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[PMID]:28467664
[Au] Autor:Gamella M; Privman M; Bakshi S; Melman A; Katz E
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, 13699-5810, USA.
[Ti] Título:DNA Release from Fe -Cross-Linked Alginate Films Triggered by Logically Processed Biomolecular Signals: Integration of Biomolecular Computing and Actuation.
[So] Source:Chemphyschem;18(13):1811-1821, 2017 Jul 05.
[Is] ISSN:1439-7641
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Signal-controlled release of DNA from Fe -cross-linked alginate hydrogel electrochemically deposited on an electrode surface was studied. The multiple input signals were logically processed with the help of the enzyme-biocatalyzed reactions. Boolean logic gates, OR, AND, INH, were realized with the biocatalytic reactions performed by the enzymes entrapped in the alginate film. Hydrogen peroxide produced by the enzymatic reactions resulted in the degradation of the alginate hydrogel and DNA release. The alginate degradation was facilitated by the formation of free radicals in the Fenton-type reaction catalyzed by iron cations cross-linking the alginate hydrogel. The studied approach is versatile and can be adapted to various chemical signals processed by various enzymes with differently implemented Boolean logic. This work illustrates a novel concept of functional integration of biomolecular computing and actuation.
[Mh] Termos MeSH primário: Alginatos/química
Computadores Moleculares
Reagentes para Ligações Cruzadas/química
DNA/metabolismo
Compostos Férricos/química
Lógica
[Mh] Termos MeSH secundário: Animais
Biocatálise
DNA/química
Esterases/química
Esterases/metabolismo
Glucose Oxidase/química
Glucose Oxidase/metabolismo
Ácido Glucurônico/química
Ácidos Hexurônicos/química
Peroxidase do Rábano Silvestre/química
Peroxidase do Rábano Silvestre/metabolismo
Lactato Desidrogenases/química
Lactato Desidrogenases/metabolismo
Oxigenases de Função Mista/química
Oxigenases de Função Mista/metabolismo
Nanopartículas/química
Nanopartículas/metabolismo
Dióxido de Silício/química
Dióxido de Silício/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alginates); 0 (Cross-Linking Reagents); 0 (Ferric Compounds); 0 (Hexuronic Acids); 7631-86-9 (Silicon Dioxide); 8A5D83Q4RW (Glucuronic Acid); 8C3Z4148WZ (alginic acid); 9007-49-2 (DNA); EC 1.- (Mixed Function Oxygenases); EC 1.1.- (Lactate Dehydrogenases); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.- (Horseradish Peroxidase); EC 1.13.12.4 (lactate 2-monooxygenase); EC 3.1.- (Esterases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1002/cphc.201700301


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[PMID]:28459537
[Au] Autor:McClure JJ; Inks ES; Zhang C; Peterson YK; Li J; Chundru K; Lee B; Buchanan A; Miao S; Chou CJ
[Ad] Endereço:Medical University of South Carolina , College of Pharmacy, Charleston, South Carolina, United States.
[Ti] Título:Comparison of the Deacylase and Deacetylase Activity of Zinc-Dependent HDACs.
[So] Source:ACS Chem Biol;12(6):1644-1655, 2017 06 16.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The acetylation status of lysine residues on histone proteins has long been attributed to a balance struck between the catalytic activity of histone acetyl transferases and histone deacetylases (HDAC). HDACs were identified as the sole removers of acetyl post-translational modifications (PTM) of histone lysine residues. Studies into the biological role of HDACs have also elucidated their role as removers of acetyl PTMs from lysine residues of nonhistone proteins. These findings, coupled with high-resolution mass spectrometry studies that revealed the presence of acyl-group PTMs on lysine residues of nonhistone proteins, brought forth the possibility of HDACs acting as removers of both acyl- and acetyl-based PTMs. We posited that HDACs fulfill this dual role and sought to investigate their specificity. Utilizing a fluorescence-based assay and biologically relevant acyl-substrates, the selectivities of zinc-dependent HDACs toward these acyl-based PTMs were identified. These findings were further validated using cellular models and molecular biology techniques. As a proof of principal, an HDAC3 selective inhibitor was designed using HDAC3's substrate preference. This resulting inhibitor demonstrates nanomolar activity and >30 fold selectivity toward HDAC3 compared to the other class I HDACs. This inhibitor is capable of increasing p65 acetylation, attenuating NF-κB activation, and thereby preventing downstream nitric oxide signaling. Additionally, this selective HDAC3 inhibition allows for control of HMGB-1 secretion from activated macrophages without altering the acetylation status of histones or tubulin.
[Mh] Termos MeSH primário: Inibidores de Histona Desacetilases/farmacologia
Processamento de Proteína Pós-Traducional
Zinco/química
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Esterases/antagonistas & inibidores
Proteína HMGB1/secreção
Histona Desacetilases/metabolismo
Seres Humanos
Lisina/metabolismo
Macrófagos/metabolismo
NF-kappa B/metabolismo
Transdução de Sinais
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (HMGB1 Protein); 0 (Histone Deacetylase Inhibitors); 0 (NF-kappa B); EC 3.1.- (Esterases); EC 3.5.1.98 (Histone Deacetylases); EC 3.5.1.98 (histone deacetylase 3); J41CSQ7QDS (Zinc); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00321


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[PMID]:29235319
[Au] Autor:Toptikov VA; Totsky VN; Alieksieieva TG; Kovtun OA
[Ti] Título:Hydrolytic enzymes expressivity in different parts of the Rapana digestive system.
[So] Source:Ukr Biochem J;88(3):5-17, 2016 May-Jun.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The relevance of comprehensive studies of the Rapana vital functions is determined by its considerab­le negative impact on the ecosystem of the Black Sea. The aim of the work was to find out the polymorphism and activity of the main hydrolases in the different parts of the digestive system of Rapana. Hydrolases (proteases, amylases, esterases, lipases and phosphatases) in glandular structures of the Rapana digestive system were studied by electrophoresis. It was found that different sets of hydrolytic enzymes are functioning in certain parts of the Rapana digestive tract. The gland of Leiblein and hepatopancreas played the most important role in the digestion of food components. The salivary glands had the significant influence on proteolysis.
[Mh] Termos MeSH primário: Mucosa Gástrica/enzimologia
Gastrópodes/enzimologia
Expressão Gênica
Hepatopâncreas/enzimologia
Espécies Introduzidas
Glândulas Salivares/enzimologia
[Mh] Termos MeSH secundário: Amilases/classificação
Amilases/genética
Amilases/metabolismo
Animais
Mar Negro
Ensaios Enzimáticos
Esterases/classificação
Esterases/genética
Esterases/metabolismo
Gastrópodes/genética
Lipase/classificação
Lipase/genética
Lipase/metabolismo
Peptídeo Hidrolases/classificação
Peptídeo Hidrolases/genética
Peptídeo Hidrolases/metabolismo
Monoéster Fosfórico Hidrolases/classificação
Monoéster Fosfórico Hidrolases/genética
Monoéster Fosfórico Hidrolases/metabolismo
Comportamento Predatório/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.- (Esterases); EC 3.1.1.3 (Lipase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.2.1.- (Amylases); EC 3.4.- (Peptide Hydrolases)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.03.005


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[PMID]:27778282
[Au] Autor:Ravindran MS; Wenk MR
[Ad] Endereço:NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore (NUS), Singapore, 117456, Singapore.
[Ti] Título:Activity-Based Lipid Esterase Profiling of M. bovis BCG at Different Metabolic States Using Tetrahydrolipstatin (THL) as Bait.
[So] Source:Methods Mol Biol;1491:75-85, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This chapter provides a step-by-step protocol using activity-based protein profiling (ABPP) as a chemical-proteomic tool to survey the antibiotic properties of a small molecule. Here, we investigate the molecular mechanism behind the bactericidal activity of tetrahydrolipstatin (THL). ABPP relies on small molecule probes that target the active site of specific enzymes in complex proteomes. These probes in turn are equipped with a reporter tag that allows capturing, visualization, enrichment, identification, and quantification of its targets either in vitro or in situ. THL possesses bactericidal activities, but its precise spectrum of molecular targets is poorly characterized. Here, we used THL analogs functionalized to enable Huisgen-base cycloaddition, commonly known as "click chemistry," to identify target proteins after enrichment from mycobacterial cell lysates obtained from different physiological conditions.
[Mh] Termos MeSH primário: Esterases/metabolismo
Lactonas/farmacologia
Metabolismo dos Lipídeos
Mycobacterium bovis/enzimologia
Proteômica
[Mh] Termos MeSH secundário: Antibacterianos/farmacologia
Química Click
Reação de Cicloadição
Inibidores Enzimáticos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Enzyme Inhibitors); 0 (Lactones); 95M8R751W8 (orlistat); EC 3.1.- (Esterases)
[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:161026
[St] Status:MEDLINE


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[PMID]:28464816
[Au] Autor:Shahinyan G; Margaryan A; Panosyan H; Trchounian A
[Ad] Endereço:Research Institute of Biology, Yerevan State University, 0025, Yerevan, Armenia.
[Ti] Título:Identification and sequence analyses of novel lipase encoding novel thermophillic bacilli isolated from Armenian geothermal springs.
[So] Source:BMC Microbiol;17(1):103, 2017 05 02.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Among the huge diversity of thermophilic bacteria mainly bacilli have been reported as active thermostable lipase producers. Geothermal springs serve as the main source for isolation of thermostable lipase producing bacilli. Thermostable lipolytic enzymes, functioning in the harsh conditions, have promising applications in processing of organic chemicals, detergent formulation, synthesis of biosurfactants, pharmaceutical processing etc. RESULTS: In order to study the distribution of lipase-producing thermophilic bacilli and their specific lipase protein primary structures, three lipase producers from different genera were isolated from mesothermal (27.5-70 °C) springs distributed on the territory of Armenia and Nagorno Karabakh. Based on phenotypic characteristics and 16S rRNA gene sequencing the isolates were identified as Geobacillus sp., Bacillus licheniformis and Anoxibacillus flavithermus strains. The lipase genes of isolates were sequenced by using initially designed primer sets. Multiple alignments generated from primary structures of the lipase proteins and annotated lipase protein sequences, conserved regions analysis and amino acid composition have illustrated the similarity (98-99%) of the lipases with true lipases (family I) and GDSL esterase family (family II). A conserved sequence block that determines the thermostability has been identified in the multiple alignments of the lipase proteins. CONCLUSIONS: The results are spreading light on the lipase producing bacilli distribution in geothermal springs in Armenia and Nagorno Karabakh. Newly isolated bacilli strains could be prospective source for thermostable lipases and their genes.
[Mh] Termos MeSH primário: Bacillus/enzimologia
Bacillus/isolamento & purificação
Proteínas de Bactérias/química
Proteínas de Bactérias/isolamento & purificação
Fontes Termais/microbiologia
Lipase/química
Lipase/isolamento & purificação
Análise de Sequência
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Armênia
Bacillus/genética
Proteínas de Bactérias/classificação
Proteínas de Bactérias/genética
Estabilidade Enzimática
Esterases
Temperatura Alta
Concentração de Íons de Hidrogênio
Lipase/classificação
Lipase/genética
Fenótipo
Filogenia
RNA Ribossômico 16S/genética
Alinhamento de Sequência
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (RNA, Ribosomal, 16S); EC 3.1.- (Esterases); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (thermostable lipase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1186/s12866-017-1016-4


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[PMID]:29061820
[Au] Autor:Opydo-Chanek M; Sladowska K; Blicharski K; Mikes J; Fedorocko P; Niemeyer U; Mazur L
[Ad] Endereço:Department of Experimental Hematology, Jagiellonian University in Krakow, Krakow, Poland.
[Ti] Título:Comparison of Antileukemic Activity of 4-Hydroperoxyifosfamide and 4-Hydroperoxycyclophosphamide.
[So] Source:Anticancer Res;37(11):6355-6361, 2017 11.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The oxazaphosphorines, ifosfamide and cyclophosphamide, represent a class of alkylating agents. The aim of the present in vitro study was to compare antileukemic activity of 4-hydroperoxyifosfamide (4-OOH-IF) and 4-hydroperoxycyclophosphamide (4-OOH-CP). MATERIALS AND METHODS: The experiments were performed on MOLT-4 and ML-1 cells. The research was conducted using flow cytometry fluorescein diacetate/propidium iodide (PI), fluorescein-conjugated annexin V/PI, CaspGLOW Red Active Caspase-8 and -9, CellEvent™ Caspase-3/7 Green assays, and tetramethylrhodamine ethyl ester test. RESULTS: 4-OOH-IF and 4-OOH-CP distinctly reduced cell viability and triggered apoptosis and necrosis, causing changes in intracellular esterase activity, plasma membrane structure and integrity, caspase activation, and mitochondrial membrane potential. The oxazaphosphorines were responsible for the different antileukemic activities. 4-Hydroperoxyifosfamide appeared to be less cytotoxic against the leukemia cells than 4-hydroperoxycyclophosphamide. MOLT-4 cells were more sensitive to the action of the oxazaphosphorines than ML-1 cells. CONCLUSION: The findings provide a new insight on the mechanisms of cytotoxic action of 4-OOH-IF and 4-OOH-CP on the human acute lymphoblastic and myeloblastic leukemia cells.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Ciclofosfamida/análogos & derivados
Ifosfamida/análogos & derivados
Leucemia/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Caspases/metabolismo
Linhagem Celular Tumoral
Membrana Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Ciclofosfamida/farmacologia
Esterases/metabolismo
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Ifosfamida/farmacologia
Leucemia/tratamento farmacológico
Potencial da Membrana Mitocondrial/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 39800-28-7 (hydroperoxyisophosphamide); 8N3DW7272P (Cyclophosphamide); EC 3.1.- (Esterases); EC 3.4.22.- (Caspases); U880A4FUDA (perfosfamide); UM20QQM95Y (Ifosfamide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE


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[PMID]:28843845
[Au] Autor:Singh R; Kumar V; Bharate SS; Vishwakarma RA
[Ad] Endereço:Preformulation Laboratory, PK-PD, Toxicology and Formulation Division, CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu 180001, India; Academy of Scientific and Innovative Research (AcSIR), CSIR-Indian Institute of Integrative Medicine, Canal Road, Jammu 180001, India.
[Ti] Título:Synthesis, pH dependent, plasma and enzymatic stability of bergenin prodrugs for potential use against rheumatoid arthritis.
[So] Source:Bioorg Med Chem;25(20):5513-5521, 2017 Oct 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bergenin is a unique C-glycoside natural product possessing anti-inflammatory and anti-arthritic activity. It is hydrophilic molecule and stable under acidic conditions however is unstable at neutral-basic pH conditions. The rate of degradation is directly proportional to the increase in pH which might be one of the reasons for its low oral bioavailability. Thus, herein our objective was to improve its stability using prodrug strategy. Various ester and ether prodrugs were synthesized and studied for lipophilicity, chemical stability and enzymatic hydrolysis in plasma/esterase. The stability of synthesized prodrugs was evaluated in buffers at different pH, in biorelevant media such as SGF, SIF, rat plasma and in esterase enzyme. All prodrugs displayed significantly improved lipophilicity compared with bergenin, which was in accordance with the criteria of drug-like compounds. Acetyl ester 4a appeared to be the most promising prodrug as it remained stable at gastric/intestinal pH and was completely transformed to the parent compound bergenin in plasma as desired for an ideal prodrug. The data presented herein, will help in designing stable prodrugs of unstable molecules with desired physicochemical properties in structurally similar chemotypes.
[Mh] Termos MeSH primário: Artrite Reumatoide/tratamento farmacológico
Benzopiranos/farmacologia
Esterases/metabolismo
Pró-Fármacos/farmacologia
Saxifragaceae/química
[Mh] Termos MeSH secundário: Animais
Benzopiranos/síntese química
Benzopiranos/metabolismo
Concentração de Íons de Hidrogênio
Fígado/enzimologia
Conformação Molecular
Pró-Fármacos/síntese química
Pró-Fármacos/metabolismo
Ratos
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzopyrans); 0 (Prodrugs); EC 3.1.- (Esterases); L84RBE4IDC (bergenin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170828
[St] Status:MEDLINE


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[PMID]:28721843
[Au] Autor:Staton GJ; Newbrook K; Clegg SR; Birtles RJ; Evans NJ; Carter SD
[Ad] Endereço:1​Department of Infection Biology, Institute of Infection and Global Health, University of Liverpool, iC2 Building, Liverpool Science Park, Brownlow Hill, Liverpool, L3 5RF, UK.
[Ti] Título:Treponema rectale sp. nov., a spirochete isolated from the bovine rectum.
[So] Source:Int J Syst Evol Microbiol;67(7):2470-2475, 2017 Jul.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A Gram-stain-negative, obligatory anaerobic spirochete, CHPAT, was isolated from the rectal tissue of a Holstein-Friesian cow. On the basis of 16S rRNA gene comparisons, CHPAT was most closely related to the human oral spirochete, Treponema parvum, with 88.8 % sequence identity. Further characterisation on the basis of recA gene sequence analysis, cell morphology, pattern of growth and physiological profiling identified marked differences with respect to other recognised species of the genus Treponema. Microscopically, the helical cells measured approximately 1-5 µm long and 0.15-0.25 µm wide, with two to five irregular spirals. Transmission electron microscopy identified four periplasmic flagella in a 2 : 4 : 2 arrangement. CHPAT grew independently of serum, demonstrated no evidence of haemolytic activity and possessed an in vitro enzyme activity profile that is unique amongst validly named species of the genus Treponema, exhibiting C4 esterase, α-galactosidase and ß-galactosidase activity. Taken together, these data indicate that CHPAT represents a novel species of the genus Treponema, for which the name Treponema rectale is proposed. The type strain of Treponema rectale is CHPAT (=DSM 103679T=NCTC 13848T).
[Mh] Termos MeSH primário: Bovinos/microbiologia
Filogenia
Reto/microbiologia
Treponema/classificação
[Mh] Termos MeSH secundário: Animais
Técnicas de Tipagem Bacteriana
DNA Bacteriano/genética
Esterases/genética
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Treponema/genética
Treponema/isolamento & purificação
Reino Unido
alfa-Galactosidase/genética
beta-Galactosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (RNA, Ribosomal, 16S); EC 3.1.- (Esterases); EC 3.2.1.22 (alpha-Galactosidase); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002051


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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]:28703362
[Au] Autor:Dube S; Dube H; Green NB; Larsen EM; White A; Johnson RJ; Kowalski JR
[Ad] Endereço:Department of Biological Sciences, Butler University, 4600 Sunset Avenue, Indianapolis, IN, 46208, USA.
[Ti] Título:In Vivo Delivery and Activation of Masked Fluorogenic Hydrolase Substrates by Endogenous Hydrolases in C. elegans.
[So] Source:Chembiochem;18(18):1807-1813, 2017 Sep 19.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Protein expression and localization are often studied in vivo by tagging molecules with green fluorescent protein (GFP), yet subtle changes in protein levels are not easily detected. To develop a sensitive in vivo method to amplify fluorescence signals and allow cell-specific quantification of protein abundance changes, we sought to apply an enzyme-activated cellular fluorescence system in vivo by delivering ester-masked fluorophores to Caenorhabditis elegans neurons expressing porcine liver esterase (PLE). To aid uptake into sensory neuron membranes, we synthesized two novel fluorogenic hydrolase substrates with long hydrocarbon tails. Recombinant PLE activated these fluorophores in vitro. In vivo activation occurred in sensory neurons, along with potent activation in intestinal lysosomes quantifiable by imaging and microplate and partially attributable to gut esterase 1 (GES-1) activity. These data demonstrate the promise of biorthogonal hydrolases and their fluorogenic substrates as in vivo neuronal imaging tools and for characterizing endogenous C. elegans hydrolase substrate specificities.
[Mh] Termos MeSH primário: Caenorhabditis elegans/metabolismo
Esterases/metabolismo
Corantes Fluorescentes/metabolismo
[Mh] Termos MeSH secundário: Animais
Meios de Contraste/química
Meios de Contraste/metabolismo
Esterases/genética
Corantes Fluorescentes/química
Microscopia de Fluorescência
Neurônios/metabolismo
RNA Mensageiro/metabolismo
Especificidade por Substrato
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contrast Media); 0 (Fluorescent Dyes); 0 (RNA, Messenger); EC 3.1.- (Esterases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700278



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