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[PMID]:28408497
[Au] Autor:Alonzi DS; Scott KA; Dwek RA; Zitzmann N
[Ad] Endereço:Department of Biochemistry, Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
[Ti] Título:Iminosugar antivirals: the therapeutic sweet spot.
[So] Source:Biochem Soc Trans;45(2):571-582, 2017 Apr 15.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Many viruses require the host endoplasmic reticulum protein-folding machinery in order to correctly fold one or more of their glycoproteins. Iminosugars with glucose stereochemistry target the glucosidases which are key for entry into the glycoprotein folding cycle. Viral glycoproteins are thus prevented from interacting with the protein-folding machinery leading to misfolding and an antiviral effect against a wide range of different viral families. As iminosugars target host enzymes, they should be refractory to mutations in the virus. Iminosugars therefore have great potential for development as broad-spectrum antiviral therapeutics. We outline the mechanism giving rise to the antiviral activity of iminosugars, the current progress in the development of iminosugar antivirals and future prospects for this field.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Glucosidases/antagonistas & inibidores
Imino Açúcares/farmacologia
[Mh] Termos MeSH secundário: Animais
Antivirais/química
Antivirais/uso terapêutico
Ensaios Clínicos como Assunto
Doenças Transmissíveis/tratamento farmacológico
Doenças Transmissíveis/virologia
Retículo Endoplasmático/enzimologia
Seres Humanos
Imino Açúcares/química
Imino Açúcares/uso terapêutico
Dobramento de Proteína/efeitos dos fármacos
Proteínas Virais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Imino Sugars); 0 (Viral Proteins); EC 3.2.1.- (Glucosidases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE
[do] DOI:10.1042/BST20160182


  2 / 4112 MEDLINE  
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[PMID]:28375157
[Au] Autor:Besse W; Dong K; Choi J; Punia S; Fedeles SV; Choi M; Gallagher AR; Huang EB; Gulati A; Knight J; Mane S; Tahvanainen E; Tahvanainen P; Sanna-Cherchi S; Lifton RP; Watnick T; Pei YP; Torres VE; Somlo S
[Ti] Título:Isolated polycystic liver disease genes define effectors of polycystin-1 function.
[So] Source:J Clin Invest;127(5):1772-1785, 2017 May 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dominantly inherited isolated polycystic liver disease (PCLD) consists of liver cysts that are radiologically and pathologically identical to those seen in autosomal dominant polycystic kidney disease, but without clinically relevant kidney cysts. The causative genes are known for fewer than 40% of PCLD index cases. Here, we have used whole exome sequencing in a discovery cohort of 102 unrelated patients who were excluded for mutations in the 2 most common PCLD genes, PRKCSH and SEC63, to identify heterozygous loss-of-function mutations in 3 additional genes, ALG8, GANAB, and SEC61B. Similarly to PRKCSH and SEC63, these genes encode proteins that are integral to the protein biogenesis pathway in the endoplasmic reticulum. We inactivated these candidate genes in cell line models to show that loss of function of each results in defective maturation and trafficking of polycystin-1, the central determinant of cyst pathogenesis. Despite acting in a common pathway, each PCLD gene product demonstrated distinct effects on polycystin-1 biogenesis. We also found enrichment on a genome-wide basis of heterozygous mutations in the autosomal recessive polycystic kidney disease gene PKHD1, indicating that adult PKHD1 carriers can present with clinical PCLD. These findings define genetic and biochemical modulators of polycystin-1 function and provide a more complete definition of the spectrum of dominant human polycystic diseases.
[Mh] Termos MeSH primário: Cistos
Glucosiltransferases
Heterozigoto
Hepatopatias
Mutação
Canais de Translocação SEC
Canais de Cátion TRPP
[Mh] Termos MeSH secundário: Adulto
Animais
Linhagem Celular Transformada
Cistos/genética
Cistos/metabolismo
Retículo Endoplasmático/genética
Retículo Endoplasmático/metabolismo
Feminino
Estudo de Associação Genômica Ampla
Glucosidases/genética
Glucosidases/metabolismo
Glucosiltransferases/genética
Glucosiltransferases/metabolismo
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Hepatopatias/genética
Hepatopatias/metabolismo
Masculino
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Camundongos
Canais de Translocação SEC/genética
Canais de Translocação SEC/metabolismo
Canais de Cátion TRPP/biossíntese
Canais de Cátion TRPP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (PRKCSH protein, human); 0 (SEC Translocation Channels); 0 (SEC61B protein, human); 0 (SEC63 protein, human); 0 (TRPP Cation Channels); 0 (polycystic kidney disease 1 protein); EC 2.4.1.- (ALG8 protein, human); EC 2.4.1.- (Glucosyltransferases); EC 3.2.1.- (Glucosidases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE


  3 / 4112 MEDLINE  
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[PMID]:28302960
[Au] Autor:Shoda SI
[Ad] Endereço:Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University.
[Ti] Título:Development of chemical and chemo-enzymatic glycosylations.
[So] Source:Proc Jpn Acad Ser B Phys Biol Sci;93(3):125-145, 2017.
[Is] ISSN:1349-2896
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Glycosidic compounds are indispensable molecules in living systems. Biological phenomena such as cell wall formation, energy storage, and cell recognition strongly depend on the multi-functional characters of these substances. Development of highly regio- and stereoselective glycosylation reactions is necessary to provide sufficient amounts of specific compounds in basic research as well as for applications in industry. This review presents an overview of chemical and chemo-enzymatic glycosylations that have been developed during my forty-year academic career in the field of glyco-science. In the course of these studies, several new concepts such as "Direct Anomeric Activation", "Glyco-Process Chemistry" and "Glyco-Chemistry Cycles" have been established.
[Mh] Termos MeSH primário: Glucosidases/metabolismo
[Mh] Termos MeSH secundário: Glucosidases/genética
Glicosídeos/química
Glicosídeos/metabolismo
Glicosilação
Estereoisomerismo
Especificidade por Substrato
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Glycosides); 059QF0KO0R (Water); EC 3.2.1.- (Glucosidases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE
[do] DOI:10.2183/pjab.93.008


  4 / 4112 MEDLINE  
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[PMID]:28266734
[Au] Autor:Avula S; Nguyen TM; Marble M; Lilje C
[Ad] Endereço:Department of Pediatrics (Cardiology), Louisiana State University Health Sciences Center, New Orleans, LA, USA.
[Ti] Título:Cardiac response to enzyme replacement therapy in infantile Pompe disease with severe hypertrophic cardiomyopathy.
[So] Source:Echocardiography;34(4):621-624, 2017 Apr.
[Is] ISSN:1540-8175
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Classic infantile-onset Pompe disease (IOPD), characterized by predominantly cardiac involvement, used to be considered uniformly lethal within months. The availability of enzyme replacement therapy (ERT) has transformed the course of the disease. Decrease in ventricular hypertrophy and improvement in ventricular function have been suggested as proof for efficacy. We report the cardiac response to ERT of a child with IOPD and severe hypertrophic cardiomyopathy. The myocardial hypertrophy resolved. Change in ejection fraction, however, was slow. We discuss the potential benefit of other parameters beyond ejection to assess cardiac function in IOPD, including speckle tracking-based strain.
[Mh] Termos MeSH primário: Cardiomiopatia Hipertrófica/complicações
Cardiomiopatia Hipertrófica/tratamento farmacológico
Terapia de Reposição de Enzimas/métodos
Doença de Depósito de Glicogênio Tipo II/complicações
Doença de Depósito de Glicogênio Tipo II/tratamento farmacológico
[Mh] Termos MeSH secundário: Acarbose/uso terapêutico
Cardiomiopatia Hipertrófica/diagnóstico por imagem
Ecocardiografia
Ecocardiografia Doppler
Feminino
Glucosidases/uso terapêutico
Doença de Depósito de Glicogênio Tipo II/diagnóstico por imagem
Inibidores de Glicosídeo Hidrolases/uso terapêutico
Seres Humanos
Lactente
Resultado do Tratamento
[Pt] Tipo de publicação:CASE REPORTS
[Nm] Nome de substância:
0 (Glycoside Hydrolase Inhibitors); EC 3.2.1.- (Glucosidases); T58MSI464G (Acarbose)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1111/echo.13490


  5 / 4112 MEDLINE  
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[PMID]:28089449
[Au] Autor:Light SH; Cahoon LA; Mahasenan KV; Lee M; Boggess B; Halavaty AS; Mobashery S; Freitag NE; Anderson WF
[Ad] Endereço:Department of Biochemistry and Molecular Genetics, Center for Structural Genomics of Infectious Diseases, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
[Ti] Título:Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.
[So] Source:Structure;25(2):295-304, 2017 Feb 07.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Active in the aqueous cellular environment where a massive excess of water is perpetually present, enzymes that catalyze the transfer of an electrophile to a non-water nucleophile (transferases) require specific strategies to inhibit mechanistically related hydrolysis reactions. To identify principles that confer transferase versus hydrolase reaction specificity, we exploited two enzymes that use highly similar catalytic apparatuses to catalyze the transglycosylation (a transferase reaction) or hydrolysis of α-1,3-glucan linkages in the cyclic tetrasaccharide cycloalternan (CA). We show that substrate binding to non-catalytic domains and a conformationally stable active site promote CA transglycosylation, whereas a distinct pattern of active site conformational change is associated with CA hydrolysis. These findings defy the classic view of induced-fit conformational change and illustrate a mechanism by which a stable hydrophobic binding site can favor transferase activity and disfavor hydrolysis. Application of these principles could facilitate the rational reengineering of transferases with desired catalytic properties.
[Mh] Termos MeSH primário: Actinomycetales/enzimologia
Glucosidases/química
Glicosídeo Hidrolases/química
Listeria monocytogenes/enzimologia
Oligossacarídeos/química
Água/química
[Mh] Termos MeSH secundário: Actinomycetales/genética
Motivos de Aminoácidos
Sítios de Ligação
Biocatálise
Configuração de Carboidratos
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glucosidases/genética
Glucosidases/metabolismo
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Glicosilação
Hidrólise
Interações Hidrofóbicas e Hidrofílicas
Cinética
Listeria monocytogenes/genética
Modelos Moleculares
Oligossacarídeos/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligosaccharides); 0 (Recombinant Proteins); 0 (cycloalternan); 059QF0KO0R (Water); EC 3.2.1.- (Glucosidases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.- (alternanase); EC 3.2.1.- (cycloalternan-degrading enzyme, Bacillus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE


  6 / 4112 MEDLINE  
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[PMID]:28064042
[Au] Autor:Totani K; Yamaya K; Hirano M; Ito Y
[Ad] Endereço:Department of Materials and Life Science, Seikei University, 3-3-1 Kichijoji-kitamachi, Musashino, Tokyo, 180-8633, Japan. Electronic address: ktotani@st.seikei.ac.jp.
[Ti] Título:Influence of aglycone structures on N-glycan processing reactions in the endoplasmic reticulum.
[So] Source:Carbohydr Res;439:16-22, 2017 Feb 01.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Glycoprotein N-linked oligosaccharides in the endoplasmic reticulum function as tags to regulate glycoprotein folding, sorting, secretion and degradation. Since the N-glycan structure of a glycoprotein should reflect the folding state, N-glycan processing may be affected by the aglycone state. In this study, we examined the influence of aglycone structures on N-glycan processing using synthetic substrates. We prepared (Glc )Man GlcNAc linked to hydrophobic BODIPY-dye with a systematic series of different linker lengths. With these compounds, glucose transfer, glucose trimming and mannose trimming reactions of an endoplasmic reticulum fraction were examined. The results showed that substrates with shorter linkers between the N-glycan and hydrophobic patch had higher activities for both the glucose transfer and the mannose trimming reactions. In contrast, the glucose trimming reaction showed lower activity when substrates had shorter linkers. Thus, the reactivity for N-linked oligosaccharide processing of glycoproteins in the endoplasmic reticulum might be tunable by the aglycone structure, e.g., protein portion of glycoproteins.
[Mh] Termos MeSH primário: Calreticulina/metabolismo
Retículo Endoplasmático/metabolismo
Glucosidases/metabolismo
Glucosiltransferases/metabolismo
Glicoproteínas/metabolismo
Manosidases/metabolismo
[Mh] Termos MeSH secundário: Acetilglucosamina/química
Acetilglucosamina/metabolismo
Animais
Compostos de Boro/química
Compostos de Boro/metabolismo
Calreticulina/química
Sequência de Carboidratos
Fracionamento Celular
Retículo Endoplasmático/química
Corantes Fluorescentes/química
Corantes Fluorescentes/metabolismo
Glucose/química
Glucose/metabolismo
Glucosidases/química
Glucosiltransferases/química
Glicoproteínas/química
Glicosilação
Hepatócitos/química
Hepatócitos/metabolismo
Interações Hidrofóbicas e Hidrofílicas
Fígado/química
Fígado/metabolismo
Masculino
Manose/química
Manose/metabolismo
Manosidases/química
Camundongos
Camundongos Endogâmicos C57BL
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene); 0 (Boron Compounds); 0 (Calreticulin); 0 (Fluorescent Dyes); 0 (Glycoproteins); EC 2.4.1.- (Glucosyltransferases); EC 3.2.1.- (Glucosidases); EC 3.2.1.- (Mannosidases); IY9XDZ35W2 (Glucose); PHA4727WTP (Mannose); V956696549 (Acetylglucosamine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170213
[Lr] Data última revisão:
170213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170109
[St] Status:MEDLINE


  7 / 4112 MEDLINE  
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[PMID]:27965112
[Au] Autor:Grbavac A; Canak I; Stuparevic I; Teparic R; Mrsa V
[Ad] Endereço:Laboratory of Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, Pierottijeva 6, 10 000 Zagreb, Croatia.
[Ti] Título:Proteolytic processing of the Saccharomyces cerevisiae cell wall protein Scw4 regulates its activity and influences its covalent binding to glucan.
[So] Source:Biochim Biophys Acta;1864(3):507-515, 2017 03.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Yeast cell wall contains a number of proteins that are either non-covalently (Scw-proteins), or covalently (Ccw-proteins) bound to ß-1,3-glucan, the latter either through GPI-anchors and ß-1,6-glucan, or by alkali labile ester linkages between γ-carboxyl groups of glutamic acid and hydroxyl groups of glucoses (Pir-proteins). It was shown that a part of Scw4, previously identified among the non-covalently bound cell wall proteins, was covalently attached to wall polysaccharides by a so far unknown alkali sensitive linkage. Thus Scw4 could be released from cell walls by treatments with hot SDS, mild alkali, or ß-1,3-glucanases, respectively. It was further shown that non-covalently bound Scw4 (SDS released) underwent the Kex2 proteolytic processing. In this paper it was demonstrated that Scw4 was also processed by yapsins at a position 9 amino acids downstream of the Kex2 cleavage site. Scw4 cleaved at the yapsin site had a markedly lower potential for covalent attachment to glucan. The overproduction of the fully processed form of Scw4 lead to high mortality, particularly in the stationary phase of growth, and to markedly increased cell size. On the other hand, the overproduction of Scw4 processed only by Kex2 or not processed at all had no apparent change in mortality indicating that only the smallest, completely mature form of Scw4 had the activity leading to observed phenotype changes.
[Mh] Termos MeSH primário: Parede Celular/metabolismo
Glucosidases/metabolismo
Pró-Proteína Convertases/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Ácido Aspártico Endopeptidases/genética
Ácido Aspártico Endopeptidases/metabolismo
Tamanho Celular
Parede Celular/química
Expressão Gênica
Glucosidases/genética
Isoenzimas/genética
Isoenzimas/metabolismo
Viabilidade Microbiana
Fenótipo
Plasmídeos/química
Plasmídeos/metabolismo
Pró-Proteína Convertases/genética
Ligação Proteica
Proteólise
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (beta-Glucans); 37361-00-5 (beta-1,6-glucan); 9051-97-2 (beta-1,3-glucan); EC 3.2.1.- (Glucosidases); EC 3.2.1.- (Scw4 protein, S cerevisiae); EC 3.4.21.- (Proprotein Convertases); EC 3.4.21.61 (KEX2 protein, S cerevisiae); EC 3.4.23.- (Aspartic Acid Endopeptidases); EC 3.4.23.25 (YPS1 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161215
[St] Status:MEDLINE


  8 / 4112 MEDLINE  
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[PMID]:27928754
[Au] Autor:Nawaz MA; Bibi Z; Karim A; Rehman HU; Jamal M; Jan T; Aman A; Qader SA
[Ad] Endereço:Department of Biotechnology, Shaheed Benazir Bhutto University, Sheringal, Dir Upper, KPK, Pakistan. asif_biotech33@sbbu.edu.pk.
[Ti] Título:Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel.
[So] Source:Environ Sci Pollut Res Int;24(4):4058-4066, 2017 Feb.
[Is] ISSN:1614-7499
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable substrate for the maximum synthesis of α-1,4-glucosidase among various agro-industrial residues. Bacillus licheniformis KIBGE-IB4 produced 6533.0 U ml of α-1,4-glucosidase when growth medium was supplemented with 1% dried and crushed sweet potato peel. It was evident from the results that bacterial isolate secreted 6539.0 U ml of α-1,4-glucosidase in the presence of 0.4% peptone and meat extract with 0.1% yeast extract. B. licheniformis KIBGE-IB4 released 6739.0 and 7190.0 U ml of enzyme at 40 °C and pH 7.0, respectively. An improved and cost-effective growth medium design resulted 8590.0 U ml of α-1,4-glucosidase with 1.3-fold increase as compared to initial amount from B. licheniformis KIBGE-IB4. This enzyme can be used to fulfill the accelerating demand of food and pharmaceutical industries. Further purification and immobilization of this enzyme can also enhance its utility for various commercial applications. Graphical abstract Pictorial representation of maltase production from sweet potato peel.
[Mh] Termos MeSH primário: Bacillus licheniformis/enzimologia
Glucosidases/metabolismo
Ipomoea batatas/metabolismo
[Mh] Termos MeSH secundário: Carbono/metabolismo
Meios de Cultura
Concentração de Íons de Hidrogênio
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 7440-44-0 (Carbon); EC 3.2.1.- (Glucosidases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171104
[Lr] Data última revisão:
171104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161209
[St] Status:MEDLINE
[do] DOI:10.1007/s11356-016-8168-x


  9 / 4112 MEDLINE  
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[PMID]:27889542
[Au] Autor:Yang JB; Tian JY; Dai Z; Ye F; Ma SC; Wang AG
[Ad] Endereço:State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, People's Republic of China.
[Ti] Título:a-Glucosidase inhibitors extracted from the roots of Polygonum multiflorum Thunb.
[So] Source:Fitoterapia;117:65-70, 2017 Mar.
[Is] ISSN:1873-6971
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A novel stilbene glucoside, polygonumnolide D (1), and a novel dianthrone glycoside, polygonumnolide E (2), were isolated from a 70% EtOH extract of the dried roots of Polygonum multiflorum Thunb., together with six known compounds (3-8). Their structures were elucidated by 1D and 2D NMR as well as mass spectroscopy data. The isolated compounds were evaluated for their a-glucosidase inhibitory activities in vitro. Compounds 1, 2 and 5 showed the inhibitory activity against a-glucosidase with the IC values of 2.4, 2.7 and 0.3µM, respectively.
[Mh] Termos MeSH primário: Fallopia multiflora/química
Glucosidases/antagonistas & inibidores
Glucosídeos/química
Glicosídeos/química
Estilbenos/química
[Mh] Termos MeSH secundário: Inibidores Enzimáticos/química
Inibidores Enzimáticos/isolamento & purificação
Glucosídeos/isolamento & purificação
Glicosídeos/isolamento & purificação
Estrutura Molecular
Extratos Vegetais/química
Raízes de Plantas/química
Estilbenos/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Glucosides); 0 (Glycosides); 0 (Plant Extracts); 0 (Stilbenes); 0 (polygonumnolide D); 0 (polygonumnolide E); EC 3.2.1.- (Glucosidases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170307
[Lr] Data última revisão:
170307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161128
[St] Status:MEDLINE


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[PMID]:27743105
[Au] Autor:Abd El-Hady FK; Fayad W; Iodice C; El-Shahid ZA; Abdel-Aziz MS; Crudele E; Tommonaro G
[Ad] Endereço:Chemistry of Natural Products Department, National Research Center, Giza, Egypt.
[Ti] Título:Investigating on the Correlation Between Some Biological Activities of Marine Sponge-Associated Bacteria Extracts and Isolated Diketopiperazines.
[So] Source:Curr Microbiol;74(1):6-13, 2017 Jan.
[Is] ISSN:1432-0991
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Marine organisms have been considered as the richest sources of novel bioactive metabolites, which can be used for pharmaceutical purposes. In the last years, the interest for marine microorganisms has grown for their enormous biodiversity and for the evidence that many novel compounds isolated from marine invertebrates are really synthesized by their associated bacteria. Nevertheless, the discovery of a chemical communication Quorum sensing (QS) between bacterial cells and between bacteria and host has gained the researchers to expand the aim of their study toward the role of bacteria associated with marine invertebrates, such as marine sponge. In the present paper, we report the evaluation of biological activities of different extracts of bacteria Vibrio sp. and Bacillus sp. associated with marine sponges Dysidea avara and Ircinia variabilis, respectively. Moreover, we evaluated the biological activities of some diketopiperazines (DKPs), previously isolated, and able to activate QS mechanism. The results showed that all extracts, fractions, and DKPs showed low scavenging activity against DPPH and superoxide anion, low cytotoxic and anti-tyrosinase activities, but no antimicrobial and acetylcholinesterase inhibitory activities. One DKP [cyclo-(trans-4-hydroxy-L-prolyl-L-leucine)] has the highest α-glucosidase inhibitory activity even than the standard acarbose.
[Mh] Termos MeSH primário: Bactérias/química
Dicetopiperazinas/farmacologia
Poríferos/microbiologia
[Mh] Termos MeSH secundário: Animais
Antioxidantes/química
Antioxidantes/metabolismo
Antioxidantes/farmacologia
Bactérias/classificação
Bactérias/genética
Bactérias/isolamento & purificação
Biodiversidade
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Dicetopiperazinas/análise
Dicetopiperazinas/metabolismo
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/farmacologia
Glucosidases/análise
Glucosidases/antagonistas & inibidores
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Diketopiperazines); 0 (Enzyme Inhibitors); EC 3.2.1.- (Glucosidases)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161016
[St] Status:MEDLINE
[do] DOI:10.1007/s00284-016-1144-3



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