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1.
J Helminthol ; 91(5): 534-538, 2017 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-27411883

RESUMO

Toxoplasmosis causes complications during pregnancy that have serious effects on fetal development. Thus far, toxocariasis has been reported to spread only via vertical transmission. Nonetheless, the population of pregnant women is also exposed to this infection. Co-infection with both Toxoplasma gondii and Toxocara spp. has been reported in children, but there are no reports of co-infection in the population of pregnant women. The aim of this study was to determine the prevalence of co-infection with T. gondii and Toxocara spp. in pregnant women at a university hospital in southern Brazil, and to identify the risk factors associated with infection by both parasites. Two hundred pregnant women were tested for the presence of anti-T. gondii and anti-Toxocara spp. antibodies and were asked to complete an epidemiological questionnaire. In this study, the co-infection rate observed in the total population of pregnant women was 8%. In addition, women with a positive result for a serology test for Toxocara spp. were at increased risk of infection by T. gondii (P = 0.019). Co-infection with both parasites in pregnant women was associated with low birth weights in neonates. The similar modes of transmission of both parasites could explain the co-infection. Only a few previous studies have investigated this phenomenon. The findings of the present study emphasize the importance of serological diagnosis during prenatal care and further research in this area to identify risk factors associated with this co-infection, and the possible implications of this co-infection during pregnancy and on the health of newborns.


Assuntos
Anticorpos Anti-Helmínticos/sangue , Coinfecção/epidemiologia , Complicações Infecciosas na Gravidez/epidemiologia , Toxocaríase/epidemiologia , Toxoplasmose/epidemiologia , Animais , Brasil/epidemiologia , Coinfecção/parasitologia , Feminino , Hospitais Universitários , Humanos , Recém-Nascido de Baixo Peso , Transmissão Vertical de Doenças Infecciosas , Gravidez , Resultado da Gravidez , Prevalência , Medição de Risco , Inquéritos e Questionários , Toxocara/imunologia , Toxoplasma/imunologia
2.
Chronobiol Int ; 21(6): 871-9, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-15646234

RESUMO

The health issues that attract our attention when analyzing the truck driver population are the high prevalence of sedentary habits, inadequate diet, obesity, and proportion of hypertensive. All these are either considered risk factors for or a consequence of Obstructive Sleep Apnea (OSA). The objective of this study was to investigate the risk for OSA among 10,101 truck drivers and to correlate it with potentially related factors, such as serum glucose and cholesterol levels, smoking habits, alcohol and drug consumption, and self-reported physical activity. The drivers were invited to participate in the campaign "Saúde na Boléia" (Health Behind the Wheel) promoted by a Brazilian company responsible for the maintenance of approximately 360km of roads in the country. Drivers who spontaneously stopped at the campaign booths placed along the roads were invited to answer a questionnaire covering sociodemographic data such as age, alcohol, and drug consumption. All participants completed a Berlin Questionnaire and were classified as low- or high-risk subjects for OSA based on questions about snoring, tiredness during the day, and the presence of hypertension or obesity. Blood collection was accomplished at the same site by nurses and/or nursing students collaborating with the campaign for subsequent laboratory studies. Approximately 26% of the truck drivers were found to be at high-risk group for OSA. An adjusted multiple logistic model found the independent risk factors of smoking (OR=1.16; p=0.014) and drug use (OR= 1.32; p < 0.0001) were associated with high risk for OSA. The presence of self-reported occasional (OR=0.62; p<0.0001) and regular (OR=0.53; p < 0.0001) physical activity was found to be an independent factor protective of OSA. Educational programs, including ones aimed at improving one's health habits, such as engagement in physical exercise, should be considered in the development of initiatives to reduce the risk for OSA among the truck driver population.


Assuntos
Condução de Veículo , Ocupações , Apneia Obstrutiva do Sono/epidemiologia , Apneia Obstrutiva do Sono/etiologia , Inquéritos e Questionários , Adulto , Glicemia/metabolismo , Índice de Massa Corporal , Brasil/epidemiologia , Colesterol/sangue , Humanos , Pessoa de Meia-Idade , Fatores de Risco , Sono , Apneia Obstrutiva do Sono/sangue , Estatística como Assunto
3.
Biochim Biophys Acta ; 1550(1): 70-80, 2001 Nov 26.
Artigo em Inglês | MEDLINE | ID: mdl-11738089

RESUMO

A novel antimicrobial peptide, anoplin, was purified from the venom of the solitary wasp Anoplius samariensis. The sequence was mostly analyzed by mass spectrometry, which was corroborated by solid-phase synthesis. Anoplin, composed of 10 amino acid residues, Gly-Leu-Leu-Lys-Arg-Ile-Lys-Thr-Leu-Leu-NH2, has a high homology to crabrolin and mastoparan-X, the mast cell degranulating peptides from social wasp venoms, and, therefore, can be predicted to adopt an amphipathic alpha-helix secondary structure. In fact, the circular dichroism (CD) spectra of anoplin in the presence of trifluoroethanol or sodium dodecyl sulfate showed a high content, up to 55%, of the alpha-helical conformation. A modeling study of anoplin based on its homology to mastoparan-X supported the CD results. Biological evaluation using the synthetic peptide revealed that this peptide exhibited potent activity in stimulating degranulation from rat peritoneal mast cells and broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria. Therefore, this is the first antimicrobial component to be found in the solitary wasp venom and it may play a key role in preventing potential infection by microorganisms during prey consumption by their larvae. Moreover, this peptide is the smallest among the linear alpha-helical antimicrobial peptides hitherto found in nature, which is advantageous for chemical manipulation and medical application.


Assuntos
Antibacterianos/isolamento & purificação , Oligopeptídeos/química , Oligopeptídeos/isolamento & purificação , Venenos de Vespas/química , Venenos de Vespas/isolamento & purificação , Sequência de Aminoácidos , Animais , Antibacterianos/química , Antibacterianos/farmacologia , Peptídeos Catiônicos Antimicrobianos , Degranulação Celular , Cromatografia Líquida de Alta Pressão , Dicroísmo Circular , Feminino , Mastócitos/efeitos dos fármacos , Mastócitos/fisiologia , Testes de Sensibilidade Microbiana , Modelos Moleculares , Oligopeptídeos/farmacologia , Ratos , Alinhamento de Sequência , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Venenos de Vespas/farmacologia , Vespas
4.
Acta Crystallogr D Biol Crystallogr ; 57(Pt 11): 1560-70, 2001 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-11679720

RESUMO

The molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement led to an R factor of 0.161 at 2.45 A resolution. The positions of 2437 non-H protein atoms in 326 residues have been determined and the model contains 143 water molecules. The structure is bilobal, consisting of two predominantly beta-sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo-twofold axis. A model of the uropepsin-pepstatin complex has been constructed based on the high-resolution crystal structure of pepsin complexed with pepstatin.


Assuntos
Endopeptidases/química , Sequência de Aminoácidos , Sítios de Ligação , Catálise , Cristalização , Cristalografia por Raios X , Humanos , Modelos Moleculares , Dados de Sequência Molecular , Pepstatinas/metabolismo , Conformação Proteica , Controle de Qualidade , Homologia de Sequência de Aminoácidos , Especificidade por Substrato
5.
Biochim Biophys Acta ; 1545(1-2): 372-6, 2001 Feb 09.
Artigo em Inglês | MEDLINE | ID: mdl-11342062

RESUMO

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. These peptides present a wide spectrum of biological activities, such as mast cell degranulation, hemolytic activity and also reveals antimicrobial activity. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized. At room temperature these crystals diffracted to 2.8 A resolution. However, upon cooling to cryogenic temperature around 85 K, the original resolution limit could be improved to 2.0 A. Crystals were determined to belong to the space group P3(1) (P3(2)). This is the first mastoparan to be crystallized and it will provide further insights in the conformational significance of mastoparan toxins, with respect to their potency and activity in G protein regulation.


Assuntos
Cristalografia por Raios X/métodos , Proteínas de Insetos/química , Venenos de Vespas/química , Vespas/metabolismo , Animais , Temperatura Baixa , Cristalização , Proteínas de Insetos/isolamento & purificação , Venenos de Vespas/isolamento & purificação
6.
Acta Crystallogr D Biol Crystallogr ; 56(Pt 11): 1434-6, 2000 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-11053843

RESUMO

Mastoparans are tetradecapeptides found to be the major component of vespid venoms. A mastoparan toxin isolated from the venom of Anterhynchium flavomarginatum micado has been crystallized and X-ray diffraction data collected to 2.7 A resolution using a synchrotron-radiation source. Crystals were determined to belong to the space group P6(2)22 (P6(4)22). This is the first mastoparan to be crystallized and will provide further insights into the conformational significance of mastoparan toxins with respect to their potency and activity in G-protein regulation.


Assuntos
Degranulação Celular , Mastócitos/citologia , Venenos de Vespas/química , Cristalização , Cristalografia por Raios X , Conformação Proteica
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