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[PMID]:29227082
[Au] Autor:Olkhovych NV
[Ti] Título:Chitotriosidase activity as additional biomarker in the diagnosis of lysosomal storage diseases.
[So] Source:Ukr Biochem J;88(1):69-78, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:To date, several genetic variants that lead to a deficiency of chitotriosidase activity have been described. The duplication of 24 bp (dup24bp) in exon 10 of the CHIT1 gene, which causes a complete loss of enzymatic activity of the gene product, is the most common among the European population. The aim of the study was to evaluate the possibility of using chitotriosidase activity as an additional biomarker in diagnosis of lysosomal storage diseases (LSDs) in Ukraine, to determine this parameter in blood plasma of the patients with various lysosomal diseases and to assess the effect of the presence of dup24bp in the CHIT1 gene on this parameter. It has been shown that chitotriosidase activity in blood plasma is a convenient additional biochemical marker in the diagnosis of some LSDs, namely Gaucher disease, Niemann-Pick disease A, B, C and GM1-gangliosidosis. Reference ranges of the normal chitotriosidase activity were determined in blood plasma of Ukrainian population and found to be 8.0-53.1 nmol 4-methylumbelliferone/h·ml of plasma. The total allele frequency of the dup24bp in the CHIT1 gene in Ukrainian population was determined, which amounted to 0.26 (323/1244) that is higher than in European population. It was indicated that moleculargenetic screening of dup24bp in the CHIT1 gene is a necessary stage in a protocol for the laboratory diagnosis of Gaucher disease, Niemann-Pick disease A, B, C as well as GM1-gangliosidosis to avoid incorrect diagnosis.
[Mh] Termos MeSH primário: Gangliosidose GM1/genética
Doença de Gaucher/genética
Frequência do Gene
Hexosaminidases/genética
Doenças de Niemann-Pick/genética
[Mh] Termos MeSH secundário: Adulto
Alelos
Biomarcadores/metabolismo
Estudos de Casos e Controles
Éxons
Feminino
Gangliosidose GM1/classificação
Gangliosidose GM1/diagnóstico
Gangliosidose GM1/patologia
Doença de Gaucher/diagnóstico
Doença de Gaucher/patologia
Duplicação Gênica
Expressão Gênica
Testes Genéticos
Hexosaminidases/sangue
Hexosaminidases/deficiência
Seres Humanos
Himecromona/sangue
Masculino
Doenças de Niemann-Pick/classificação
Doenças de Niemann-Pick/diagnóstico
Doenças de Niemann-Pick/patologia
Ucrânia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 3T5NG4Q468 (Hymecromone); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.- (chitotriosidase)
[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:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.069


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[PMID]:28551069
[Au] Autor:Dany M; Elston D
[Ad] Endereço:Department of Dermatology and Dermatologic Surgery, Medical University of South Carolina, Charleston, South Carolina.
[Ti] Título:Gene expression of sphingolipid metabolism pathways is altered in hidradenitis suppurativa.
[So] Source:J Am Acad Dermatol;77(2):268-273.e6, 2017 Aug.
[Is] ISSN:1097-6787
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hidradenitis suppurativa (HS) is a debilitating skin disease characterized by painful recurrent nodules and abscesses caused by chronic inflammation. Early events in the development of HS are believed to occur in the folliculopilosebaceous unit; however, the signaling pathways behind this mechanism are unknown. Sphingolipids, such as ceramide, are essential components of the skin and appendages and have important structural and signaling roles. OBJECTIVE: We sought to explore whether the gene expression of enzymes involved in sphingolipid metabolic pathways is altered in HS. METHODS: A microarray data set including 30 samples was used to compare the expression of sphingolipid-related enzymes in inflammatory skin lesions from HS patients (n = 17) with the expression in clinically healthy skin tissue (n = 13). Differential expression of sphingolipid metabolism-related genes was analyzed using Gene Expression Omnibus 2R. RESULTS: HS lesional skin samples have significantly decreased expression of enzymes generating ceramide and sphingomyelin, increased expression of enzymes catabolizing ceramide to sphingosine, and increased expression of enzymes converting ceramide to galactosylceramide and gangliosides. LIMITATIONS: Limitations of this study include assessing the expression of sphingolipid-related enzymes without assessing the levels of the related sphingolipids. CONCLUSION: Our study suggests that sphingolipid metabolism is altered in HS lesional skin compared with normal skin.
[Mh] Termos MeSH primário: Expressão Gênica
Hidradenite Supurativa/enzimologia
Hidradenite Supurativa/genética
Perilipinas/genética
Pele/enzimologia
Esfingolipídeos/metabolismo
[Mh] Termos MeSH secundário: Ceramidase Alcalina/genética
Estudos de Casos e Controles
Ceramidas/metabolismo
Proteínas Quinases Dependentes de AMP Cíclico/genética
Glucosilceramidase/genética
Glucosiltransferases/genética
Glicoesfingolipídeos/metabolismo
Hexosaminidases/genética
Seres Humanos
Lisofosfolipídeos/metabolismo
Proteínas de Membrana/genética
Redes e Vias Metabólicas/genética
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Serina C-Palmitoiltransferase/genética
Transdução de Sinais/genética
Esfingolipídeos/biossíntese
Esfingomielina Fosfodiesterase/genética
Esfingomielinas/metabolismo
Esfingosina/análogos & derivados
Esfingosina/metabolismo
Esfingosina N-Aciltransferase/genética
Proteínas Supressoras de Tumor/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ceramides); 0 (Glycosphingolipids); 0 (Lysophospholipids); 0 (Membrane Proteins); 0 (Perilipins); 0 (Sphingolipids); 0 (Sphingomyelins); 0 (Tumor Suppressor Proteins); 26993-30-6 (sphingosine 1-phosphate); EC 2.3.1.24 (CERS2 protein, human); EC 2.3.1.24 (CERS5 protein, human); EC 2.3.1.24 (Sphingosine N-Acyltransferase); EC 2.3.1.50 (Serine C-Palmitoyltransferase); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.80 (ceramide glucosyltransferase); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.91 (sphingosine kinase 2, human); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 3.1.4.12 (Sphingomyelin Phosphodiesterase); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.45 (Glucosylceramidase); EC 3.5.1.23 (Alkaline Ceramidase); NGZ37HRE42 (Sphingosine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


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[PMID]:28506293
[Au] Autor:Kim YM; Shin DH; Park SB; Cheon CK; Yoo HW
[Ad] Endereço:Department of Pediatrics, College of Medicine, Pusan National University Children's Hospital, Yangsan, Korea.
[Ti] Título:Case report of unexpected gastrointestinal involvement in type 1 Gaucher disease: comparison of eliglustat tartrate treatment and enzyme replacement therapy.
[So] Source:BMC Med Genet;18(1):55, 2017 May 15.
[Is] ISSN:1471-2350
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Gastrointestinal involvement in Gaucher disease is very rare, and appears to be unresponsive to enzyme replacement therapy (ERT). CASE PRESENTATION: Here, we describe identical twin, splenectomized, non-neuronopathic Gaucher patients on long-term ERT for 9 years, who complained of epigastric discomfort due to Gaucher cell infiltration of the gastroduodenal mucosa. Rare compound heterozygous mutations (p.Arg48Trp and p.Arg257Gln) of the GBA gene were found in both. Improvement in the gastroduodenal infiltration and reduced chitotriosidase levels were observed in one who switched to eliglustat tartrate for 1 year, whereas the other one who maintained ERT showed no improvement of chitotriosidase level and persistent duodenal lesions. CONCLUSION: This shows that eliglustat might be an effective treatment for Gaucher disease patients having lesions resistant to ERT.
[Mh] Termos MeSH primário: Duodeno/patologia
Terapia de Reposição de Enzimas/métodos
Doença de Gaucher/tratamento farmacológico
Pirrolidinas/uso terapêutico
[Mh] Termos MeSH secundário: Adulto
Criança
Inibidores Enzimáticos/uso terapêutico
Doença de Gaucher/genética
Hexosaminidases/metabolismo
Seres Humanos
Lactente
Masculino
Resultado do Tratamento
Gêmeos Monozigóticos
beta-Glucosidase/genética
[Pt] Tipo de publicação:CASE REPORTS; COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Pyrrolidines); DR40J4WA67 (eliglustat); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.- (chitotriosidase); EC 3.2.1.21 (beta-Glucosidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1186/s12881-017-0403-x


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[PMID]:28406460
[Au] Autor:Djenane Z; Nateche F; Amziane M; Gomis-Cebolla J; El-Aichar F; Khorf H; Ferré J
[Ad] Endereço:Microbiology Group, Laboratory of Cellular and Molecular Biology, Faculty of Biological Sciences, University of Science and Technology Houari Boumediene (USTHB), BP 32, EL ALIA, Bab Ezzouar, 16111 Algiers, Algeria. zad@uv.es.
[Ti] Título:Assessment of the Antimicrobial Activity and the Entomocidal Potential of Bacillus thuringiensis Isolates from Algeria.
[So] Source:Toxins (Basel);9(4), 2017 Apr 13.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:This work represents the first initiative to analyze the distribution of in Algeria and to evaluate the biological potential of the isolates. A total of 157 isolates were recovered, with at least one isolate in 94.4% of the samples. The highest Bt index was found in samples from rhizospheric soil (0.48) and from the Mediterranean area (0.44). Most isolates showed antifungal activity (98.5%), in contrast to the few that had antibacterial activity (29.9%). A high genetic diversity was made evident by the finding of many different crystal shapes and various combinations of shapes within a single isolate (in 58.4% of the isolates). Also, over 50% of the isolates harbored , , or genes, and 69.3% contained a gene. A good correlation between the presence of chitinase genes and antifungal activity was observed. More than half of the isolates with a broad spectrum of antifungal activity harbored both endochitinase and exochitinase genes. Interestingly, 15 isolates contained the two chitinase genes and all of the above family genes, with some of them harboring a gene as well. The combination of this large number of genes coding for entomopathogenic proteins suggests a putative wide range of entomotoxic activity.
[Mh] Termos MeSH primário: Anti-Infecciosos/farmacologia
Bacillus thuringiensis
Proteínas de Bactérias/farmacologia
Toxinas Bacterianas/farmacologia
[Mh] Termos MeSH secundário: Argélia
Anti-Infecciosos/isolamento & purificação
Bacillus thuringiensis/química
Bacillus thuringiensis/genética
Bacillus thuringiensis/isolamento & purificação
Bacillus thuringiensis/ultraestrutura
Proteínas de Bactérias/isolamento & purificação
Toxinas Bacterianas/isolamento & purificação
Quitinases/genética
Criptocromos/genética
Escherichia coli/efeitos dos fármacos
Escherichia coli/crescimento & desenvolvimento
Fungos/efeitos dos fármacos
Fungos/crescimento & desenvolvimento
Genes Bacterianos
Hexosaminidases/genética
Microscopia Eletrônica de Varredura
Pseudomonas aeruginosa/efeitos dos fármacos
Pseudomonas aeruginosa/crescimento & desenvolvimento
Microbiologia do Solo
Staphylococcus aureus/efeitos dos fármacos
Staphylococcus aureus/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (Cryptochromes); EC 3.2.1.- (1,4-beta-chitobiosidase); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE


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[PMID]:28330482
[Au] Autor:Marques RE; Del Sarto JL; Rocha RP; Gomes GF; Cramer A; Rachid MA; Souza DG; Nogueira ML; Teixeira MM
[Ad] Endereço:Immunopharmacology, Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, Minas Gerais, Brazil. rafael.marques@lnbio.cnpem.br.
[Ti] Título:Development of a model of Saint Louis encephalitis infection and disease in mice.
[So] Source:J Neuroinflammation;14(1):61, 2017 Mar 22.
[Is] ISSN:1742-2094
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Flaviviruses are a genre of closely related viral pathogens which emerged in the last decades in Brazil and in the world. Saint (St.) Louis encephalitis virus (SLEV) is a neglected flavivirus that can cause a severe neurological disease that may lead to death or sequelae. St. Louis encephalitis pathogenesis is poorly understood, which hinders the development of specific treatment or vaccine. METHODS: To address this problem, we developed a model of SLEV infection in mice to study mechanisms involved in the pathogenesis of severe disease. The model consists in the intracranial inoculation of the SLEV strain BeH 355964, a strain isolated from a symptomatic human patient in Brazil, in adult immunocompetent mice. RESULTS: Inoculated mice presented SLEV replication in the brain, accompanied by tissue damage, disease signs, and mortality approximately 7 days post infection. Infection was characterized by the production of proinflammatory cytokines and interferons and by leukocyte recruitment to the brain, composed mainly by neutrophils and lymphocytes. In vitro experiments indicated that SLEV is able to replicate in both neurons and glia and caused neuronal death and cytokine production, respectively. CONCLUSIONS: Altogether, intracranial SLEV infection leads to meningoencephalitis in mice, recapitulating several aspects of St. Louis encephalitis in humans. Our study indicates that the central nervous system (CNS) inflammation is a major component of SLEV-induced disease. This model may be useful to identify mechanisms of disease pathogenesis or resistance to SLEV infection.
[Mh] Termos MeSH primário: Citocinas/metabolismo
Modelos Animais de Doenças
Vírus da Encefalite de St. Louis/fisiologia
Encefalite de St. Louis/patologia
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Linhagem Celular Transformada
Encefalite de St. Louis/virologia
Peroxidase de Eosinófilo/metabolismo
Hexosaminidases/metabolismo
Leucócitos/metabolismo
Leucócitos/virologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Peroxidase/metabolismo
Fatores de Tempo
Carga Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); EC 1.11.1.- (Eosinophil Peroxidase); EC 1.11.1.7 (Peroxidase); EC 3.2.1.- (Hexosaminidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1186/s12974-017-0837-2


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[PMID]:28199385
[Au] Autor:Medina JL; Brooks EG; Chaparro A; Dube PH
[Ad] Endereço:Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, San Antonio, Texas, United States of America.
[Ti] Título:Mycoplasma pneumoniae CARDS toxin elicits a functional IgE response in Balb/c mice.
[So] Source:PLoS One;12(2):e0172447, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycoplasma pneumoniae is strongly associated with new onset asthma and asthma exacerbations. Until recently, the molecular mechanisms utilized by M. pneumoniae to influence asthma symptoms were unknown. However, we recently reported that an ADP-ribosylating and vacuolating toxin called the Community Acquired Respiratory Distress Syndrome toxin, CARDS toxin, produced by M. pneumoniae was sufficient to promote allergic inflammation and asthma-like disease in mice. A mouse model of CARDS toxin exposure was used to evaluate total and CARDS-toxin specific serum IgE responses. Mast cell sensitization, challenge, and degranulation studies determined functionality of the CARDS toxin-specific IgE. In the current study, we report that a single mucosal exposure to CARDS toxin was sufficient to increase total serum IgE and CARDS toxin-specific IgE in mice. Mice given a second mucosal challenge of CARDS toxin responded with significant increases in total and CARDS toxin-specific IgE. CARDS toxin-specific IgE bound to an N-terminal peptide of CARDS toxin but not the C-terminal peptide. Likewise, full-length CARDS toxin and the N-terminal peptide induced mast cell degranulation. Altogether, these data demonstrate that exposure to CARDS toxin is sufficient to generate functional IgE in mice. M. pneumoniae and CARDS toxin are strongly associated with asthma exacerbations raising the possibility that the CARDS toxin-specific IgE-mast cell axis contributes to disease pathogenesis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/imunologia
Toxinas Bacterianas/imunologia
Imunoglobulina E/sangue
Mycoplasma pneumoniae/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/química
Toxinas Bacterianas/genética
Toxinas Bacterianas/metabolismo
Células da Medula Óssea/citologia
Células da Medula Óssea/metabolismo
Células Cultivadas
Modelos Animais de Doenças
Epitopos/imunologia
Hexosaminidases
Camundongos
Camundongos Endogâmicos BALB C
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/isolamento & purificação
Fator de Transcrição STAT6/genética
Fator de Transcrição STAT6/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (CARDS toxin, Mycoplasma pneumoniae); 0 (Epitopes); 0 (Recombinant Proteins); 0 (STAT6 Transcription Factor); 37341-29-0 (Immunoglobulin E); EC 3.2.1.- (Hexosaminidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172447


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[PMID]:28137256
[Au] Autor:Berini F; Presti I; Beltrametti F; Pedroli M; Vårum KM; Pollegioni L; Sjöling S; Marinelli F
[Ad] Endereço:Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy. f.berini@uninsubria.it.
[Ti] Título:Production and characterization of a novel antifungal chitinase identified by functional screening of a suppressive-soil metagenome.
[So] Source:Microb Cell Fact;16(1):16, 2017 Jan 31.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Through functional screening of a fosmid library, generated from a phytopathogen-suppressive soil metagenome, the novel antifungal chitinase-named Chi18H8 and belonging to family 18 glycosyl hydrolases-was previously discovered. The initial extremely low yield of Chi18H8 recombinant production and purification from Escherichia coli cells (21 µg/g cell) limited its characterization, thus preventing further investigation on its biotechnological potential. RESULTS: We report on how we succeeded in producing hundreds of milligrams of pure and biologically active Chi18H8 by developing and scaling up to a high-yielding, 30 L bioreactor process, based on a novel method of mild solubilization of E. coli inclusion bodies in lactic acid aqueous solution, coupled with a single step purification by hydrophobic interaction chromatography. Chi18H8 was characterized as a Ca -dependent mesophilic chitobiosidase, active on chitin substrates at acidic pHs and possessing interesting features, such as solvent tolerance, long-term stability in acidic environment and antifungal activity against the phytopathogens Fusarium graminearum and Rhizoctonia solani. Additionally, Chi18H8 was found to operate according to a non-processive endomode of action on a water-soluble chitin-like substrate. CONCLUSIONS: Expression screening of a metagenomic library may allow access to the functional diversity of uncultivable microbiota and to the discovery of novel enzymes useful for biotechnological applications. A persisting bottleneck, however, is the lack of methods for large scale production of metagenome-sourced enzymes from genes of unknown origin in the commonly used microbial hosts. To our knowledge, this is the first report on a novel metagenome-sourced enzyme produced in hundreds-of-milligram amount by recovering the protein in the biologically active form from recombinant E. coli inclusion bodies.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Quitinases/metabolismo
Quitinases/farmacologia
Escherichia coli/genética
Hexosaminidases/metabolismo
Hexosaminidases/farmacologia
Microbiologia do Solo
[Mh] Termos MeSH secundário: Antifúngicos/isolamento & purificação
Antifúngicos/metabolismo
Reatores Biológicos
Quitina/metabolismo
Quitinases/genética
Quitinases/isolamento & purificação
Clonagem Molecular
Escherichia coli/metabolismo
Fusarium/efeitos dos fármacos
Biblioteca Gênica
Hexosaminidases/genética
Hexosaminidases/isolamento & purificação
Concentração de Íons de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Corpos de Inclusão/enzimologia
Ácido Láctico/metabolismo
Metagenoma
Metagenômica/métodos
Filogenia
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/farmacologia
Rhizoctonia/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Recombinant Proteins); 1398-61-4 (Chitin); 33X04XA5AT (Lactic Acid); EC 3.2.1.- (1,4-beta-chitobiosidase); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.14 (Chitinases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0634-8


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[PMID]:28130448
[Au] Autor:Mine S; Watanabe M; Kamachi S; Abe Y; Ueda T
[Ad] Endereço:From the Biomedical Research Institute (BMD), National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, s-mine@aist.go.jp.
[Ti] Título:The Structure of an Archaeal ß-Glucosaminidase Provides Insight into Glycoside Hydrolase Evolution.
[So] Source:J Biol Chem;292(12):4996-5006, 2017 Mar 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The archaeal exo-ß-d-glucosaminidase (GlmA) is a dimeric enzyme that hydrolyzes chitosan oligosaccharides into monomer glucosamines. GlmA is a member of the glycosidase hydrolase (GH)-A superfamily-subfamily 35 and is a novel enzyme in terms of its primary structure. Here, we present the crystal structure of GlmA in complex with glucosamine at 1.27 Å resolution. The structure reveals that a monomeric form of GlmA shares structural homology with GH42 ß-galactosidases, whereas most of the spatial positions of the active site residues are identical to those of GH35 ß-galactosidases. We found that upon dimerization, the active site of GlmA changes shape, enhancing its ability to hydrolyze the smaller substrate in a manner similar to that of homotrimeric GH42 ß-galactosidase. However, GlmA can differentiate glucosamine from galactose based on one charged residue while using the "evolutionary heritage residue" it shares with GH35 ß-galactosidase. Our study suggests that GH35 and GH42 ß-galactosidases evolved by exploiting the structural features of GlmA.
[Mh] Termos MeSH primário: Glicosídeo Hidrolases/química
Hexosaminidases/química
Pyrococcus horikoshii/enzimologia
Thermococcus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Cristalografia por Raios X
Evolução Molecular
Glucosamina/metabolismo
Glicosídeo Hidrolases/metabolismo
Hexosaminidases/metabolismo
Modelos Moleculares
Conformação Proteica
Multimerização Proteica
Pyrococcus horikoshii/química
Pyrococcus horikoshii/metabolismo
Especificidade por Substrato
Thermococcus/química
Thermococcus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.- (exo-beta-D-glucosaminidase); N08U5BOQ1K (Glucosamine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.766535


  9 / 4160 MEDLINE  
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[PMID]:28129403
[Au] Autor:Kuusk S; Sørlie M; Väljamäe P
[Ad] Endereço:Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
[Ti] Título:Human Chitotriosidase Is an Endo-Processive Enzyme.
[So] Source:PLoS One;12(1):e0171042, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human chitotriosidase (HCHT) is involved in immune response to chitin-containing pathogens in humans. The enzyme is able to degrade chitooligosaccharides as well as crystalline chitin. The catalytic domain of HCHT is connected to the carbohydrate binding module (CBM) through a flexible hinge region. In humans, two active isoforms of HCHT are found-the full length enzyme and its truncated version lacking CBM and the hinge region. The active site architecture of HCHT is reminiscent to that of the reducing-end exo-acting processive chitinase ChiA from bacterium Serratia marcescens (SmChiA). However, the presence of flexible hinge region and occurrence of two active isoforms are reminiscent to that of non-processive endo-chitinase from S. marcescens, SmChiC. Although the studies on soluble chitin derivatives suggest the endo-character of HCHT, the mode of action of the enzyme on crystalline chitin is not known. Here, we made a thorough characterization of HCHT in terms of the mode of action, processivity, binding, and rate constants for the catalysis and dissociation using α-chitin as substrate. HCHT efficiently released the end-label from reducing-end labelled chitin and had also high probability (95%) of endo-mode initiation of processive run. These results qualify HCHT as an endo-processive enzyme. Processivity and the rate constant of dissociation of HCHT were found to be in-between those, characteristic to processive exo-enzymes, like SmChiA and randomly acting non-processive endo-enzymes, like SmChiC. Apart from increasing the affinity for chitin, CBM had no major effect on kinetic properties of HCHT.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Quitina/química
Quitinases/química
Quitosana/química
Hexosaminidases/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Catálise
Domínio Catalítico
Quitina/análogos & derivados
Quitinases/genética
Hexosaminidases/genética
Seres Humanos
Imunidade Inata/genética
Cinética
Serratia marcescens/enzimologia
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (oligochitosan); 1398-61-4 (Chitin); 9012-76-4 (Chitosan); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.- (chitotriosidase); EC 3.2.1.14 (Chitinases); EC 3.2.1.14 (chitinase A, Serratia marcescens)
[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:170128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0171042


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[PMID]:28103924
[Au] Autor:Ceravolo F; Grisolia M; Sestito S; Falvo F; Moricca MT; Concolino D
[Ad] Endereço:Pediatrics Unit, Department of Medical and Surgical Science, University "Magna Graecia", Catanzaro, Italy. geneticacatanzaro@gmail.com.
[Ti] Título:Combination therapy in a patient with chronic neuronopathic Gaucher disease: a case report.
[So] Source:J Med Case Rep;11(1):19, 2017 Jan 20.
[Is] ISSN:1752-1947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The variants of neuronopathic Gaucher disease may be viewed as a clinical phenotypic continuum divided into acute and chronic forms. The chronic neuronopathic form of Gaucher disease is characterized by a later onset of neurological symptoms and protracted neurological and visceral involvement. The first-choice treatment for nonneuronopathic Gaucher disease is enzyme replacement therapy with recombinant analogues of the deficient human enzyme glucocerebrosidase. Enzyme replacement therapy has been shown to improve hematological and bone manifestations associated with Gaucher disease, but, as with most proteins, recombinant enzymes cannot cross the blood-brain barrier, which prevents effects on neurological manifestations. Substrate reduction therapy with miglustat (N-butyldeoxynojirimycin) inhibits glucosylceramide synthase, which catalyzes the first step in glycosphingolipid synthesis. Because miglustat can cross the blood-brain barrier, it has been suggested that, combined with enzyme replacement therapy, it might be effective in treating neurological symptoms in patients with neuronopathic Gaucher disease. CASE PRESENTATION: We report observed effects of combined enzyme replacement therapy and substrate reduction therapy in a 7-year-old Caucasian boy with neuronopathic Gaucher disease who was homozygous for L444P mutations. He had received enzyme replacement therapy from the age of 18 months, and concomitant miglustat treatment was commenced, with dosing according to body surface area uptitrated over 1 month with dietary modifications when he reached the age of 30 months. He experienced mild diarrhea after commencing miglustat therapy, which decreased in frequency/severity over time. His splenomegaly was reduced, and his hematological values and plasma angiotensin-converting enzyme activity normalized. Plasma chitotriosidase also showed substantial and sustained decreases. After 5 years of combination therapy, the patient showed no signs of neurological impairment. CONCLUSIONS: This case supports the concept that oral miglustat in combination with intravenous enzyme replacement therapy may be beneficial in preventing neurological signs in patients with chronic neuronopathic Gaucher disease. The importance of dietary modifications has also been confirmed. Further follow-up studies are needed to better define the therapeutic effect of combined treatment in this Gaucher disease subtype.
[Mh] Termos MeSH primário: 1-Desoxinojirimicina/análogos & derivados
Inibidores Enzimáticos/administração & dosagem
Terapia de Reposição de Enzimas
Doença de Gaucher/terapia
[Mh] Termos MeSH secundário: 1-Desoxinojirimicina/administração & dosagem
Administração Intravenosa
Barreira Hematoencefálica/fisiopatologia
Criança
Doença Crônica
Terapia Combinada
Glucosilceramidase/deficiência
Hexosaminidases/sangue
Seres Humanos
Masculino
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 19130-96-2 (1-Deoxynojirimycin); ADN3S497AZ (miglustat); EC 3.2.1.- (Hexosaminidases); EC 3.2.1.- (chitotriosidase); EC 3.2.1.45 (Glucosylceramidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1186/s13256-016-1147-5



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