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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.
Salud pública Méx ; 56(6): 654-659, nov.-dic. 2014. tab
Article in Spanish | LILACS | ID: lil-733345

ABSTRACT

La listeriosis es una enfermedad transmitida por alimentos (ETA) y ocasionada por Listeria monocytogenes. La importancia de ésta se debe a su impacto clínico, la alta tasa de mortalidad y el efecto económico derivado de los brotes asociados con el consumo de alimentos. En México, las fallas en los sistemas de vigilancia epidemiológicos son causa de información imprecisa sobre la incidencia de la listeriosis y sobre su caracterización como ETA. En este trabajo se presentan datos referentes a la presencia de la bacteria en alimentos, reportes de casos de la enfermedad y patologías relacionadas con infección por L. monocytogenes. La falta de datos exactos sobre la importancia de esta bacteria plantea la necesidad de concientizar a las instancias correspondientes para definir estrategias de búsqueda intencionada de L. monocytogenes en alimentos y de la recopilación de información clínica precisa que permita conocer la importancia clínica y epidemiológica de la listeriosis en México.


Listeriosis is caused by Listeria monocytogenes, an important food-borne disease due to its clinical forms, high mortality rate, and the economic impact in both clinical and food production industries. In Mexico, the lack of epidemiological surveillance systems leads to the need of accurate data on the incidence of listeriosis and its association with food-borne disease. In this paper, we present data about the presence of this bacterium in food, reports related to clinical cases of listeriosis, and information of diseases in which L. monocytogenes may be involved. However, in most of these cases the etiology was not established. Given this, there's a need to inform and warn the appropriate entities, to define strategies for the mandatory search of L. monocytogenes through the whole food production chain and clinical suspects, for the epidemiological importance and control of listeriosis in Mexico.


Subject(s)
Animals , Cysteine Endopeptidases/isolation & purification , Egg Proteins/metabolism , Enzyme Precursors/isolation & purification , Antimalarials/pharmacology , Chromatography, Gel , Cysteine Endopeptidases/metabolism , Cysteine Proteinase Inhibitors/pharmacology , Egg Yolk/chemistry , Electrophoresis, Polyacrylamide Gel , Enzyme Activation , Enzyme Precursors/metabolism , Hydrogen-Ion Concentration , Leucine/analogs & derivatives , Leucine/metabolism , Molecular Weight , Orthoptera
3.
Indian J Biochem Biophys ; 2012 Dec; 49(6): 421-427
Article in English | IMSEAR | ID: sea-144082

ABSTRACT

Proenzymes with various lengths of propeptides have been observed in GluV8 from Staphylococcus aureus and GluSE from S. epidermidis. However, the production mechanism of these proenzymes and roles of truncated propeptides have yet to be elucidated. Here we demonstrate that shortening of propeptide commonly occurs in an auto-catalytic manner in GluV8-family members, including those from coagulase negative Staphylococci and Enterococcus faecalis. Accompanied with propeptide shortening, the pro-mature junction (Asn/Ser-1-Val1) becomes more susceptible towards the hetero-catalytic maturation enzymes. The auto-catalytic propeptide truncation is not observed in Ser169Ala inert molecules of GluV8-family members. A faint proteolytic activity of proenzymes from Staphylococcus caprae and E. faecalis is detected. In addition, proteolytic activity of proenzyme of GluV8 carrying Arg-3AlaAsn-1 is demonstrated with synthetic peptide substrates LLE/Q-MCA. These results suggest that GluV8-family proenzymes with shortened propeptides intrinsically possess proteolytic activity and are involved in the propeptide shortening that facilitates the final hetero-catalytic maturation.


Subject(s)
Enterococcus faecalis/analysis , Enterococcus faecalis/metabolism , Enzyme Precursors/metabolism , Protein Precursors , Proteolysis , Enzyme Precursors/metabolism , Staphylococcus aureus
4.
Korean Journal of Ophthalmology ; : 288-292, 2005.
Article in English | WPRIM | ID: wpr-146517

ABSTRACT

PURPOSE: To study the effect of systemic administration of phenyl-N-tert-butylnitrone (PBN) on the degeneration of photoreceptor cells in rd mice. METHODS: PBN was injected intraperitoneally into FVB/rd mice on postnatal days (P) 5 to 14 (group A), and P10 to 18 (group B). At days P14, 16, 18, 20 and 27, morphological changes and apoptosis were analyzed by staining with hematoxylin and eosin or DAPI. The effect of PBN on apoptosis was analyzed in retinal pigment epithelial (RPE) cells by the measurement of caspase-3 activity. RESULTS: In control and group B mice, the outer nuclear layer (ONL) of the retina was composed of 8-10 rows at P12, and rapidly decreased to one row at P18. In group A mice, the ONL was preserved with 5-7 rows at P18, and decreased to one row at P22. PBN inhibited caspase-3 activity in cultured RPE cells. CONCLUSIONS: PBN delayed, but did not block, the degeneration of photoreceptor cells in rd mice. PBN may exert its inhibitory effect during the early phase of photoreceptor cell degeneration.


Subject(s)
Mice , Male , Female , Animals , Retinal Degeneration/drug therapy , Pigment Epithelium of Eye/drug effects , Photoreceptor Cells, Vertebrate/drug effects , Nitrogen Oxides/administration & dosage , Neuroprotective Agents/administration & dosage , Injections, Intraperitoneal , Free Radical Scavengers/administration & dosage , Follow-Up Studies , Enzyme Precursors/metabolism , Disease Models, Animal , Cells, Cultured , Caspases/metabolism , Caspase 3 , Apoptosis/drug effects
5.
Biocell ; 28(3): 311-316, dic. 2004. ilus, tab
Article in English | LILACS | ID: lil-405203

ABSTRACT

Acrosin activity is associated with normal fertility in human and bovine spermatozoa. The aim of the study was to determine the variation of the enzyme activity in the proacrosin-acrosin system in capacitated and acrosome recated cryopreserved bovine sperm. Enzyme activity was assessed spectrophotometrically using N-alpha-benzoyl-DL-arginine p-nitroanilide (BAPNA) as specific substrate for acrosin at pH 8. Capacitation with heparin and quercitin failed to induce conversion of proacrosin to acrosin. An increase in acrosin activity produced by the presence of progesterone, in a dose-dependent manner, was related with the induction of true acrosome reaction. The total level of acrosin activity registered showed that 96 per cent of acrosin of capacitated sperm samples and control is present in the zymogen form. Moreover, progesterone is capable of duplicating the level of active enzyme, indicating that enzyme activity changes are related to acrosome reaction, suggesting that only a minor proportion of the total of proacrosin-acrosin system is required in the exocytotic process on cryopreserved bovine sperm.


Subject(s)
Cattle , Animals , Acrosin/metabolism , Sperm Capacitation/physiology , Spermatozoa , Enzyme Precursors/metabolism , Quercetin/analogs & derivatives , Quercetin/pharmacology , Acrosome Reaction/physiology , Semen/cytology , Trypan Blue/chemistry , Cryopreservation , Chlortetracycline/chemistry , Spermatozoa/enzymology , Spermatozoa/physiology , Heparin/pharmacology , Microscopy, Fluorescence , Microscopy, Interference , Progesterone/pharmacology
6.
Biocell ; 27(1): 47-55, Apr. 2003.
Article in English | LILACS | ID: lil-384251

ABSTRACT

This study shows a strong association between cell attachment to substratum and activation of beta 1-integrin-signaling with resistance to the camptothecin derivative topotecan (TPT) in breast cancer cells. We propose a mechanistic-driven approach to sensitize the cells to camptothecins. ZR-75-1 anchorage-dependent breast cancer cell line, its derivative 9D3S suspension cells (9D3S-S), and 9D3S cells attached to fibronectin-coated plates (9D3S-A) were treated with TPT (1 microM) or CPT-11 (40 microM) for 48 h. Programmed cell death (PCD), as shown by poly(ADP-ribose) polymerase (PARP), pro-caspase-3 and pro-caspase-9 cleavage, was observed in 9D3S-S cells but not in ZR-75-1 or 9D3S-A cells. Because p125 focal adhesion kinase (FAK) is a transducer in the beta 1-integrin signaling pathway, it is essential to cell adhesion and it is overexpressed in metastatic breast cancer, we hypothesized that attenuation of FAK might enhance the sensitivity of breast cancer cells to camptothecins. Moreover, inhibition of FAK gene expression by a phosphorothioated antisense oligodeoxynucleotide targeting the portion of the gene encoding amino acids 262-268, increased the sensitivity of ZR-75-1, MDA-MB-231 and MCF7 breast cancer cells to treatment with TPT or CPT-11.


Subject(s)
Humans , Female , Antineoplastic Agents, Phytogenic/therapeutic use , Camptothecin/therapeutic use , Breast Neoplasms/metabolism , Oligonucleotides, Antisense , Protein-Tyrosine Kinases , Cell Adhesion/drug effects , Antibodies, Monoclonal/metabolism , Antineoplastic Agents/therapeutic use , Apoptosis/drug effects , Caspases/metabolism , Enzyme Activation , Fibronectins/metabolism , Gene Expression Regulation, Neoplastic , Breast Neoplasms/pathology , Poly(ADP-ribose) Polymerases/metabolism , Enzyme Precursors/metabolism , Sensitivity and Specificity , Tumor Cells, Cultured , Topotecan/therapeutic use
7.
Biocell ; 20(2): 133-142, Aug. 1996.
Article in English | LILACS | ID: lil-336000

ABSTRACT

The proacrosin/acrosin system has been immunolocalized, by the silver enhanced immunogold technique on the acrosomal region of capacitated and perivitelline rabbit spermatozoa. The purpose of the present work was to investigate the kinetics of the activation of acrosin by determining the proportion of proacrosin and acrosin present in the acrosome of the rabbit spermatozoa during capacitation and the induction of the acrosome reaction by the calcium ionophore A23187. Rabbit spermatozoa selected by the percoll gradient technique were incubated for 0, 0.5 and 6 hours and then the acrosome reaction was induced at 0 and 6 hours with 1.9 microM of the calcium ionophore A23187. It was found that 95 of acrosin activity in rabbit spermatozoa at zero time corresponds to proacrosin and after capacitation and acrosome reaction, a diminution of the activity of proacrosin/acrosin system was found. However, proacrosin represents the large majority of the system activity. Western blot prepared with sperm extract obtained at the start of incubation showed the characteristic doublet band about 53-55 kDa that may correspond to proacrosin and alpha-acrosin. After six hours of incubation and with induction with the calcium ionophore A23187 the same doublet was seen in addition to a third band of 49 kDa that could correspond to a transition form between alpha-acrosin to beta-acrosin. In conclusion, rabbit proacrosin/acrosin system remains in the large proportion as proacrosin during capacitation and acrosome reaction.


Subject(s)
Animals , Male , Rabbits , Acrosin , In Vitro Techniques , Enzyme Precursors/metabolism , Spermatozoa , Acrosome , Sperm Capacitation/physiology , Immunohistochemistry , Kinetics
8.
Biol. Res ; 25(2): 91-3, 1992. ilus
Article in English | LILACS | ID: lil-228638

ABSTRACT

It has been suggested that acrosin may function in penetration of the zona pellucida and of the highly structured extracellular matrix of the perivitelline space. In this study we investigated whether golden hamster perivitelline spermatozoa contain proacrosin/acrosin, as evidenced by the silver enhanced immunogold technique using the monoclonal antibody antiacrosin C2E5. None of the 197 spermatozoa recovered from the perivitelline space showed proacrosin/acrosin associated with the acrosomal region, suggesting that acrosin would not play a role in the penetration of the perivitelline extracellular matrix


Subject(s)
Animals , Female , Cricetinae , Acrosin/metabolism , Enzyme Precursors/metabolism , Intracellular Membranes/metabolism , Spermatozoa/metabolism , Cellular Senescence , Mesocricetus , Oocytes/physiology , Sperm-Ovum Interactions , Vitelline Membrane
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