanos
Leite/enzimologia
Estrutura Molecular
Relação Estrutura-Atividade
Triazóis/química
Uridina/análogos & derivados
Uridina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amides); 0 (Glycoconjugates); 0 (Triazoles); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.- (beta-1,4-galactosyltransferase I); WHI7HQ7H85 (Uridine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE


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[PMID]:28330559
[Au] Autor:Xu Z; Wang M; Shi D; Zhou G; Niu T; Hahn MG; O'Neill MA; Kong Y
[Ad] Endereço:Key Laboratory for Tobacco Gene Resources, Tobacco Research Institute, Chinese Academy of Agricultural Sciences, Qingdao 266101, PR China; Graduate School of Chinese Academy of Agricultural Science, Beijing 100081, PR China. Electronic address: xuzc1110@163.com.
[Ti] Título:DGE-seq analysis of MUR3-related Arabidopsis mutants provides insight into how dysfunctional xyloglucan affects cell elongation.
[So] Source:Plant Sci;258:156-169, 2017 May.
[Is] ISSN:1873-2259
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Our previous study of the Arabidopsis mur3-3 mutant and mutant plants in which the mur3-3 phenotypes are suppressed (xxt2mur3-3, xxt5mur3-3, xxt1xxt2mur3-3 and 35Spro:XLT2:mur3-3) showed that hypocotyl cell elongation is decreased in plants that synthesize galactose-deficient xyloglucan. To obtain genome-wide insight into the transcriptome changes and regulatory networks that may be involved in this decreased elongation, we performed digital gene expression analyses of the etiolated hypocotyls of wild type (WT), mur3-3 and the four suppressor lines. Numerous differentially expressed genes (DEGs) were detected in comparisons between WT and mur3-3 (1423), xxt2mur3-3 and mur3-3 (675), xxt5mur3-3 and mur3-3 (1272), xxt1xxt2mur3-3 and mur3-3 (1197) and 35Spro:XLT2:mur3-3 vs mur3-3 (121). 550 overlapped DEGs were detected among WT vs mur3-3, xxt2mur3-3 vs mur3-3, xxt5mur3-3 vs mur3-3, and xxt1xxt2mur3-3 vs mur3-3 comparisons. These DEGs include 46 cell wall-related genes, 24 transcription factors, 6 hormone-related genes, 9 protein kinase genes and 9 aquaporin genes. The expression of all of the 550 overlapped genes is restored to near wild-type levels in the four mur3-3 suppressor lines. qRT-PCR of fifteen of these 550 genes showed that their expression levels are consistent with the digital gene expression data. Overexpression of some of these genes (XTH4, XTH30, PME3, EXPA11, MYB88, ROT3, AT5G37790, WAG2 and TIP2;3) that are down-regulated in mur3-3 partially rescued the short hypocotyl phenotype but not the aerial phenotype of mur3-3, indicating that different mechanisms exist between hypocotyl cell elongation and leaf cell elongation.
[Mh] Termos MeSH primário: Arabidopsis/genética
Crescimento Celular
Galactosiltransferases/fisiologia
Glucanos/fisiologia
[Mh] Termos MeSH secundário: Arabidopsis/metabolismo
Arabidopsis/fisiologia
Galactosiltransferases/genética
Perfilação da Expressão Gênica
Regulação da Expressão Gênica de Plantas/fisiologia
Glucanos/metabolismo
Mutação
Reação em Cadeia da Polimerase em Tempo Real
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (Xylans); 37294-28-3 (xyloglucan); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.- (MUR3 protein, Arabidopsis)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170519
[Lr] Data última revisão:
170519
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


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[PMID]:28320304
[Au] Autor:Pérez-Cruz M; Bello-Gil D; Costa C; Mañez R
[Ad] Endereço:Bellvitge Biomedical Research Institute (IDIBELL), Hospitalet de Llobregat, 08908, Spain.
[Ti] Título:Cytokine Profile Associated with Selective Removal of Natural Anti-αGal Antibodies in a Sepsis Model in Gal-KO Mice.
[So] Source:Biochemistry (Mosc);82(2):205-212, 2017 Feb.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Selective depletion of natural anti-Galα1-3Galß1-4GlcNAc (so-called anti-αGal) antibodies is achieved in α1,3-galactosyltransferase knockout (Gal-KO) mice by administration of the soluble glycoconjugate of αGal GAS914. This molecule removed up to 90% of natural circulating anti-αGal antibodies without causing unspecific production of cytokines in wild-type (CBA) and Gal-KO mice. However, the removal of anti-αGal antibodies in Gal-KO mice with GAS914 in the context of sepsis after cecal ligation and puncture (CLP) was associated with a significant increase in the production of leptin, CXLC1, CXLC13, and TIMP-1 cytokines compared to vehicle (PBS)-treated controls. Despite the current lack of understanding of the underlying mechanism, our data suggest a putative role of natural anti-αGal antibodies in the regulation of some cytokines during sepsis.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Citocinas/sangue
Galactosiltransferases/deficiência
Sepse/sangue
Trissacarídeos/farmacologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Camundongos
Camundongos Knockout
Sepse/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Cytokines); 0 (Trisaccharides); 0 (alpha-galactosyl epitope); EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.133 (alpha 1,3 galactosyltransferase, mouse)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170322
[Lr] Data última revisão:
170322
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917020122



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