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  1 / 1903 MEDLINE  
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[PMID]:29353723
[Au] Autor:Wu YZ; Zhang HW; Sun ZH; Dai JG; Hu YC; Li R; Lin PC; Xia GY; Wang LY; Qiu BL; Zhang JF; Ge GB; Lin S
[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, China.
[Ti] Título:Bysspectin A, an unusual octaketide dimer and the precursor derivatives from the endophytic fungus Byssochlamys spectabilis IMM0002 and their biological activities.
[So] Source:Eur J Med Chem;145:717-725, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Bysspectin A (1), a polyketide-derived octaketide dimer with a novel carbon skeleton, and two new precursor derivatives, bysspectins B and C (2 and 3), were obtained from an organic extract of the endophytic fungus Byssochlamys spectabilis that had been isolated from a leaf tissue of the traditional Chinese medicinal plant Edgeworthia chrysantha, together with a known octaketide, paecilocin A (4). Their structures were determined by HRMS, 1D and 2D NMR spectroscopic analysis. A plausible route for their biosynthetic pathway is proposed. Compounds 1-3 were tested for their antimicrobial activities. Only compound 3 was weakly active against Escherichia coli and Staphyloccocus aureus with MIC values of 32 and 64 µg/mL, respectively. Further, the inhibitory effects on human carboxylesterases (hCE1, hCE2) of compounds 1 and 4 were evaluated. The results demonstrated that bysspectin A (1) was a novel and highly selective inhibitor against hCE2 with the IC value of 2.01 µM. Docking simulation also demonstrated that active compound 1 created interaction with the Ser-288 (the catalytic amino-acid in the catalytic cavity) of hCE2 via hydrogen bonding, revealing its highly selective inhibition toward hCE2.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Byssochlamys/química
Carboxilesterase/antagonistas & inibidores
Hidrolases de Éster Carboxílico/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Escherichia coli/efeitos dos fármacos
Policetídeos/farmacologia
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Antibacterianos/química
Antibacterianos/isolamento & purificação
Biocatálise
Carboxilesterase/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Dimerização
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Inibidores Enzimáticos/isolamento & purificação
Seres Humanos
Testes de Sensibilidade Microbiana
Simulação de Acoplamento Molecular
Estrutura Molecular
Policetídeos/química
Policetídeos/isolamento & purificação
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Enzyme Inhibitors); 0 (Polyketides); 0 (bysspectin A); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.1 (CES1 protein, human); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180123
[St] Status:MEDLINE


  2 / 1903 MEDLINE  
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[PMID]:29264996
[Au] Autor:Chen F; Zhang B; Parker RB; Laizure SC
[Ad] Endereço:a Department of Clinical Pharmacy , College of Pharmacy, University of Tennessee Health Science Center , Memphis , TN , USA.
[Ti] Título:Clinical implications of genetic variation in carboxylesterase drug metabolism.
[So] Source:Expert Opin Drug Metab Toxicol;14(2):131-142, 2018 Feb.
[Is] ISSN:1744-7607
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Mammalian carboxylesterase enzymes are a highly conserved metabolic pathway involved in the metabolism of endogenous and exogenous compounds including many widely prescribed therapeutic agents. Recent advances in our understanding of genetic polymorphisms affecting enzyme activity have exposed potential therapeutic implications. Areas covered: The aims of this review are to provide an overview of carboxylesterase 1 (CES1) and carboxylesterase 2 (CES2) gene structure, to summarize the known polymorphism affecting substrate-drug metabolism, and to assess the potential therapeutic implications of genetic variations affecting enzyme function. Expert opinion: Genetic variability in carboxylesterase drug metabolism is a nascent area of research with only a handful of the thousands of SNPs investigated for their potential effects of enzyme activity or carboxylesterase-substrate disposition and therapeutics. It remains to be determined if the wide variability in enzyme activity can be explained by genetic variation, and used in personalized medicine to improve clinical outcomes.
[Mh] Termos MeSH primário: Carboxilesterase/genética
Hidrolases de Éster Carboxílico/genética
Preparações Farmacêuticas/metabolismo
[Mh] Termos MeSH secundário: Carboxilesterase/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Variação Genética
Seres Humanos
Preparações Farmacêuticas/administração & dosagem
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Pharmaceutical Preparations); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.1 (CES1 protein, human); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1080/17425255.2018.1420164


  3 / 1903 MEDLINE  
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[PMID]:29188674
[Au] Autor:Ding BF; Shao L; Zhang RS; Liang C; Zhang YR
[Ad] Endereço:College of Life and Environmental Sciences, Shanghai Normal University, Shanghai 200234, China.
[Ti] Título:[Research Progress on Abused Drugs Metabolic in vivo].
[So] Source:Fa Yi Xue Za Zhi;32(4):290-295, 2016 Aug.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Under the catalysis of a variety of metabolic enzymes , such as UDP-glucuronyl transferases, cytochrome P450, carboxylesterase, sulfotransferase, butyrylcholinesterase, catechol- -methyl transferase and 6-morphine dehydrogenase, the drugs perform glucuronidation, hydrolysis, oxidation, sulfonation and other reactions, then translate into active or inactive metabolites, which are excreted through urination, bile or the other pathways at last. Different drugs own their different metabolic pathways. This paper introduces the studies about the metabolism of drugs in human and animal in recent years, such as morphine-like drugs, amphetamine, ketamine, cannabis and cocaine, and reviews the research progress about the sites of metabolism, metabolic enzymes, metabolites and physiological activity of those drugs metabolic .
[Mh] Termos MeSH primário: Colinesterases/metabolismo
Sistema Enzimático do Citocromo P-450/metabolismo
Glucuronosiltransferase/metabolismo
Drogas Ilícitas/metabolismo
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/metabolismo
Animais
Carboxilesterase/metabolismo
Catecol O-Metiltransferase/metabolismo
Seres Humanos
Oxirredução
Sulfotransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Street Drugs); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.218 (morphine 6-dehydrogenase); EC 2.1.1.6 (Catechol O-Methyltransferase); EC 2.4.1.17 (Glucuronosyltransferase); EC 2.8.2.- (Sulfotransferases); EC 3.1.1.1 (Carboxylesterase); EC 3.1.1.8 (Cholinesterases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2016.04.013


  4 / 1903 MEDLINE  
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[PMID]:28470863
[Au] Autor:Ravikumar G; Bagheri M; Saini DK; Chakrapani H
[Ad] Endereço:Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune, 411008, Maharashtra, India.
[Ti] Título:FLUORO/NO: A Nitric Oxide Donor with a Fluorescence Reporter.
[So] Source:Chembiochem;18(15):1529-1534, 2017 08 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Nitric oxide (NO) plays significant signalling roles in cells; the controlled generation of NO is of therapeutic relevance. Although a number of methods for the delivery and detection of NO are available, these events are typically mutually exclusive. Furthermore, the efficiency of delivery of NO can be compromised by detection technologies that consume NO. Here, we report FLUORO/NO, an esterase-activated diazeniumdiolate-based NO donor with an in-built fluorescence reporter. We demonstrate that this compound is capable of enhancing NO within cells in a dose-dependent manner, accompanied by a similar increase in fluorescence. The compatibility of this tool to study NO-mediated signalling as well as NO-mediated stress is demonstrated. FLUORO/NO is a convenient tool that shows NO-like activity and allows monitoring of NO release. This tool will help interrogate the redox biology of NO.
[Mh] Termos MeSH primário: Cumarínicos/farmacologia
Doadores de Óxido Nítrico/farmacologia
Triazenos/farmacologia
Triazinas/farmacologia
Umbeliferonas/farmacologia
[Mh] Termos MeSH secundário: Carboxilesterase/metabolismo
Cumarínicos/síntese química
Dano ao DNA
Fluorescência
Células HEK293
Células HeLa
Seres Humanos
Óxido Nítrico/metabolismo
Doadores de Óxido Nítrico/síntese química
Nitritos/análise
Guanilil Ciclase Solúvel/metabolismo
Estereoisomerismo
Triazenos/síntese química
Triazinas/síntese química
Umbeliferonas/síntese química
Valeratos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coumarins); 0 (FLUORO-NO compound); 0 (Nitric Oxide Donors); 0 (Nitrites); 0 (Triazenes); 0 (Triazines); 0 (Umbelliferones); 0 (Valerates); 31C4KY9ESH (Nitric Oxide); EC 3.1.1.1 (Carboxylesterase); EC 4.6.1.2 (Soluble Guanylyl Cyclase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700155


  5 / 1903 MEDLINE  
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[PMID]:29253734
[Au] Autor:Wang AH; Tian XG; Cui YL; Huo XK; Zhang BJ; Deng S; Feng L; Ma XC; Jia JM; Wang C
[Ad] Endereço:School of Traditional Chinese Materia Medica, Shenyang Pharmaceutical University, Shenyang 110016, People's Republic of China; College of Pharmacy, Academy of Integrative Medicine, Dalian Medical University, Dalian 116044, People's Republic of China.
[Ti] Título:Diterpenoids from the roots of Euphorbia ebracteolata and their inhibitory effects on human carboxylesterase 2.
[So] Source:Phytochemistry;146:82-90, 2018 Feb.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A chemical investigation of the roots of Euphorbia ebracteolata identified eighteen diterpenoids and glycosides. On the basis of spectroscopic data, they were determined to be ent-kauranes, ent-atisanes, tigliane derivatives, ingenane, and ent-abietanes, among which were eleven previously undescribed diterpenoids. The inhibitory effects of the isolated compounds against human carboxylesterase 2 (hCE-2) were evaluated in vitro, which revealed moderate inhibitory effects with IC values < 50 µM. Next, the inhibitory kinetics were evaluated for the putative hCE-2 inhibitor 4ß,9α,16,20-tetrahydroxy-14(13 → 12)-abeo-12αH-1,6-tigliadiene-3,13-dione (IC 3.88 µM), and results indicated competitive inhibition with K 4.94 µM. Additionally, none of the diterpenoids showed cytotoxic effects against five human tumor cell lines as determined by MTT assays.
[Mh] Termos MeSH primário: Carboxilesterase/antagonistas & inibidores
Diterpenos/farmacologia
Inibidores Enzimáticos/farmacologia
Euphorbia/química
Raízes de Plantas/química
[Mh] Termos MeSH secundário: Carboxilesterase/metabolismo
Diterpenos/química
Diterpenos/isolamento & purificação
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/química
Inibidores Enzimáticos/isolamento & purificação
Seres Humanos
Conformação Molecular
Estereoisomerismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Diterpenes); 0 (Enzyme Inhibitors); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE


  6 / 1903 MEDLINE  
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[PMID]:28945798
[Au] Autor:Piscitelli A; Tarallo V; Guarino L; Sannia G; Birolo L; Pezzella C
[Ad] Endereço:Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Napoli, Italy.
[Ti] Título:New lipases by mining of Pleurotus ostreatus genome.
[So] Source:PLoS One;12(9):e0185377, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The analysis of Pleurotus ostreatus genome reveals the presence of automatically annotated 53 lipase and 34 carboxylesterase putative coding-genes. Since no biochemical or physiological data are available so far, a functional approach was applied to identify lipases from P. ostreatus. In the tested growth conditions, four lipases were found expressed, with different patterns depending on the used C source. Two of the four identified proteins (PleoLip241 and PleoLip369), expressed in both analysed conditions, were chosen for further studies, such as an in silico analysis and their molecular characterization. To overcome limits linked to native production, a recombinant expression approach in the yeast Pichia pastoris was applied. Different expression levels were obtained: PleoLip241 reached a maximum activity of 4000 U/L, whereas PleoLip369 reached a maximum activity of 700 U/L. Despite their sequence similarity, these enzymes exhibited different substrate specificity and diverse stability at pH, temperature, and presence of metals, detergents and organic solvents. The obtained data allowed classifying PleoLip241 as belonging to the "true lipase" family. Indeed, by phylogenetic analysis the two proteins fall in different clusters. PleoLip241 was used to remove the hydrophobic layer from wool surface in order to improve its dyeability. The encouraging results obtained with lipase treated wool led to forecast PleoLip241 applicability in this field.
[Mh] Termos MeSH primário: Proteínas Fúngicas/genética
Genoma Fúngico
Lipase/genética
Pleurotus/enzimologia
Pleurotus/genética
[Mh] Termos MeSH secundário: Animais
Carboxilesterase/química
Carboxilesterase/genética
Carboxilesterase/metabolismo
Domínio Catalítico
Corantes
Mineração de Dados
Proteínas Fúngicas/química
Proteínas Fúngicas/metabolismo
Microbiologia Industrial
Cinética
Lipase/química
Lipase/metabolismo
Modelos Moleculares
Filogenia
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato

[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coloring Agents); 0 (Fungal Proteins); 0 (Recombinant Proteins); EC 3.1.1.1 (Carboxylesterase); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185377


  7 / 1903 MEDLINE  
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[PMID]:28929747
[Au] Autor:Hopkins DH; Fraser NJ; Mabbitt PD; Carr PD; Oakeshott JG; Jackson CJ
[Ad] Endereço:Research School of Chemistry, Australian National University , Canberra, Australian Capital Territory 0200, Australia.
[Ti] Título:Structure of an Insecticide Sequestering Carboxylesterase from the Disease Vector Culex quinquefasciatus: What Makes an Enzyme a Good Insecticide Sponge?
[So] Source:Biochemistry;56(41):5512-5525, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carboxylesterase (CBE)-mediated metabolic resistance to organophosphate and carbamate insecticides is a major problem for the control of insect disease vectors, such as the mosquito. The most common mechanism involves overexpression of CBEs that bind to the insecticide with high affinity, thereby sequestering them before they can interact with their target. However, the absence of any structure for an insecticide-sequestering CBE limits our understanding of the molecular basis for this process. We present the first structure of a CBE involved in sequestration, Cqestß2 , from the mosquito disease vector Culex quinquefasciatus. Lysine methylation was used to obtain the crystal structure of Cqestß2 , which adopts a canonical α/ß-hydrolase fold that has high similarity to the target of organophosphate and carbamate insecticides, acetylcholinesterase. Sequence similarity networks of the insect carboxyl/cholinesterase family demonstrate that CBEs associated with metabolic insecticide resistance across many species share a level of similarity that distinguishes them from a variety of other classes. This is further emphasized by the structural similarities and differences in the binding pocket and active site residues of Cqestß2 and other insect carboxyl/cholinesterases. Stopped-flow and steady-state inhibition studies support a major role for Cqestß2 in organophosphate resistance and a minor role in carbamate resistance. Comparison with another isoform associated with insecticide resistance, Cqestß1, showed both enzymes have similar affinity to insecticides, despite 16 amino acid differences between the two proteins. This provides a molecular understanding of pesticide sequestration by insect CBEs and could facilitate the design of CBE-specific inhibitors to circumvent this resistance mechanism in the future.
[Mh] Termos MeSH primário: Carboxilesterase/metabolismo
Culex/enzimologia
Proteínas de Insetos/metabolismo
Inseticidas/metabolismo
Modelos Moleculares
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Sítios de Ligação
Carbamatos/química
Carbamatos/metabolismo
Carboxilesterase/química
Carboxilesterase/genética
Domínio Catalítico
Cristalografia por Raios X
Proteínas de Insetos/química
Proteínas de Insetos/genética
Inseticidas/química
Cinética
Ligantes
Conformação Molecular
Mutação
Organofosfatos/química
Organofosfatos/metabolismo
Filogenia
Conformação Proteica
Dobramento de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Especificidade da Espécie
Umbeliferonas/química
Umbeliferonas/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbamates); 0 (Insect Proteins); 0 (Insecticides); 0 (Ligands); 0 (Organophosphates); 0 (Recombinant Proteins); 0 (Umbelliferones); EC 3.1.1.1 (Carboxylesterase)
[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:170921
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00774


  8 / 1903 MEDLINE  
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[PMID]:28760607
[Au] Autor:Wang AH; Huo XK; Feng L; Sun CP; Deng S; Zhang HL; Zhang BJ; Ma XC; Jia JM; Wang C
[Ad] Endereço:School of Traditional Chinese Materia Medica, Shenyang Pharmaceutical University, Shenyang 110016, People's Republic of China; College of Pharmacy, Academy of Integrative Medicine, Dalian Medical University, Dalian 116044, People's Republic of China.
[Ti] Título:Phenolic glycosides and monoterpenoids from the roots of Euphorbia ebracteolata and their bioactivities.
[So] Source:Fitoterapia;121:175-182, 2017 Sep.
[Is] ISSN:1873-6971
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The bioactive substance investigation of Euphorbia ebracteolata obtained 17 compounds by various chromatographic techniques. Their structures were elucidated using widely spectroscopic data, including ESI-MS, HRESI-MS, CD, 1D- and 2D-NMR, which gave 5 new phenolic glucosides and 4 new monoterpenoids. The phenolic glucosides and monoterpenoids showed the inhibitory effect against the human carboxylesterase-2 (hCE-2) using a fluorescence bioassay in vitro, with the strongest inhibitor compound 4 (IC 7.17µM). The antioxidant effects of these isolated compounds were evaluated using a DPPH scavenging assay. All of the phenolic acids displayed the DPPH scavenging effect, especially that eight compounds have better effect than vitamin C, with the IC values ranging from 4.52 to 7.52µM. Additionally, compounds 1-17 showed no cytotoxic effect against five human cancer cell lines by MTT assay.
[Mh] Termos MeSH primário: Euphorbia/química
Glicosídeos/química
Monoterpenos/química
Fenóis/química
[Mh] Termos MeSH secundário: Carboxilesterase/antagonistas & inibidores
Linhagem Celular Tumoral
Inibidores Enzimáticos/química
Inibidores Enzimáticos/isolamento & purificação
Depuradores de Radicais Livres/química
Depuradores de Radicais Livres/isolamento & purificação
Glicosídeos/isolamento & purificação
Seres Humanos
Estrutura Molecular
Monoterpenos/isolamento & purificação
Fenóis/isolamento & purificação
Extratos Vegetais/química
Raízes de Plantas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Free Radical Scavengers); 0 (Glycosides); 0 (Monoterpenes); 0 (Phenols); 0 (Plant Extracts); EC 3.1.1.1 (CES2 protein, human); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


  9 / 1903 MEDLINE  
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[PMID]:28719874
[Au] Autor:Freitas JS; Felício AA; Teresa FB; Alves de Almeida E
[Ad] Endereço:Graduate Program in Animal Biology, Department of Chemistry and Environmental Sciences, Universidade Estadual Paulista "Júlio de Mesquita Filho", Cristóvão Colombo, 2265, 15054-000 São José do Rio Preto, SP, Brazil. Electronic address: ju_freitass@hotmail.com.
[Ti] Título:Combined effects of temperature and clomazone (Gamit ) on oxidative stress responses and B-esterase activity of Physalaemus nattereri (Leiuperidae) and Rhinella schneideri (Bufonidae) tadpoles.
[So] Source:Chemosphere;185:548-562, 2017 Oct.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Temperature is an important factor influencing the toxicity of chemicals in aquatic environments. Neotropical tadpoles experience large temperature fluctuations in their habitats and many species are distributed in areas impacted by agriculture. This study evaluated the effects caused by the exposure to clomazone (Gamit ) at different temperatures (28, 32 and 36 °C) on biochemical stress responses and esterase activities in Physalaemus nattereri and Rhinella schneideri tadpoles. Results evidenced that temperature modulates the effects of clomazone on biochemical response of tadpoles. Antioxidant enzymes, including catalase, superoxide dismutase (SOD), and glucose-6-phosphate dehydrogenase had their activities increased by clomazone in P. nattereri treated at higher temperatures. The biotransformation enzyme glutathione-S-transferase (GST) was also induced by clomazone at 32 and 36 °C. In R. schneideri, clomazone failed to alter antioxidant enzymes at 28 °C, but SOD and GST were increased by clomazone at higher temperatures after three days. All enzymes had their activities returned to the control levels after eight days in R. schneideri. Lipid peroxidation was induced in both species exposed to clomazone at 32 and 36 °C, but not at 28 °C. Acetylcholinesterase was not sensitive to clomazone and temperature, while most treatments impaired carboxylesterase activity. Integrated biomarker response (IBR) was notably induced by temperature in both species, and a synergic effect of temperature and clomazone was mostly observed after three days of exposure. These findings imply that tadpoles from tropical areas may present differential responses in their physiological mechanism linked to antioxidant defense to deal with temperature fluctuations and agrochemicals presence in their habitats.
[Mh] Termos MeSH primário: Anuros/fisiologia
Esterases/metabolismo
Herbicidas/toxicidade
Isoxazóis/toxicidade
Oxazolidinonas/toxicidade
Estresse Oxidativo/fisiologia
[Mh] Termos MeSH secundário: Acetilcolinesterase/metabolismo
Animais
Antioxidantes/metabolismo
Bufonidae/fisiologia
Carboxilesterase/metabolismo
Catalase/metabolismo
Glutationa Transferase/metabolismo
Larva/efeitos dos fármacos
Peroxidação de Lipídeos/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Superóxido Dismutase/metabolismo
Temperatura Ambiente
Testes de Toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Herbicides); 0 (Isoxazoles); 0 (Oxazolidinones); 570RAC03NF (clomazone); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase); EC 2.5.1.18 (Glutathione Transferase); EC 3.1.- (Esterases); EC 3.1.1.1 (Carboxylesterase); EC 3.1.1.7 (Acetylcholinesterase)
[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:170719
[St] Status:MEDLINE


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[PMID]:28475833
[Au] Autor:Li D; Li Z; Chen W; Yang X
[Ad] Endereço:Shaanxi Engineering Laboratory for Food Green Processing and Safety Control, College of Food Engineering and Nutritional Science, Shaanxi Normal University , Xi'an 710062, China.
[Ti] Título:Imaging and Detection of Carboxylesterase in Living Cells and Zebrafish Pretreated with Pesticides by a New Near-Infrared Fluorescence Off-On Probe.
[So] Source:J Agric Food Chem;65(20):4209-4215, 2017 May 24.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A new near-infrared fluorescence off-on probe was developed and applied to fluorescence imaging of carboxylesterase in living HepG-2 cells and zebrafish pretreated with pesticides (carbamate, organophosphorus, and pyrethroid). The probe was readily prepared by connecting (4-acetoxybenzyl)oxy as a quenching and recognizing moiety to a stable hemicyanine skeleton that can be formed via the decomposition of IR-780. The fluorescence off-on response of the probe to carboxylesterase is based on the enzyme-catalyzed spontaneous hydrolysis of the carboxylic ester bond, followed by a further fragmentation of the phenylmethyl unit and thereby the fluorophore release. Compared with the only existing near-infrared carboxylesterase probe, the proposed probe exhibits superior analytical performance, such as near-infrared fluorescence emission over 700 nm as well as high selectivity and sensitivity, with a detection limit of 4.5 × 10 U/mL. More importantly, the probe is cell membrane permeable, and its applicability has been successfully demonstrated for monitoring carboxylesterase activity in living HepG-2 cells and zebrafish pretreated with pesticides, revealing that pesticides can effectively inhibit the activity of carboxylesterase. The superior properties of the probe make it of great potential use in indicating pesticide exposure.
[Mh] Termos MeSH primário: Carboxilesterase/química
Inibidores Enzimáticos/farmacologia
Praguicidas/farmacologia
Proteínas de Peixe-Zebra/química
[Mh] Termos MeSH secundário: Animais
Carboxilesterase/antagonistas & inibidores
Inibidores Enzimáticos/química
Corantes Fluorescentes/química
Células HeLa
Seres Humanos
Espectrometria de Fluorescência/métodos
Peixe-Zebra
Proteínas de Peixe-Zebra/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Fluorescent Dyes); 0 (Pesticides); 0 (Zebrafish Proteins); EC 3.1.1.1 (Carboxylesterase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170622
[Lr] Data última revisão:
170622
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b00959



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