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Pesquisa : D08.811.277.450.483.044 [Categoria DeCS]
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[PMID]:28546425
[Au] Autor:Sato M; Liebschner D; Yamada Y; Matsugaki N; Arakawa T; Wills SS; Hattie M; Stubbs KA; Ito T; Senda T; Ashida H; Fushinobu S
[Ad] Endereço:From the Department of Biotechnology, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
[Ti] Título:The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors.
[So] Source:J Biol Chem;292(29):12126-12138, 2017 Jul 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The α- -acetylgalactosaminidase from the probiotic bacterium (NagBb) belongs to the glycoside hydrolase family 129 and hydrolyzes the glycosidic bond of Tn-antigen (GalNAcα1-Ser/Thr). NagBb is involved in assimilation of -glycans on mucin glycoproteins by in the human gastrointestinal tract, but its catalytic mechanism has remained elusive because of a lack of sequence homology around putative catalytic residues and of other structural information. Here we report the X-ray crystal structure of NagBb, representing the first GH129 family structure, solved by the single-wavelength anomalous dispersion method based on sulfur atoms of the native protein. We determined ligand-free, GalNAc, and inhibitor complex forms of NagBb and found that Asp-435 and Glu-478 are located in the catalytic domain at appropriate positions for direct nucleophilic attack at the anomeric carbon and proton donation for the glycosidic bond oxygen, respectively. A highly conserved Asp-330 forms a hydrogen bond with the O4 hydroxyl of GalNAc in the -1 subsite, and Trp-398 provides a stacking platform for the GalNAc pyranose ring. Interestingly, a metal ion, presumably Ca , is involved in the recognition of the GalNAc -acetyl group. Mutations at Asp-435, Glu-478, Asp-330, and Trp-398 and residues involved in metal coordination (including an all-Ala quadruple mutant) significantly reduced the activity, indicating that these residues and the metal ion play important roles in substrate recognition and catalysis. Interestingly, NagBb exhibited some structural similarities to the GH101 endo-α- -acetylgalactosaminidases, but several critical differences in substrate recognition and reaction mechanism account for the different activities of these two enzymes.
[Mh] Termos MeSH primário: Acetilgalactosamina/metabolismo
Proteínas de Bactérias/metabolismo
Bifidobacterium bifidum/enzimologia
Coenzimas/metabolismo
Glicosídeo Hidrolases/metabolismo
Metais/metabolismo
alfa-N-Acetilgalactosaminidase/metabolismo
[Mh] Termos MeSH secundário: Acetilgalactosamina/química
Sequência de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação
Domínio Catalítico
Coenzimas/química
Sequência Conservada
Cristalografia por Raios X
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/farmacologia
Glicosídeo Hidrolases/antagonistas & inibidores
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/genética
Ligantes
Metais/química
Modelos Moleculares
Mutagênese Sítio-Dirigida
Mutação
Probióticos
Conformação Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Alinhamento de Sequência
Homologia Estrutural de Proteína
alfa-N-Acetilgalactosaminidase/antagonistas & inibidores
alfa-N-Acetilgalactosaminidase/química
alfa-N-Acetilgalactosaminidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Enzyme Inhibitors); 0 (Ligands); 0 (Metals); 0 (Recombinant Fusion Proteins); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase); KM15WK8O5T (Acetylgalactosamine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.777391


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[PMID]:28545388
[Au] Autor:Rashid MH; Sadik G; Alam AK; Tanaka T
[Ad] Endereço:Institute of Biological Science, University of Rajshahi, Rajshahi, 6205, Bangladesh.
[Ti] Título:Chemical and structural characterization of α-N-acetylgalactosaminidase I and II from starfish, asterina amurensis.
[So] Source:BMC Biochem;18(1):9, 2017 May 25.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The marine invertebrate starfish was found to contain a novel α-N-acetylgalactosaminidase, α-GalNAcase II, which catalyzes removal of terminal α-N-acetylgalactosamine (α-GalNAc), in addition to a typical α-N-acetylgalactosaminidase, α-GalNAcase I, which catalyzes removal of terminal α-N-acetylgalactosamine (α-GalNAc) and, to a lesser extent, galactose. The interrelationship between α-GalNAcase I and α-GalNAcase II and the molecular basis of their differences in substrate specificity remain unknown. RESULTS: Chemical and structural comparisons between α-GalNAcase I and II using immunostaining, N-terminal amino acid sequencing and peptide analysis showed high homology to each other and also to other glycoside hydrolase family (GHF) 27 members. The amino acid sequence of peptides showed conserved residues at the active site as seen in typical α-GalNAcase. Some substitutions of conserved amino acid residues were found in α-GalNAcase II that were located near catalytic site. Among them G171 and A173, in place of C171 and W173, respectively in α-GalNAcase were identified to be responsible for lacking intrinsic α-galactosidase activity of α-GalNAcase II. Chemical modifications supported the presence of serine, aspartate and tryptophan as active site residues. Two tryptophan residues (W16 and W173) were involved in α-galactosidase activity, and one (W16) of them was involved in α-GalNAcase activity. CONCLUSIONS: The results suggested that α-GalNAcase I and II are closely related with respect to primary and higher order structure and that their structural differences are responsible for difference in substrate specificities.
[Mh] Termos MeSH primário: Asterina/enzimologia
alfa-N-Acetilgalactosaminidase/química
[Mh] Termos MeSH secundário: Animais
Domínio Catalítico
Dados de Sequência Molecular
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
alfa-Galactosidase/metabolismo
alfa-N-Acetilgalactosaminidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.22 (alpha-Galactosidase); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0085-1


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[PMID]:27907862
[Au] Autor:Zoga M; Nikou T; Ioannidis A; Tzavellas E; Paparrigopoulos T; Lambrokostopoulos KT; Vasdekis VG; Magana M; Chatzipanagiotou S
[Ad] Endereço:Athens Medical School, Aeginition Hospital, Department of Biopathology and Clinical Microbiology, National and Kapodistrian University of Athens, Greece.
[Ti] Título:Alteration of α-N-acetylgalactosaminidase (nagalase) concentration in alcohol-dependent individuals without liver disease, during the detoxification therapy.
[So] Source:Drug Alcohol Depend;170:147-151, 2017 Jan 01.
[Is] ISSN:1879-0046
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The present study aimed to investigate for the first time, the alteration of α-N-acetylgalactosaminidase (nagalase) concentration in alcohol-dependent individuals without liver disease, before, during and at the end of the detoxification therapy. METHODS: Forty-eight alcohol-dependent individuals without liver disease who were admitted for alcohol detoxification, and eighty-four healthy controls participated in this study. Patients' blood was obtained upon admission, two weeks later and after the completion of the detoxification period (4-5 weeks). Nagalase concentration in serum was assessed by enzyme-linked immunosorbent assay. RESULTS: Nagalase concentration was significantly elevated in the patient samples in all serum collections as compared to the normal controls, with a progressive fall from admission to discharge (p-value<0.001). Values differed significantly among the three time points, with a net shift to decrease, but remained still high, above normal control level at the end of the therapy. No significant correlations were detected among the nagalase levels and the liver enzymes values. Moreover, no significant correlation was found between the alterations of nagalase concentrations and the amount of consumed alcohol. CONCLUSIONS: The high nagalase concentrations in alcohol abuse might be associated with macrophage impairment through decreasing the endogenous macrophage-activating factor (MAF) production by Gc-protein. The possible pathogenetic association between nagalase activity and alcohol overconsumption remains a matter of further investigation. Nagalase could also serve as a marker of alcohol overconsumption for the evaluation of alcohol-dependent individuals before, as well as during the detoxification therapy.
[Mh] Termos MeSH primário: Alcoolismo/sangue
alfa-N-Acetilgalactosaminidase/sangue
[Mh] Termos MeSH secundário: Adulto
Alcoolismo/tratamento farmacológico
Diazepam/uso terapêutico
Ensaio de Imunoadsorção Enzimática
Feminino
Moduladores GABAérgicos/uso terapêutico
Seres Humanos
Fatores Ativadores de Macrófagos/sangue
Masculino
Meia-Idade
Terapêutica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GABA Modulators); 0 (Macrophage-Activating Factors); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase); Q3JTX2Q7TU (Diazepam)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE


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[PMID]:27503803
[Au] Autor:Borges CR; Rehder DS
[Ad] Endereço:School of Molecular Sciences, Arizona State University, Tempe, AZ 85287, USA; The Biodesign Institute at Arizona State University, Tempe, AZ 85287, USA. Electronic address: chad.borges@asu.edu.
[Ti] Título:Glycan structure of Gc Protein-derived Macrophage Activating Factor as revealed by mass spectrometry.
[So] Source:Arch Biochem Biophys;606:167-79, 2016 Sep 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Disagreement exists regarding the O-glycan structure attached to human vitamin D binding protein (DBP). Previously reported evidence indicated that the O-glycan of the Gc1S allele product is the linear core 1 NeuNAc-Gal-GalNAc-Thr trisaccharide. Here, glycan structural evidence is provided from glycan linkage analysis and over 30 serial glycosidase-digestion experiments which were followed by analysis of the intact protein by electrospray ionization mass spectrometry (ESI-MS). Results demonstrate that the O-glycan from the Gc1F protein is the same linear trisaccharide found on the Gc1S protein and that the hexose residue is galactose. In addition, the putative anti-cancer derivative of DBP known as Gc Protein-derived Macrophage Activating Factor (GcMAF, which is formed by the combined action of ß-galactosidase and neuraminidase upon DBP) was analyzed intact by ESI-MS, revealing that the activating E. coli ß-galactosidase cleaves nothing from the protein-leaving the glycan structure of active GcMAF as a Gal-GalNAc-Thr disaccharide, regardless of the order in which ß-galactosidase and neuraminidase are applied. Moreover, glycosidase digestion results show that α-N-Acetylgalactosamindase (nagalase) lacks endoglycosidic function and only cleaves the DBP O-glycan once it has been trimmed down to a GalNAc-Thr monosaccharide-precluding the possibility of this enzyme removing the O-glycan trisaccharide from cancer-patient DBP in vivo.
[Mh] Termos MeSH primário: Fatores Ativadores de Macrófagos/química
Polissacarídeos/química
[Mh] Termos MeSH secundário: Alelos
Dissacarídeos/química
Escherichia coli/enzimologia
Glicosídeo Hidrolases/química
Glicosídeos/química
Glicosilação
Seres Humanos
Ativação de Macrófagos
Manose/química
Neuraminidase/química
Espectrometria de Massas por Ionização por Electrospray
Ácido Trifluoracético/química
Trissacarídeos/química
Proteína de Ligação a Vitamina D/química
alfa-N-Acetilgalactosaminidase/química
beta-Galactosidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disaccharides); 0 (Glycosides); 0 (Macrophage-Activating Factors); 0 (Polysaccharides); 0 (Trisaccharides); 0 (Vitamin D-Binding Protein); 0 (vitamin D-binding protein-macrophage activating factor); E5R8Z4G708 (Trifluoroacetic Acid); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.18 (Neuraminidase); EC 3.2.1.23 (beta-Galactosidase); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase); PHA4727WTP (Mannose)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE


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[PMID]:26112363
[Au] Autor:Ding JC; Wang ZL
[Ad] Endereço:Department of Plastic Surgery at the Xuzhou Central Hospital, Xuzhou, China - djicun@126.com.
[Ti] Título:Clinical significance of joint detection of mALB and NAG for early kidney damage in burn patients.
[So] Source:Minerva Chir;71(3):168-72, 2016 Jun.
[Is] ISSN:1827-1626
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The aim of this study was to study the clinical significance of joint detection of mALB and NAG in early kidney damage in burn patients. METHODS: Forty-five burn patients of different degrees were selected and divided into mild, moderate, severe, and heavy burns, and normal healthy controls according to their severity. Their b2- macroglobulin (b2-MG), a1-macroglobulin (a1-MG), mALB and N-acetyl-b-D-NAG were tested for 3 days, 1 week, 2 weeks, 4 weeks after the burn, respectively. RESULTS: The urine concentration change b2-MG, a1-MG, MALB, and NAG are related to the area, depth and degree of the burn. The more serious the burn is, the higher the levels of mALB and NAG (P<0.001 or P<0.01) is. CONCLUSIONS: Early detection of mALB and NAG is helpful for early kidney damage diagnosis in burn patients to prevent further complications.
[Mh] Termos MeSH primário: Queimaduras/complicações
Nefropatias/diagnóstico
Nefropatias/urina
Proteínas de Neoplasias/urina
alfa-N-Acetilgalactosaminidase/urina
[Mh] Termos MeSH secundário: Adolescente
Adulto
Biomarcadores/urina
Criança
Pré-Escolar
Feminino
Seres Humanos
Nefropatias/etiologia
Nefropatias/metabolismo
Masculino
Meia-Idade
Valor Preditivo dos Testes
Prognóstico
Sensibilidade e Especificidade
Índice de Gravidade de Doença
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (NAG protein, human); 0 (Neoplasm Proteins); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150627
[St] Status:MEDLINE


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[PMID]:26443390
[Au] Autor:Sarbu M; Zhu F; Peter-Katalinic J; Clemmer DE; Zamfir AD
[Ad] Endereço:West University of Timisoara, Romania.
[Ti] Título:Application of ion mobility tandem mass spectrometry to compositional and structural analysis of glycopeptides extracted from the urine of a patient diagnosed with Schindler disease.
[So] Source:Rapid Commun Mass Spectrom;29(21):1929-37, 2015 Nov 15.
[Is] ISSN:1097-0231
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RATIONALE: Schindler disease is caused by the deficient activity of α-N-acetylgalactosaminidase, which leads to an abnormal accumulation of O-glycopeptides in tissues and body fluids. In this work the Schindler condition is for the first time approached by ion mobility (IMS) tandem mass spectrometry (MS/MS), for determining urine glycopeptide fingerprints and discriminate isomeric structures. METHODS: IMS-MS experiments were conducted on a Synapt G2s mass spectrometer operating in negative ion mode. A glycopeptide mixture extracted from the urine of a patient suffering from Schindler disease was dissolved in methanol and infused into the mass spectrometer by electrospray ionization using a syringe-pump system. MS/MS was performed by collision-induced dissociation (CID) at low energies, after mobility separation in the transfer cell. Data acquisition and processing were performed using MassLynx and Waters Driftscope software. RESULTS: IMS-MS data indicated that the attachment of one or two amino acids to the carbohydrate backbone has a minimal influence on the molecule conformation, which limits the discrimination of the free oligosaccharides from the glycosylated amino acids and dipeptides. The structural analysis by CID MS/MS in combination with IMS-MS of species exhibiting the same m/z but different configurations demonstrated for the first time the presence of positional isomers for some of the Schindler disease biomarker candidates. CONCLUSIONS: The IMS-MS and CID MS/MS platform was for the first time optimized and applied to Schindler disease glycourinome. By this approach the separation and characterization of Neu5Ac positional isomers was possible. IMS CID MS/MS showed the ability to determine the type of the glycopeptide isomers from a series of possible candidates.
[Mh] Termos MeSH primário: Glicopeptídeos/química
Glicopeptídeos/urina
Doenças por Armazenamento dos Lisossomos/urina
Distrofias Neuroaxonais/urina
Espectrometria de Massas em Tandem/métodos
alfa-N-Acetilgalactosaminidase/deficiência
[Mh] Termos MeSH secundário: Pré-Escolar
Seres Humanos
Isomerismo
Masculino
alfa-N-Acetilgalactosaminidase/urina
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycopeptides); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:151007
[Lr] Data última revisão:
151007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151008
[St] Status:MEDLINE
[do] DOI:10.1002/rcm.7288


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[PMID]:26268136
[Au] Autor:Nagdas SK; Smith L; Mcnamara A; Hernandez-Encarnacion L; Medina-Ortiz I
[Ad] Endereço:Department of Chemistry and Physics, Fayetteville State University, 1200 Murchison Road, Fayetteville, NC, 28301, USA. snagdas@uncfsu.edu.
[Ti] Título:Identification and characterization of a bovine sperm acrosomal matrix protein and its mechanism of interaction with acrosomal hydrolases.
[So] Source:Mol Cell Biochem;410(1-2):11-23, 2015 Dec.
[Is] ISSN:1573-4919
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Fertilization, the union of male and female gametes to create offspring, is an intricate biological process dependent upon several biochemical and physiological events. Our understanding of the functions of protein constituents of the outer acrosomal membrane-associated matrix complex (OMC) is limited. A highly purified OMC fraction isolated from bovine cauda sperm heads comprised 54, 50, 45, and 38-19 kDa polypeptides. The objective of this study is to identify and characterize the 45 kDa (OMC45) polypeptide, to define its role in binding acrosomal hydrolases, and to examine the fate of OMC45 polypeptide during the acrosome reaction. We isolated OMC45 polypeptide from the high-pH insoluble fraction of OMC. Proteomic analysis of OMC45 by MALDI-TOF-TOF yielded eight peptides that matched the NCBI database sequence of Tektin 3 (TEKT3). Triton X-100-permeabilized cauda sperm exhibited intense staining of the acrosomal segment with anti-OMC45 and anti-TEKT3. The OMC45 polypeptide was solubilized by radio-immunoprecipitation assay buffer extraction. The solubilized fraction was subjected to immunoprecipitation analysis. The OMC45 polypeptide was recovered in the anti-OMC45 immunoprecipitation pellet. An identical blot stained with anti-TEKT3 exhibited the presence of TEKT3 polypeptide in the anti-OMC45 pellet. Our immunofluorescence and biochemical studies confirm the proteomics identification of OMC45 polypeptide and that it exhibits a sequence similarity to TEKT3. OMC45 glycoprotein possesses both N-linked and O-linked oligosaccharides. Deglycosylated OMC45 revealed a significant reduction in both acrosin and N-acetylglucosaminidase (NAGA) binding in comparison with acrosin and NAGA binding to a native OMC45 polypeptide, demonstrating the important role of oligosaccharides in hydrolase binding. OMC45 polypeptide is not released during the acrosome reaction but remains in the particulate cell subfraction, associated with the hybrid membrane complex.
[Mh] Termos MeSH primário: Acrosina/metabolismo
Reação Acrossômica
Acrossomo/enzimologia
Glicoproteínas/metabolismo
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Bovinos
Bases de Dados de Proteínas
Glicoproteínas/química
Glicoproteínas/isolamento & purificação
Glicosilação
Masculino
Proteínas de Membrana/química
Proteínas de Membrana/isolamento & purificação
Peso Molecular
Ligação Proteica
Processamento de Proteína Pós-Traducional
Proteômica/métodos
Solubilidade
Capacitação Espermática
alfa-N-Acetilgalactosaminidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Membrane Proteins); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase); EC 3.4.21.10 (Acrosin)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170209
[Lr] Data última revisão:
170209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150814
[St] Status:MEDLINE
[do] DOI:10.1007/s11010-015-2534-8


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[PMID]:26143644
[Au] Autor:Suh MJ; Tovchigrechko A; Thovarai V; Rolfe MA; Torralba MG; Wang J; Adkins JN; Webb-Robertson BJ; Osborne W; Cogen FR; Kaplowitz PB; Metz TO; Nelson KE; Madupu R; Pieper R
[Ad] Endereço:†J. Craig Venter Institute, 9704 Medical Center Drive, Rockville, Maryland 20850, United States.
[Ti] Título:Quantitative Differences in the Urinary Proteome of Siblings Discordant for Type 1 Diabetes Include Lysosomal Enzymes.
[So] Source:J Proteome Res;14(8):3123-35, 2015 Aug 07.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Individuals with type 1 diabetes (T1D) often have higher than normal blood glucose levels, causing advanced glycation end product formation and inflammation and increasing the risk of vascular complications years or decades later. To examine the urinary proteome in juveniles with T1D for signatures indicative of inflammatory consequences of hyperglycemia, we profiled the proteome of 40 T1D patients with an average of 6.3 years after disease onset and normal or elevated HbA1C levels, in comparison with a cohort of 41 healthy siblings. Using shotgun proteomics, 1036 proteins were identified, on average, per experiment, and 50 proteins showed significant abundance differences using a Wilcoxon signed-rank test (FDR q-value ≤ 0.05). Thirteen lysosomal proteins were increased in abundance in the T1D versus control cohort. Fifteen proteins with functional roles in vascular permeability and adhesion were quantitatively changed, including CD166 antigen and angiotensin-converting enzyme 2. α-N-Acetyl-galactosaminidase and α-fucosidase 2, two differentially abundant lysosomal enzymes, were detected in western blots with often elevated quantities in the T1D versus control cohort. Increased release of proteins derived from lysosomes and vascular epithelium into urine may result from hyperglycemia-associated inflammation in the kidney vasculature.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 1/urina
Enzimas/urina
Proteoma/metabolismo
Proteômica/métodos
Irmãos
[Mh] Termos MeSH secundário: Molécula de Adesão de Leucócito Ativado/metabolismo
Molécula de Adesão de Leucócito Ativado/urina
Adolescente
Western Blotting
Criança
Cromatografia Líquida
Estudos de Coortes
Diabetes Mellitus Tipo 1/sangue
Diabetes Mellitus Tipo 1/metabolismo
Enzimas/metabolismo
Feminino
Seres Humanos
Lisossomos/enzimologia
Lisossomos/metabolismo
Masculino
Peptidil Dipeptidase A/metabolismo
Peptidil Dipeptidase A/urina
Espectrometria de Massas em Tandem
alfa-L-Fucosidase/metabolismo
alfa-L-Fucosidase/urina
alfa-N-Acetilgalactosaminidase/metabolismo
alfa-N-Acetilgalactosaminidase/urina
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Activated-Leukocyte Cell Adhesion Molecule); 0 (Enzymes); 0 (Proteome); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase); EC 3.2.1.51 (alpha-L-Fucosidase); EC 3.4.15.1 (Peptidyl-Dipeptidase A); EC 3.4.17.- (angiotensin converting enzyme 2)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150807
[Lr] Data última revisão:
150807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150707
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.5b00052


  9 / 208 MEDLINE  
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[PMID]:25964111
[Au] Autor:Kwan DH; Ernst S; Kötzler MP; Withers SG
[Ad] Endereço:Centre for High-Throughput Biology Department of Chemistry, University of British Columbia, Vancouver, BC, Canada V6T 1Z1.
[Ti] Título:Chemoenzymatic Synthesis of a Type 2 Blood Group A Tetrasaccharide and Development of High-throughput Assays Enables a Platform for Screening Blood Group Antigen-cleaving Enzymes.
[So] Source:Glycobiology;25(8):806-11, 2015 Aug.
[Is] ISSN:1460-2423
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A facile enzymatic synthesis of the methylumbelliferyl ß-glycoside of the type 2 A blood group tetrasaccharide in good yields is reported. Using this compound, we developed highly sensitive fluorescence-based high-throughput assays for both endo-ß-galactosidase and α-N-acetylgalactosaminidase activity specific for the oligosaccharide structure of the blood group A antigen. We further demonstrate the potential to use this assay to screen the expressed gene products of metagenomic libraries in the search for efficient blood group antigen-cleaving enzymes.
[Mh] Termos MeSH primário: Sistema do Grupo Sanguíneo ABO/química
Glicosídeos/síntese química
Himecromona/síntese química
Oligossacarídeos/síntese química
alfa-N-Acetilgalactosaminidase/química
beta-Galactosidase/química
[Mh] Termos MeSH secundário: Sistema do Grupo Sanguíneo ABO/metabolismo
Bioensaio
Escherichia coli/enzimologia
Escherichia coli/genética
Fluorescência
Expressão Gênica
Biblioteca Gênica
Glicosídeos/biossíntese
Ensaios de Triagem em Larga Escala
Seres Humanos
Himecromona/metabolismo
Metagenoma
Oligossacarídeos/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
alfa-N-Acetilgalactosaminidase/genética
alfa-N-Acetilgalactosaminidase/metabolismo
beta-Galactosidase/genética
beta-Galactosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ABO Blood-Group System); 0 (Glycosides); 0 (Oligosaccharides); 0 (Recombinant Proteins); 3T5NG4Q468 (Hymecromone); EC 3.2.1.23 (beta-Galactosidase); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150703
[Lr] Data última revisão:
150703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150513
[St] Status:MEDLINE
[do] DOI:10.1093/glycob/cwv031


  10 / 208 MEDLINE  
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[PMID]:25330411
[Au] Autor:Blériot Y; Auberger N; Jagadeesh Y; Gauthier C; Prencipe G; Tran AT; Marrot J; Désiré J; Yamamoto A; Kato A; Sollogoub M
[Ad] Endereço:Glycochemistry Group of "Organic Synthesis" Team, Université de Poitiers , UMR-CNRS 7285 IC2MP, Bât. B28, 4 rue Michel Brunet, TSA 51106, 86073 Poitiers Cedex 9, France.
[Ti] Título:Synthesis of 1,2-cis-homoiminosugars derived from GlcNAc and GalNAc exploiting a ß-amino alcohol skeletal rearrangement.
[So] Source:Org Lett;16(21):5512-5, 2014 Nov 07.
[Is] ISSN:1523-7052
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The synthesis of 1,2-cis-homoiminosugars bearing an NHAc group at the C-2 position is described. The key step to prepare these α-D-GlcNAc and α-D-GalNAc mimics utilizes a ß-amino alcohol skeletal rearrangement applied to an azepane precursor. This strategy also allows access to naturally occurring α-HGJ and α-HNJ. The α-D-GlcNAc-configured iminosugar was coupled to a glucoside acceptor to yield a novel pseudodisaccharide. Preliminary glycosidase inhibition evaluation indicates that the α-D-GalNAc-configured homoiminosugar is a potent and selective α-N-acetylgalactosaminidase inhibitor.
[Mh] Termos MeSH primário: Amino Álcoois/química
Amino Açúcares/química
Inibidores Enzimáticos/química
Galactosamina/química
Glucosamina/química
alfa-N-Acetilgalactosaminidase/antagonistas & inibidores
alfa-N-Acetilgalactosaminidase/química
[Mh] Termos MeSH secundário: Galactosamina/análogos & derivados
Glucosamina/análogos & derivados
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Alcohols); 0 (Amino Sugars); 0 (Enzyme Inhibitors); 7535-00-4 (Galactosamine); EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase); N08U5BOQ1K (Glucosamine)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:141107
[Lr] Data última revisão:
141107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141021
[St] Status:MEDLINE
[do] DOI:10.1021/ol502926f



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