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1.
Ciênc. Saúde Colet. (Impr.) ; 20(2): 449-460, fev. 2015. tab
Article in Portuguese | LILACS | ID: lil-742218

ABSTRACT

O objetivo deste trabalho foi analisar os motivos das faltas às consultas odontológicas em Unidades de Saúde da Família (USF) e implementar estratégias para sua redução por meio da pesquisa-ação. O estudo foi realizado em 12 USF de Piracicaba/SP, de 01 de janeiro a 31 de dezembro de 2010. A amostra se consistiu de 385 usuários, entrevistados por telefone, sobre os motivos das faltas, além de 12 cirurgiões-dentistas e 12 enfermeiras. Realizaram-se duas oficinas com os profissionais: uma para problematização dos dados coletados nas entrevistas e elaboração de estratégias; e outra após 4 meses, para avaliação. O maior motivo de faltas foi a coincidência do horário de funcionamento das unidades com o de trabalho dos usuários. Dentre as estratégias ressaltou-se a realização de palestras sobre saúde bucal, educação permanente nas reuniões de equipe, capacitação dos Agentes Comunitários de Saúde, participação em grupos terapêuticos e parcerias entre Equipe de Saúde Bucal e equipamentos sociais da comunidade. A adoção de prontuário único foi a estratégia desafiadora encontrada pelos profissionais. Concluiu-se que as estratégias implementadas levaram à diminuição das faltas em 66,6% e o caráter motivador das oficinas possibilitou a reflexão crítica para o redirecionamento da prática em saúde.


The aim of this study was to analyze the reasons for missed appointments in dental Family Health Units (FHU) and implement strategies to reduce same through action research. This is a study conducted in 12 FHUs in Piracicaba in the State of São Paulo from January, 1 to December, 31 2010. The sample was composed of 385 users of these health units who were interviewed over the phone and asked about the reasons for missing dental appointments, as well as 12 dentists and 12 nurses. Two workshops were staged with professionals: the first to assess the data collected in interviews and develop strategy, and the second for evaluation after 4 months. The primary cause for missed appointments was the opening hours of the units coinciding with the work schedule of the users. Among the strategies suggested were lectures on oral health, ongoing education in team meetings, training of Community Health Agents, participation in therapeutic groups and partnerships between Oral Health Teams and the social infrastructure of the community. The adoption of the single medical record was the strategy proposed by professionals. The strategies implemented led to a 66.6% reduction in missed appointments by the units and the motivating nature of the workshops elicited critical reflection to redirect health practices.


Subject(s)
Cysteine Endopeptidases/metabolism , Enzyme Precursors/metabolism , Plant Proteins/metabolism , Amino Acid Sequence , Biocatalysis , Computer Simulation , Cysteine Endopeptidases/chemistry , Cysteine Endopeptidases/genetics , Cysteine Proteinase Inhibitors/chemistry , Cysteine Proteinase Inhibitors/metabolism , Cysteine Proteinase Inhibitors/pharmacology , Enzyme Activation , Enzyme Precursors/antagonists & inhibitors , Enzyme Precursors/chemistry , Enzyme Precursors/genetics , Hot Temperature , Hydrogen-Ion Concentration , Hydrolysis , Isoenzymes/antagonists & inhibitors , Isoenzymes/chemistry , Isoenzymes/genetics , Isoenzymes/metabolism , Kinetics , Leucine/analogs & derivatives , Leucine/chemistry , Leucine/metabolism , Leucine/pharmacology , Models, Molecular , Molecular Sequence Data , Plant Proteins/antagonists & inhibitors , Plant Proteins/chemistry , Plant Proteins/genetics , Protein Conformation , Protein Folding , Protein Stability , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism
2.
Article in English | IMSEAR | ID: sea-163225

ABSTRACT

Aims: To highlight whether metabolites of Alcaligenes faecalis BW1 extract can be administered orally for their possible antimycobacterial effects. Study Design: Study of the influence of certain parameters on the extract of Alcaligenes faecalis by using either discs or well diffusion methods against M. smegmatis. Place and duration of study: Laboratory of Microbial Biotechnology, Department of Biology, Faculty of Sciences and Technical, University Sidi Mohamed Ben Abdellah, BP 2202, Road of Immouzer, Fez, Morocco. From April to August, 2012. Methodology: The impact of acidic pH of gastric juice, bile, hydrogen peroxide, pancreatic enzymes and lysozyme on the antimycobacterial activity of Alcaligenes faecalis BW1 extract was evaluated by agar diffusion method. Detection whether or not antibacterial metabolites having a synergistic effect with rifampicin against M. smegmatis was also explored. Results: Antibacterial metabolites of Alcaligenes faecalis BW1 extract resist to the action of gastric pH, gallbladder bile and hydrogen peroxide. In addition, they are not affected by pancreatic enzymes and lysozyme. Moreover, they have a synergistic effect with rifampicin against M. smegmatis. Conclusion: Anti-mycobacterial metabolites of Alcaligenes faecalis BW1 extract are compatible with rifampicin and could be administered orally as antitubercular agents after their purification, identification in further work.


Subject(s)
Alcaligenes faecalis/physiology , Anti-Infective Agents/physiology , Anti-Infective Agents/pharmacokinetics , Bacteria/physiology , Bacteria/pharmacokinetics , Bile/chemistry , Cell Extracts/isolation & purification , Gastric Juice/chemistry , Isoenzymes/chemistry , Pancreas/chemistry , Pancreas/enzymology , Sensitivity and Specificity
3.
Indian J Biochem Biophys ; 2007 Oct; 44(5): 379-85
Article in English | IMSEAR | ID: sea-26744

ABSTRACT

Filariasis is a major health problem, affecting millions of people in tropical and sub-tropical regions of the world. The isolation and characterization of parasite-specific enzyme targets is essential for developing effective control measures against filariasis. Acetylcholinesterase (AchE, E.C. 3.1.1.7), an important enzyme of neuromuscular transmission is found in a number of helminths including filarial parasites and may be playing a role in host-parasite interactions. Earlier, we demonstrated the presence of two isozymes of AchE, different from the host enzyme in the human (Brugia malayi) and bovine (Setaria cervi) filarial parasites. In the present study, two isozymes of AchE (pAchE1 and pAchE2) were isolated from S. cervi adults and characterized biochemically and immunochemically. The AchE was partially purified on Con-A Sepharose column and then subjected to preparative polyacrylamide gel electrophoresis (PAGE) for separation of the isozymes. The AchE activity was localized by the staining of gel and the isozymes were isolated from the PAGE strips by electroelution. Both isozymes preferentially utilized acetylcholine iodide as substrate and were strongly inhibited by the true AchE inhibitor (BW284c51), suggesting that they were true AchE. The polyclonal antibodies produced against the isozymes showed significant cross-reactivity with B. malayi AchE, but not against the host enzyme. These findings suggested that both the isozymes were biochemically (in terms of their substrate specificity and inhibitor sensitivity) and immunochemically similar, but different from the host enzyme.


Subject(s)
Acetylcholinesterase/chemistry , Animals , Buffaloes/parasitology , Enzyme Activation , Enzyme Stability , Female , Host-Parasite Interactions/immunology , Isoenzymes/chemistry , Male , Setaria Nematode/enzymology , Substrate Specificity
4.
Braz. j. med. biol. res ; 38(8): 1203-1208, Aug. 2005. ilus
Article in English | LILACS | ID: lil-405521

ABSTRACT

Many cellular proteins are bound to the surfaces of membranes and participate in various cell signaling responses. Interactions between this group of proteins are in part controlled by the membrane surface to which the proteins are bound. This review focuses on the effects of pressure on membrane-associated proteins. Initially, the effect of pressure on membrane surfaces and how pressure may perturb the membrane binding of proteins is discussed. Next, the effect of pressure on the activity and lateral association of proteins is considered. We then discuss how pressure can be used to gain insight into these types of proteins.


Subject(s)
Humans , Hydrostatic Pressure , Membrane Proteins/metabolism , Isoenzymes/chemistry , Isoenzymes/metabolism , Lipid Bilayers/chemistry , Lipid Bilayers/metabolism , Membrane Proteins/chemistry , Phospholipase C delta , Protein Binding , Static Electricity , Type C Phospholipases/chemistry , Type C Phospholipases/metabolism
5.
Indian J Biochem Biophys ; 2001 Feb-Apr; 38(1-2): 56-63
Article in English | IMSEAR | ID: sea-28849

ABSTRACT

The energetics and models of COX-2 complexed with nonsteroidal anti-inflammatory drugs (NSAIDs) having different degrees of selectivity for two isoforms of COX (COX-2 and COX-1) have been studied using computer modelling approach. The models are obtained for complexes of NS398 (NS), a selective COX-2 inhibitor; indoprofen (Ind), a non-selective inhibitor; di-tert-butylbenzofurans (DHDMBFs) with substituents at the 5th position: CONH(CH2)2OMe (BF1), CONH-c-Pr (BF2), 3-methylene-gamma-butyrolactonyl (BF3) and oxicams namely, meloxicam (Mel), piroxicam (Pir) and tenoxicam (Ten). These were optimized using molecular mechanics (MM) and molecular dynamics (MD) techniques. The binding energies and structures were compared with pharmacological parameters and available results with COX-1. In case of NS a larger difference in the binding energies between COX-2 and COX-1 was noticed as compared to that of Ind. It also had stronger interaction with His90 and Tyr355 which is considered important for COX-2 selectivity. There was a difference in the compactness at the channel entrance between COX-2 selective and non-selective ligands. Models with DHDMBFs and oxicams showed a similar correlation. The results were used to design a peptide inhibitor, Tyr-Arg-Cys-Ala-delta Phe-Cys (Pept) which could fit better in the COX-2 cavity. As per our MD simulation results this peptide inhibitor showed both higher activity and COX-2 selectivity.


Subject(s)
Anti-Inflammatory Agents, Non-Steroidal/pharmacology , Binding Sites , Cyclooxygenase 1 , Cyclooxygenase 2 , Inhibitory Concentration 50 , Isoenzymes/chemistry , Kinetics , Ligands , Models, Chemical , Models, Molecular , Monte Carlo Method , Prostaglandin-Endoperoxide Synthases/chemistry , Protein Binding , Protein Conformation , Software , Thermodynamics , X-Ray Diffraction
6.
Experimental & Molecular Medicine ; : 76-82, 2001.
Article in English | WPRIM | ID: wpr-42078

ABSTRACT

5'-upstream region of the phospholipase C-beta2 gene, 810 bp, was cloned and characterized. S1 nuclease mapping and primer extension analyses revealed that a single transcriptional start site locates at 284 nucleotides upstream from the beginning of translation. The 5-upstream region lacks both TATA motif and typical initiator sequence, but retains GC-rich segment. Two putative regulatory regions, a negative region (-636/-588) and a positive region (-98/ -13) were identified in the upstream region of PLC-beta2 gene. We suggest that the transcription of PLC-beta2 may be regulated by binding of regulatory proteins to the negative and/or positive regulatory regions located in the upstream of the gene.


Subject(s)
Single-Strand Specific DNA and RNA Endonucleases/metabolism , Base Sequence , Cells, Cultured , Chloramphenicol O-Acetyltransferase/metabolism , Cloning, Molecular , Conserved Sequence , Gene Deletion , Isoenzymes/chemistry , Molecular Sequence Data , Mutagenesis, Site-Directed , Type C Phospholipases/chemistry , Promoter Regions, Genetic , Protein Binding , Transcription, Genetic , Transfection
7.
Braz. j. med. biol. res ; 33(7): 725-9, July 2000. graf
Article in English | LILACS | ID: lil-262672

ABSTRACT

Potato apyrase, a soluble ATP-diphosphohydrolase, was purified to homogeneity from several clonal varieties of Solanum tuberosum. Depending on the source of the enzyme, differences in kinetic and physicochemical properties have been described, which cannot be explained by the amino acid residues present in the active site. In order to understand the different kinetic behavior of the Pimpernel (ATPase/ADPase = 10) and Desirée (ATPase/ADPase = 1) isoenzymes, the nucleotide-binding site of these apyrases was explored using the intrinsic fluorescence of tryptophan. The intrinsic fluorescence of the two apyrases was slightly different. The maximum emission wavelengths of the Desirée and Pimpernel enzymes were 336 and 340 nm, respectively, suggesting small differences in the microenvironment of Trp residues. The Pimpernel enzyme emitted more fluorescence than the Desirée apyrase at the same concentration although both enzymes have the same number of Trp residues. The binding of the nonhydrolyzable substrate analogs decreased the fluorescence emission of both apyrases, indicating the presence of conformational changes in the neighborhood of Trp residues. Experiments with quenchers of different polarities, such as acrylamide, Cs+ and I- indicated the existence of differences in the nucleotide-binding site, as further shown by quenching experiments in the presence of nonhydrolyzable substrate analogs. Differences in the nucleotide-binding site may explain, at least in part, the kinetic differences of the Pimpernel and Desirée isoapyrases.


Subject(s)
Adenosine Diphosphate/metabolism , Apyrase/metabolism , Nucleotides/metabolism , Solanum tuberosum/enzymology , Apyrase/chemistry , Apyrase/isolation & purification , Cesium/chemistry , Cesium/metabolism , Iodine/chemistry , Iodine/metabolism , Isoenzymes/chemistry , Solanum tuberosum/chemistry , Spectrometry, Fluorescence
8.
Indian J Biochem Biophys ; 2000 Apr; 37(2): 86-96
Article in English | IMSEAR | ID: sea-26580

ABSTRACT

We have studied the conformational flexibility of three 5-keto-substituted 7-tert-butyl-2,3-dihydro-3,3-dimethylbenzofurans (DHDMBFs) which show dual cyclooxygenase (COX) and 5-lipoxygenase (LOX) inhibition and are potential candidates as antiinflammatory agents and analgesics. The conformations were studied by systematic search, molecular mechanics (MM) and simulated annealing molecular dynamics (SAMD) techniques. We also studied several structure based parameters and distribution of molecular electrostatic potential (MEP) around these molecules. All the three compounds were docked in the active cavity of cyclooxygenase-2 (COX-2) using graphical and energy grid search techniques. The complex geometries were optimized by MM. The results on conformational flexibility, inter-atomic distances and angles, MEP distribution and points of contacts with peptide side chains in active cavity have been used to understand the mechanistic cause of differential action of these molecules.


Subject(s)
Arachidonate 5-Lipoxygenase/antagonists & inhibitors , Benzofurans/chemistry , Catalytic Domain , Cyclooxygenase 2 , Cyclooxygenase 2 Inhibitors , Cyclooxygenase Inhibitors/chemistry , Isoenzymes/chemistry , Lipoxygenase Inhibitors/chemistry , Models, Molecular , Molecular Conformation , Prostaglandin-Endoperoxide Synthases/chemistry
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