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1.
J. pediatr. (Rio J.) ; 100(2): 177-183, Mar.-Apr. 2024. tab
Artigo em Inglês | LILACS-Express | LILACS | ID: biblio-1558311

RESUMO

Abstract Objective: To correlate the nasal anatomical characteristics of newborns with the dimensions of short binasal prongs. Method: Observational, cross-sectional study carried out in two hospitals in southern Brazil. The authors evaluated 1620 newborns with neonatal data and nasal dimensions. To measure the dimensions of the nasal region, the authors considered the width of the medial columella, the right nostril diameter, and the left nostril diameter. These data were correlated with the dimensions of two models of short binasal prongs. Results: Of the total newborns evaluated, 807 were female (49.8%), and 813 were male (50.2%). The majority were white (96.2%). The mean gestational age was 37.4 ± 2.9 weeks, ranging from 22 to 42 weeks. The birth weight was 2946.8 ± 699.3 g, ranging from 490.0 to 4740.0 g. Most of the nasal measures were significantly larger than both prong model measurements. Conclusion: The sizes of short binasal prongs available on the Brazilian market do not match the nasal anatomical characteristics of newborns.

2.
Annu Int Conf IEEE Eng Med Biol Soc ; 2019: 1048-1049, 2019 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-31946073

RESUMO

The chronic wound in legs due to vascular abnormalities occurs in 1% to 2% of the adult population. The current treatments are unsatisfactory, and new approaches should be studied. We report in this article a case of a 52-year-old man with a chronic venous wound at the tibia, which has been conventionally treated for nine years. With six weeks of treatment with the autologous fibrin membrane, we were able to identify scar tissue and vascularization, which are characteristic of a healing process.


Assuntos
Cicatrização , Doença Crônica , Cicatriz , Fibrina , Humanos , Masculino , Pessoa de Meia-Idade , Projetos Piloto
3.
PLoS One ; 6(9): e24093, 2011.
Artigo em Inglês | MEDLINE | ID: mdl-21961033

RESUMO

Hsp60 is an abundant and highly conserved family of intracellular molecules. Increased levels of this family of proteins have been observed in the extracellular compartment in chronic inflammation. Administration of M. leprae Hsp65 [WT] in [NZBxNZW]F(1) mice accelerates the Systemic Lupus Erythematosus [SLE] progression whereas the point mutated K(409)A Hsp65 protein delays the disease. Here, the biological effects of M. leprae Hsp65 Leader pep and K(409)A pep synthetic peptides, which cover residues 352-371, are presented. Peptides had immunomodulatory effects similar to that observed with their respective proteins on survival and the combined administration of K(409)A+Leader pep or K(409)A pep+WT showed that the mutant forms were able to inhibit the deleterious effect of WT on mortality, indicating the neutralizing potential of the mutant molecules in SLE progression. Molecular modeling showed that replacing Lysine by Alanine affects the electrostatic potential of the 352-371 region. The number of interactions observed for WT is much higher than for Hsp65 K(409)A and mouse Hsp60. The immunomodulatory effects of the point-mutated protein and peptide occurred regardless of the catalytic activity. These findings may be related to the lack of effect on survival when F(1) mice were inoculated with Hsp60 or K(409)A pep. Our findings indicate the use of point-mutated Hsp65 molecules, such as the K(409)A protein and its corresponding peptide, that may minimize or delay the onset of SLE, representing a new approach to the treatment of autoimmune diseases.


Assuntos
Proteínas de Bactérias/imunologia , Chaperonina 60/imunologia , Lúpus Eritematoso Sistêmico/imunologia , Mutação de Sentido Incorreto , Sequência de Aminoácidos , Animais , Anticorpos Antibacterianos/sangue , Anticorpos Antibacterianos/imunologia , Proteínas de Bactérias/administração & dosagem , Proteínas de Bactérias/genética , Chaperonina 60/administração & dosagem , Chaperonina 60/genética , Ensaio de Imunoadsorção Enzimática , Feminino , Imunização , Imunoglobulina G/sangue , Imunoglobulina G/imunologia , Lúpus Eritematoso Sistêmico/prevenção & controle , Masculino , Camundongos , Camundongos Endogâmicos NZB , Camundongos Endogâmicos , Dados de Sequência Molecular , Peptídeos/administração & dosagem , Peptídeos/genética , Peptídeos/imunologia , Sinais Direcionadores de Proteínas/genética
4.
PLoS One ; 3(8): e3025, 2008 Aug 21.
Artigo em Inglês | MEDLINE | ID: mdl-18716655

RESUMO

The heat shock protein [Hsp] family guides several steps during protein synthesis, are abundant in prokaryotic and eukaryotic cells, and are highly conserved during evolution. The Hsp60 family is involved in assembly and transport of proteins, and is expressed at very high levels during autoimmunity or autoinflammatory phenomena. Here, the pathophysiological role of the wild type [WT] and the point mutated K(409)A recombinant Hsp65 of M. leprae in an animal model of Systemic Lupus Erythematosus [SLE] was evaluated in vivo using the genetically homogeneous [NZBxNZW]F(1) mice. Anti-DNA and anti-Hsp65 antibodies responsiveness was individually measured during the animal's life span, and the mean survival time [MST] was determined. The treatment with WT abbreviates the MST in 46%, when compared to non-treated mice [p<0.001]. An increase in the IgG2a/IgG1 anti-DNA antibodies ratio was also observed in animals injected with the WT Hsp65. Incubation of BALB/c macrophages with F(1) serum from WT treated mice resulted in acute cell necrosis; treatment of these cells with serum from K(409)A treated mice did not cause any toxic effect. Moreover, the involvement of WT correlates with age and is dose-dependent. Our data suggest that Hsp65 may be a central molecule intervening in the progression of the SLE, and that the point mutated K(409)A recombinant immunogenic molecule, that counteracts the deleterious effect of WT, may act mitigating and delaying the development of SLE in treated mice. This study gives new insights into the general biological role of Hsp and the significant impact of environmental factors during the pathogenesis of this autoimmune process.


Assuntos
Proteínas de Bactérias/uso terapêutico , Chaperoninas/uso terapêutico , Lúpus Eritematoso Sistêmico/prevenção & controle , Lúpus Eritematoso Sistêmico/fisiopatologia , Animais , Formação de Anticorpos , Chaperonina 60 , DNA/imunologia , Modelos Animais de Doenças , Progressão da Doença , Relação Dose-Resposta a Droga , Glomerulonefrite/etiologia , Glomerulonefrite/fisiopatologia , Lúpus Eritematoso Sistêmico/classificação , Camundongos , Mycobacterium leprae
5.
Toxicon ; 52(3): 501-7, 2008 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-18652839

RESUMO

BPPs have been identified in the venom of the Bothrops jararaca snake, or deduced from precursor proteins expressed either in the venom gland or in the brain of the snake. Their potentiating activity on bradykinin (Bk) is assumed to occur through a somatic angiotensin-converting enzyme (sACE) inhibitory mechanism. We have demonstrated that synthetic BPPs show remarkable functional differences, despite their high amino acid sequence similarities. Recently, we demonstrated that BPP-10c, after i.p. administration, was found in its intact form and in the form of a unique metabolite (des-Pro(10) BPP-10c) in mouse urine. Given this finding, we selected a number of BPPs with different structure-activities - BPP-5a (

Assuntos
Oligopeptídeos/metabolismo , Oligopeptídeos/urina , Sequência de Aminoácidos , Animais , Masculino , Camundongos , Oligopeptídeos/química , Oligopeptídeos/farmacologia , Relação Estrutura-Atividade
6.
Toxicon ; 51(4): 515-23, 2008 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-18160089

RESUMO

The snake venom proline-rich peptide BPP 10c is an active somatic angiotensin-converting enzyme (sACE) inhibitors. Recently we demonstrated that the anti-hypertensive effect of BPP 10c is not related to the inhibition of sACE alone, thus suggesting that this enzyme is not its only target for blood pressure reduction. In the present work, a biodistribution study in Swiss mice of [(125)I]-BPP 10c in the absence or in the presence of a saturating concentration of captopril, a selective active-site inhibitor of sACE, demonstrated that: (1) [(125)I]-BPP 10c was present in several organs and the renal absorption was significantly high; (2) [(125)I]-BPP 10c showed a clear preference for the kidney, maintaining a high concentration in this organ in the presence of captopril for at least 3h; (3) The residual amount of [(125)I]-BPP 10c in the kidney of animals simultaneously treated with captopril suggest that the peptide can interact with other targets different from sACE in this organ. We also showed that Cy3-labeled BPP 10c was internalized by human embryonic kidney cells (HEK-293T). Taken together, these results suggest that sACE inhibition by captopril affects the tissue distribution of [(125)I]-BPP 10c and that the anti-hypertensive effects of BPP 10c are not only dependent on sACE inhibition.


Assuntos
Anti-Hipertensivos/farmacocinética , Bothrops , Peptídeos/farmacocinética , Proteínas de Répteis/farmacocinética , Animais , Anti-Hipertensivos/química , Linhagem Celular , Humanos , Masculino , Camundongos , Peptídeos/química , Prolina , Proteínas de Répteis/química , Distribuição Tecidual
7.
J Neurochem ; 85(4): 969-77, 2003 May.
Artigo em Inglês | MEDLINE | ID: mdl-12716428

RESUMO

The bradykinin-potentiating peptides from Bothrops jararaca venom are the most potent natural inhibitors of the angiotensin-converting enzyme. The biochemical and biological features of these peptides were crucial to demonstrate the pivotal role of the angiotensin-converting enzyme in blood pressure regulation. In the present study, seven bradykinin-potentiating peptides were identified within the C-type natriuretic peptide precursor cloned from snake brain. The bradykinin-potentiating peptides deduced from the B. jararaca brain precursor are strong in vitro inhibitors of the angiotensin-converting enzyme (nanomolar range), and also potentiate the bradykinin effects in ex vivo and in vivo experiments. Two of these peptides are novel bradykinin-potentiating peptides, one of which displays high specificity toward the N-domain active site of the somatic angiotensin-converting enzyme. In situ hybridization studies revealed the presence of the bradykinin-potentiating peptides precursor mRNAs in distinct regions of the B. jararaca brain, such as the ventromedial hypothalamus, the paraventricular nuclei, the paraventricular organ, and the subcommissural organ. The biochemical and pharmacological properties of the brain bradykinin-potentiating peptides, their presence within the neuroendocrine regulator C-type natriuretic peptide precursor, and their expression in regions of the snake brain correlated to neuroendocrine functions, strongly suggest that these peptides belong to a novel class of endogenous vasoactive peptides.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Encéfalo/metabolismo , Peptídeo Natriurético Tipo C , Oligopeptídeos/farmacologia , Fragmentos de Peptídeos/farmacologia , Precursores de Proteínas/genética , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/química , Animais , Bioensaio , Pressão Sanguínea/efeitos dos fármacos , Bothrops , Bradicinina/farmacologia , Química Encefálica , Sinergismo Farmacológico , Cobaias , Íleo/efeitos dos fármacos , Técnicas In Vitro , Masculino , Dados de Sequência Molecular , Contração Muscular/efeitos dos fármacos , Peptídeo Natriurético Tipo C/biossíntese , Oligopeptídeos/química , Oligopeptídeos/genética , Especificidade de Órgãos , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/genética , Precursores de Proteínas/química , Precursores de Proteínas/metabolismo , RNA Mensageiro/metabolismo , Ratos , Ratos Wistar , Análise de Sequência de DNA , Homologia de Sequência de Aminoácidos , Especificidade por Substrato
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