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[PMID]:29484750
[Au] Autor:Saraswati S; Alhaider AA; Abdelgadir AM
[Ad] Endereço:Camel Biomedical Research Unit, College of Pharmacy and Medicine, King Saud University, Riyadh, Saudi Arabia.
[Ti] Título:Costunolide suppresses an inflammatory angiogenic response in a subcutaneous murine sponge model.
[So] Source:APMIS;126(3):257-266, 2018 Mar.
[Is] ISSN:1600-0463
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Costunolide is known to possess anti-inflammatory and antitumor activity, but its role in tumor angiogenesis, the key step involved in tumor growth and metastasis, and the involved molecular mechanism is still unknown. We aimed to investigate the effects of costunolide on key components of inflammatory angiogenesis in the murine cannulated sponge implant angiogenesis model. Polyester-polyurethane sponges, used as a framework for fibrovascular tissue growth, were implanted in Swiss albino mice and costunolide (5, 10 and 20 mg/kg/day) was administered for 14 days through installed cannula. The implants collected at day 14 post-implantation were processed for the assessment of hemoglobin (Hb), myeloperoxidase (MPO), N-acetylglucosaminidase (NAG) and collagen, which were used as indices for angiogenesis, neutrophil and macrophage accumulation, and extracellular matrix deposition, respectively. Relevant inflammatory, angiogenic and fibrogenic cytokines were also determined. Costunolide treatment attenuated the main components of the fibrovascular tissue, wet weight, vascularization (Hb content), macrophage recruitment (NAG activity), collagen deposition, and the levels of vascular endothelial growth factor (VEGF), interleukin (IL)-1ß, IL-6, IL-17, tumor necrosis factor (TNF)-α and transforming growth factor (TGF-ß). Regulatory function of costunolide on multiple parameters of the main components of inflammatory angiogenesis has been revealed giving insight into the potential therapeutic benefit underlying the anti-angiogenic actions of costunolide.
[Mh] Termos MeSH primário: Inibidores da Angiogênese/farmacologia
Macrófagos/imunologia
Neovascularização Patológica/imunologia
Neutrófilos/imunologia
Poliésteres/efeitos adversos
Poliuretanos/efeitos adversos
Sesquiterpenos/farmacologia
[Mh] Termos MeSH secundário: Acetilglucosaminidase/metabolismo
Animais
Colágeno/metabolismo
Citocinas/metabolismo
Modelos Animais de Doenças
Hemoglobinas/metabolismo
Masculino
Camundongos
Peroxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiogenesis Inhibitors); 0 (Cytokines); 0 (Hemoglobins); 0 (Polyesters); 0 (Polyurethanes); 0 (Sesquiterpenes); 4IK578SA7Z (costunolide); 9007-34-5 (Collagen); EC 1.11.1.7 (Peroxidase); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180228
[St] Status:MEDLINE
[do] DOI:10.1111/apm.12808


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[PMID]:29339067
[Au] Autor:Sun Y; Zhang J; Xiang J
[Ad] Endereço:College of Life Sciences, Hebei University, Baoding, Hebei 071002, China; College of Marine Life and Fisheries, Huaihai Institute of Technology, 59 Cangwu Road, Lianyungang 222005, China.
[Ti] Título:Molecular characterization and function of ß-N-acetylglucosaminidase from ridgetail white prawn Exopalaemon carinicauda.
[So] Source:Gene;648:12-20, 2018 Mar 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Chitin degradation is catalyzed by a two-component chitinolytic enzyme system, chitinase and ß-N-acetylglucosaminidase (NAGase). In this paper, the full-length cDNA sequence encoding NAGase (EcNAG) was obtained from Exopalaemon carinicauda. The deduced amino acid sequence of EcNAG open reading frame (ORF) contained one Glycohydro_20b2 domain and one Glyco_hydro_20 domain. Based on the cDNA sequence, the genomic structure of EcNAG was characterized and it was composed of six exons and five introns. EcNAG mRNA majorly expressed in the hepatopancreas and epidermis. During the molting stages, EcNAG mRNA expression was well-regulated and its expression reached the highest level at the molting stage E. In addition, EcNAG was recombinant expressed in Pichia pastoris and the partial enzymatic characterization of recombinant EcNAG was confirmed. After being challenged with Vibrio parahaemolyticus and Aeromonas hydrophila, the expression of EcNAG was up-regulated significantly at 6 h and reached the peak at 12 h. And then, the expression began to down-regulated and came to the normal level at 72 h. It is helpful to research the relationship between the molt-related hormones and chitinlytic enzymes.
[Mh] Termos MeSH primário: Acetilglucosaminidase/genética
Proteínas de Artrópodes/genética
Muda/genética
Palaemonidae/genética
[Mh] Termos MeSH secundário: Acetilglucosaminidase/classificação
Acetilglucosaminidase/metabolismo
Aeromonas hydrophila/fisiologia
Sequência de Aminoácidos
Animais
Proteínas de Artrópodes/classificação
Proteínas de Artrópodes/metabolismo
Sequência de Bases
Epiderme/crescimento & desenvolvimento
Epiderme/metabolismo
Epiderme/microbiologia
Doenças dos Peixes/genética
Doenças dos Peixes/microbiologia
Perfilação da Expressão Gênica/métodos
Regulação da Expressão Gênica no Desenvolvimento
Regulação Enzimológica da Expressão Gênica
Hepatopâncreas/crescimento & desenvolvimento
Hepatopâncreas/metabolismo
Hepatopâncreas/microbiologia
Palaemonidae/crescimento & desenvolvimento
Palaemonidae/microbiologia
Filogenia
Homologia de Sequência de Aminoácidos
Vibrio parahaemolyticus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


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[PMID]:29253000
[Au] Autor:Lin S; Wang S; Si Y; Yang W; Zhu S; Ni W
[Ad] Endereço:College of Environmental and Resource Sciences, Zhejiang University, Key Laboratory of Agricultural Resource and Environment of Zhejiang Province, Hangzhou, P. R. China.
[Ti] Título:Variations in eco-enzymatic stoichiometric and microbial characteristics in paddy soil as affected by long-term integrated organic-inorganic fertilization.
[So] Source:PLoS One;12(12):e0189908, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To investigate the effects of different nutrient management regimes on the soil chemical, eco-enzymatic stoichiometric and microbial characteristics, soil samples were collected from a 30-year, long-term field experiment with six plots growing rice. The results showed that as integrated fertilization increased, so did the concentrations of soil total or available nutrients and microbial biomass carbon (MBC). Our results also found enhanced soil basal respiration and cumulative carbon mineralization compared to chemical fertilization alone at the same nutrient doses. The activities of soil protease (Pro), ß-glucosidase (ßG), N-acetyl-glucosaminidase (NAG) and acid phosphatase (AP) from the integrated fertilization treatments were significantly higher than those of the treatments without organic manure, so did the activities of soil leucyl aminopeptidase (LAP) and urease (Ure) from the treatment with organic manure in addition to farmer practise fertilization (NPKM2). The stoichiometric ratios, expressed as lnßG/ln(NAG+LAP)/lnPro/lnUre/lnAP, ranged from 1:0.94:1.04:0.67:1.01 to 1:0.98:1.10:0.78:1.25, indicating that the acquisition of C, N and P changed consistently and synchronously under different nutrient management strategies. Integrated fertilization was more beneficial to the acquisition and utilization of soil organic carbon compared to low-molecular-weight organic nitrogen. We concluded that protease and urease should be considered in eco-enzymatic stoichiometric assessments for the hydrolysis of proteins, amino acids, carbohydrates and phosphomonoesters in soil, and integrated fertilization with chemical fertilizers and organic manure should be recommended as a preferable nutrient management system for intensive rice cultivation.
[Mh] Termos MeSH primário: Agricultura/métodos
Carbono/química
Fertilizantes
Microbiologia do Solo
Solo/química
[Mh] Termos MeSH secundário: Acetilglucosaminidase/metabolismo
Fosfatase Ácida/metabolismo
Aminopeptidases/metabolismo
Biomassa
China
Esterco
Nitrogênio/química
Oryza
Fósforo/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fertilizers); 0 (Manure); 0 (Soil); 27YLU75U4W (Phosphorus); 7440-44-0 (Carbon); EC 3.1.3.2 (Acid Phosphatase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.52 (Acetylglucosaminidase); EC 3.4.11.- (Aminopeptidases); N762921K75 (Nitrogen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189908


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[PMID]:28849998
[Au] Autor:Song Y; Evenseth LM; Iguchi T; Tollefsen KE
[Ad] Endereço:a Norwegian Institute for Water Research (NIVA) , Gaustadalléen , Oslo , Norway.
[Ti] Título:Release of chitobiase as an indicator of potential molting disruption in juvenile Daphnia magna exposed to the ecdysone receptor agonist 20-hydroxyecdysone.
[So] Source:J Toxicol Environ Health A;80(16-18):954-962, 2017.
[Is] ISSN:1528-7394
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:During arthropod molting, the old exoskeleton is degraded and recycled by the molting fluid. Chitobiase, a major chitinolytic enzyme in the molting fluid, has been widely used as a biomarker to indicate endocrine disruption of molting in arthropods under environmental stress. Although release of chitobiase was extensively studied in organisms exposed to molting-inhibiting chemicals, enzymic association with molting and response of the molting hormone receptor, ecdysone receptor (EcR), is not well understood. The present study was therefore conducted to identify potential linkages between release of chitobiase, molting frequency, and EcR activation in a freshwater crustacean Daphnia magna after short-term (96 hr) exposure to endogenous molting hormone 20-hydroxyecdysone (20E). A suite of bioassays was used for this purpose, including the chitobiase activity, molting frequency, viability, and in vitro EcR activation. Effect concentrations were compared between different assays analyzed. Results showed that exposure to 20E reduced chitobiase release and molting frequency in a concentration-dependent manner. Exposure to as low as 250 nM 20E significantly decreased release of chitobiase after 72 hr exposure, whereas adverse effects on molting frequency and incomplete molting-associated mortality required higher 20E exposure concentrations. The EcR reporter assay further demonstrated that as low as 100 nM 20E may activate EcR in vitro. Data suggest that release of chitobiase may be employed as a sensitive indicator of potential molting disruption in crustaceans after exposure to EcR agonists such as 20E.
[Mh] Termos MeSH primário: Acetilglucosaminidase/metabolismo
Daphnia/efeitos dos fármacos
Ecdisterona/toxicidade
Muda/efeitos dos fármacos
Receptores de Esteroides/metabolismo
[Mh] Termos MeSH secundário: Animais
Daphnia/crescimento & desenvolvimento
Disruptores Endócrinos/toxicidade
Determinação de Ponto Final
Feminino
Receptores de Esteroides/agonistas
Poluentes Químicos da Água/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endocrine Disruptors); 0 (Receptors, Steroid); 0 (Water Pollutants, Chemical); 0 (ecdysone receptor); 5289-74-7 (Ecdysterone); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE
[do] DOI:10.1080/15287394.2017.1352215


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[PMID]:28814130
[Au] Autor:Katoh T; Maeshibu T; Kikkawa KI; Gotoh A; Tomabechi Y; Nakamura M; Liao WH; Yamaguchi M; Ashida H; Yamamoto K; Katayama T
[Ad] Endereço:a Graduate School of Biostudies , Kyoto University , Kyoto , Japan.
[Ti] Título:Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization.
[So] Source:Biosci Biotechnol Biochem;81(10):2018-2027, 2017 Oct.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by bifidobacteria remains fragmentary, especially regarding how they decompose sulfated glycans, which are abundantly found in mucin sugar-chains. Here, we examined the abilities of several Bifidobacterium strains to degrade a sulfated glycan substrate and identified a 6-sulfo-ß-d-N-acetylglucosaminidase, also termed sulfoglycosidase, encoded by bbhII from Bifidobacterium bifidum JCM 7004. A recombinant BbhII protein showed a substrate preference toward 6-sulfated and 3,4-disulfated N-acetylglucosamines over non-sulfated and 3-sulfated N-acetylglucosamines. The purified BbhII directly released 6-sulfated N-acetylglucosamine from porcine gastric mucin and the expression of bbhII was moderately induced in the presence of mucin. This de-capping activity may promote utilization of sulfated glycans of mucin by other bacteria including bifidobacteria, thereby establishing the symbiotic relationship between human and gut microbes.
[Mh] Termos MeSH primário: Acetilglucosaminidase/metabolismo
Bifidobacterium bifidum/enzimologia
Mucinas/metabolismo
Polissacarídeos/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosaminidase/química
Acetilglucosaminidase/genética
Sequência de Aminoácidos
Bifidobacterium bifidum/genética
Bifidobacterium bifidum/metabolismo
Regulação Bacteriana da Expressão Gênica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mucins); 0 (Polysaccharides); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170818
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1361810


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[PMID]:28713035
[Au] Autor:Tardieu M; Zérah M; Gougeon ML; Ausseil J; de Bournonville S; Husson B; Zafeiriou D; Parenti G; Bourget P; Poirier B; Furlan V; Artaud C; Baugnon T; Roujeau T; Crystal RG; Meyer C; Deiva K; Heard JM
[Ad] Endereço:Paediatric Neurology Department, Université Paris Sud and Assistance Publique-Hôpitaux de Paris, Hôpitaux Universitaires Paris Sud, Le Kremlin-Bicêtre, France. Electronic address: marc.tardieu@aphp.fr.
[Ti] Título:Intracerebral gene therapy in children with mucopolysaccharidosis type IIIB syndrome: an uncontrolled phase 1/2 clinical trial.
[So] Source:Lancet Neurol;16(9):712-720, 2017 Sep.
[Is] ISSN:1474-4465
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mucopolysaccharidosis type IIIB syndrome (also known as Sanfilippo type B syndrome) is a lysosomal storage disease resulting in progressive deterioration of cognitive acquisition after age 2-4 years. No treatment is available for the neurological manifestations of the disease. We sought to assess the safety and efficacy of a novel intracerebral gene therapy. METHODS: Local regulatory authorities in France allowed inclusion of up to four children in this phase 1/2 study. Treatment was 16 intraparenchymal deposits (four in the cerebellum) of a recombinant adenoassociated viral vector serotype 2/5 (rAAV2/5) encoding human α-N-acetylglucosaminidase (NAGLU) plus immunosuppressive therapy. We assessed tolerance, neurocognitive progression, brain growth, NAGLU enzymatic activity in CSF, and specific anti-NAGLU immune response for 30 months after surgery. This trial is registered with EudraCT, number 2012-000856-33, and the International Standard Clinical Trial Registry, number ISRCTN19853672. FINDINGS: Of seven eligible children, the four youngest, from France (n=2), Italy (n=1), and Greece (n=1), aged 20, 26, 30, and 53 months, were included between February, 2012, and February, 2014. 125 adverse events were recorded, of which 117 were treatment emergent and included six classified as severe, but no suspected unexpected serious adverse drug reactions were seen. Vector genomes were detected in blood for 2 days after surgery. Compared with the natural history of mucopolysaccharidosis type III syndromes, neurocognitive progression was improved in all patients, with the youngest patient having function close to that in healthy children. Decrease in developmental quotient was -11·0 points in patient one, -23·0 in patient two, -29·0 in patient three, and -17·0 in patient four, compared with -37·7 in the natural history of the disease. NAGLU activity was detected in lumbar CSF and was 15-20% of that in unaffected children. Circulating T lymphocytes that proliferated and produced tumour necrosis factor α upon ex-vivo exposure to NAGLU antigens were detectable at 1-12 months and 3-12 months, respectively, but not at 30 months in three of four patients. INTERPRETATION: Intracerebral rAVV2/5 was well tolerated and induced sustained enzyme production in the brain. The initial specific anti-NAGLU immune response that later subsided suggested acquired immunological tolerance. The best results being obtained in the youngest patient implies a potential window of opportunity. Longer follow-up is needed to further assess safety outcomes and persistence of improved cognitive development. FUNDING: Association Française Contre les Myopathies, Vaincre les Maladies Lysosomales, Institut Pasteur, and UniQure.
[Mh] Termos MeSH primário: Acetilglucosaminidase
Encéfalo/enzimologia
Dependovirus/genética
Terapia Genética/métodos
Vetores Genéticos/farmacologia
Mucopolissacaridose III/terapia
Avaliação de Resultados (Cuidados de Saúde)
[Mh] Termos MeSH secundário: Acetilglucosaminidase/genética
Pré-Escolar
Terapia Genética/efeitos adversos
Vetores Genéticos/administração & dosagem
Seres Humanos
Imunossupressores/uso terapêutico
Lactente
Mucopolissacaridose III/tratamento farmacológico
Síndrome
[Pt] Tipo de publicação:CLINICAL TRIAL, PHASE I; CLINICAL TRIAL, PHASE II; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunosuppressive Agents); EC 3.2.1.50 (alpha-N-acetyl-D-glucosaminidase); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170904
[Lr] Data última revisão:
170904
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


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[PMID]:28526403
[Au] Autor:Kintsu H; Okumura T; Negishi L; Ifuku S; Kogure T; Sakuda S; Suzuki M
[Ad] Endereço:Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan.
[Ti] Título:Crystal defects induced by chitin and chitinolytic enzymes in the prismatic layer of Pinctada fucata.
[So] Source:Biochem Biophys Res Commun;489(2):89-95, 2017 Jul 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biomineralization, in which organisms create biogenic hard tissues, with hardness or flexibility enhanced by organic-inorganic interaction is an interesting and attractive focus for application of biomimetic functional materials. Calcites in the prismatic layer of Pinctada fucata are tougher than abiotic calcites due to small crystal defects. However, the molecular mechanism of the defect formation remains unclear. Here, chitin and two chitinolytic enzymes, chitinase and chitobiase, were identified as organic matrices related to for the formation of small crystal defects in the prismatic layer. Experiments with a chitinase inhibitor in vivo showed chitinase is necessary to form the prismatic layer. Analysis of calcite crystals, which were synthesized in a chitin hydrogel treated with chitinolytic enzymes, by electron microscopy and X-ray diffraction showed that crystal defects became larger as chitin was more degraded. These results suggest that interactions between chitin and calcium carbonate increase as chitin is thinner.
[Mh] Termos MeSH primário: Acetilglucosaminidase/química
Quitina/química
Quitinases/química
Pinctada/química
[Mh] Termos MeSH secundário: Acetilglucosaminidase/metabolismo
Acetilglucosaminidase/ultraestrutura
Animais
Quitina/metabolismo
Quitina/ultraestrutura
Quitinases/metabolismo
Quitinases/ultraestrutura
Microscopia Eletrônica
Tamanho da Partícula
Pinctada/metabolismo
Pinctada/ultraestrutura
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
1398-61-4 (Chitin); EC 3.2.1.14 (Chitinases); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE


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[PMID]:28399848
[Au] Autor:Zhou J; Song Z; Zhang R; Liu R; Wu Q; Li J; Tang X; Xu B; Ding J; Han N; Huang Z
[Ad] Endereço:Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China.
[Ti] Título:Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 ß-N-acetylglucosaminidase and salt tolerance.
[So] Source:BMC Biotechnol;17(1):37, 2017 Apr 11.
[Is] ISSN:1472-6750
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Enzymatic degradation of chitin has attracted substantial attention because chitin is an abundant renewable natural resource, second only to lignocellulose, and because of the promising applications of N-acetylglucosamine in the bioethanol, food and pharmaceutical industries. However, the low activity and poor tolerance to salts and N-acetylglucosamine of most reported ß-N-acetylglucosaminidases limit their applications. Mining for novel enzymes from new microorganisms is one way to address this problem. RESULTS: A glycoside hydrolase family 20 (GH 20) ß-N-acetylglucosaminidase (GlcNAcase) was identified from Microbacterium sp. HJ5 harboured in the saline soil of an abandoned salt mine and was expressed in Escherichia coli. The purified recombinant enzyme showed specific activities of 1773.1 ± 1.1 and 481.4 ± 2.3 µmol min mg towards p-nitrophenyl ß-N-acetylglucosaminide and N,N'-diacetyl chitobiose, respectively, a V of 3097 ± 124 µmol min mg towards p-nitrophenyl ß-N-acetylglucosaminide and a K of 14.59 mM for N-acetylglucosamine inhibition. Most metal ions and chemical reagents at final concentrations of 1.0 and 10.0 mM or 0.5 and 1.0% (v/v) had little or no effect (retaining 84.5 - 131.5% activity) on the enzyme activity. The enzyme can retain more than 53.6% activity and good stability in 3.0-20.0% (w/v) NaCl. Compared with most GlcNAcases, the activity of the enzyme is considerably higher and the tolerance to salts and N-acetylglucosamine is much better. Furthermore, the enzyme had higher proportions of aspartic acid, glutamic acid, alanine, glycine, random coils and negatively charged surfaces but lower proportions of cysteine, lysine, α-helices and positively charged surfaces than its homologs. These molecular characteristics were hypothesised as potential factors in the adaptation for salt tolerance and high activity of the GH 20 GlcNAcase. CONCLUSIONS: Biochemical characterization revealed that the GlcNAcase had novel salt-GlcNAc tolerance and high activity. These characteristics suggest that the enzyme has versatile potential in biotechnological applications, such as bioconversion of chitin waste and the processing of marine materials and saline foods. Molecular characterization provided an understanding of the molecular-function relationships for the salt tolerance and high activity of the GH 20 GlcNAcase.
[Mh] Termos MeSH primário: Acetilglucosamina/química
Acetilglucosaminidase/química
Acetilglucosaminidase/ultraestrutura
Actinobacteria/enzimologia
Sais/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Ativação Enzimática
Estabilidade Enzimática
Glicosídeo Hidrolases/química
Ligação Proteica
Conformação Proteica
Tolerância a Sal
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Salts); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.52 (Acetylglucosaminidase); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170704
[Lr] Data última revisão:
170704
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE
[do] DOI:10.1186/s12896-017-0358-1


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[PMID]:28380198
[Au] Autor:Lobato GR; Lobato MR; Thomé FS; Veronese FV
[Ad] Endereço:Programa de Pós Graduação em Medicina: Ciências Médicas, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brasil.
[Ti] Título:Performance of urinary kidney injury molecule-1, neutrophil gelatinase-associated lipocalin, and N-acetyl-ß-D-glucosaminidase to predict chronic kidney disease progression and adverse outcomes.
[So] Source:Braz J Med Biol Res;50(5):e6106, 2017 Mar 30.
[Is] ISSN:1414-431X
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:Urinary biomarkers can predict the progression of chronic kidney disease (CKD). In this study, kidney injury molecule-1 (KIM-1), neutrophil gelatinase-associated lipocalin (NGAL), and N-acetyl-ß-D-glucosaminidase (NAG) were correlated with the stages of CKD, and the association of these biomarkers with CKD progression and adverse outcomes was determined. A total of 250 patients, including 111 on hemodialysis, were studied. Urinary KIM-1, NGAL, and NAG were measured at baseline. Patients not on dialysis at baseline who progressed to a worse CKD stage were compared with those who did not progress. The association of each biomarker and selected covariates with progression to more advanced stages of CKD, end-stage kidney disease, or death was evaluated by Poisson regression. NGAL was moderately correlated (rs=0.467, P<0.001) with the five stages of CKD; KIM-1 and NAG were also correlated, but weakly. Sixty-four patients (46%) progressed to a more advanced stage of CKD. Compared to non-progressors, those patients exhibited a trend to higher levels of KIM-1 (P=0.064) and NGAL (P=0.065). In patients not on dialysis at baseline, NGAL was independently associated with progression of CKD, ESKD, or death (RR=1.022 for 300 ng/mL intervals; CI=1.007-1.037, P=0.004). In patients on dialysis, for each 300-ng/mL increase in urinary NGAL, there was a 1.3% increase in the risk of death (P=0.039). In conclusion, urinary NGAL was associated with adverse renal outcomes and increased risk of death in this cohort. If baseline urinary KIM-1 and NGAL predict progression to worse stages of CKD is something yet to be explored.
[Mh] Termos MeSH primário: Acetilglucosaminidase/urina
Receptor Celular 1 do Vírus da Hepatite A/análise
Lipocalina-2/urina
Insuficiência Renal Crônica/patologia
Insuficiência Renal Crônica/urina
[Mh] Termos MeSH secundário: Adulto
Fatores Etários
Idoso
Análise de Variância
Biomarcadores/urina
Creatinina/sangue
Creatinina/urina
Progressão da Doença
Feminino
Taxa de Filtração Glomerular
Seres Humanos
Masculino
Meia-Idade
Valor Preditivo dos Testes
Padrões de Referência
Valores de Referência
Diálise Renal
Insuficiência Renal Crônica/complicações
Insuficiência Renal Crônica/fisiopatologia
Reprodutibilidade dos Testes
Fatores de Risco
Fatores Sexuais
Estatísticas não Paramétricas
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (HAVCR1 protein, human); 0 (Hepatitis A Virus Cellular Receptor 1); 0 (LCN2 protein, human); 0 (Lipocalin-2); AYI8EX34EU (Creatinine); EC 3.2.1.52 (Acetylglucosaminidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE


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[PMID]:28314232
[Au] Autor:Luo L; Meng H; Wu RN; Gu JD
[Ad] Endereço:College of Environmental Sciences, Sichuan Agricultural University, Huimin Road, Chengdu, 611130, People's Republic of China; Laboratory of Environmental Microbiology and Toxicology, School of Biological Sciences, The University of Hong Kong, Pokfulam Road, Hong Kong Special Administrative Region. E
[Ti] Título:Impact of nitrogen pollution/deposition on extracellular enzyme activity, microbial abundance and carbon storage in coastal mangrove sediment.
[So] Source:Chemosphere;177:275-283, 2017 Jun.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:This study applied different concentration of NaNO solution to simulate the effect of inorganic nitrogen (N) deposition/pollution on carbon (C) storage in coastal mangrove sediment through observing the changes of enzyme activity and microbial abundance. Sediment collected from mangrove forest (MG) and intertidal zone (IZ) were incubated with different N rates (0 (control), 5 (low-N) and 20 (high-N) µg N g dry sediment, respectively). After incubation, the activities of phenol oxidase (PHO) and acid phosphatase (ACP) were enhanced, but ß-glucosidase (GLU) and N-ß-acetyl-glucosaminidase (NAG) activities were reduced by N addition. The altered enzymatic stoichiometries by N input implied that microbial phosphorus (P) limitation was increased, whereas C and N limitation were alleviated. Besides, N input decreased the bacterial abundance but increased fungal abundance in both types of sediment. The increased pH and soluble phenolics along with the exacerbated P limitation by N addition might explain these changes. Furthermore, sediment with N addition (except high-N treated MG sediment) showed a trend of C sequestration, which might be largely caused by the decrease of bacterial abundance and GLU activity. However, MG sediment with high-N suggested a trend of C loss, and the possible reason for this discrepancy might be the relatively higher increase of PHO and ACP activity. To better understand the influence of N deposition/pollution on C cycling, the long-term N effect on microorganisms, enzymes, and thus C storage should be paid more attention in the future.
[Mh] Termos MeSH primário: Sequestro de Carbono
Enzimas/química
Sedimentos Geológicos/química
Nitrogênio/análise
Fósforo/química
Microbiologia da Água
Zonas Úmidas
[Mh] Termos MeSH secundário: Acetilglucosaminidase/química
Fosfatase Ácida/química
Bactérias
Poluição Ambiental
Fungos
Geografia
Concentração de Íons de Hidrogênio
Monofenol Mono-Oxigenase/química
Nitrogênio/química
Temperatura Ambiente
Poluentes Químicos da Água/análise
Poluentes Químicos da Água/química
beta-Glucosidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes); 0 (Water Pollutants, Chemical); 27YLU75U4W (Phosphorus); EC 1.14.18.1 (Monophenol Monooxygenase); EC 3.1.3.2 (Acid Phosphatase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.52 (Acetylglucosaminidase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE



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