Navegando por Autor "Machado, Richele Janaína Araújo"
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TCC Avaliação do risco cardiovascular por diferentes métodos no âmbito da atenção primária à saúde(Universidade Federal do Rio Grande do Norte, 2016-06) Sousa, Iasmin Matias de; Fayh, Ana Paula Trussardi; Victor Araújo Ferreira Matos; Fayh, Ana Paula Trussardi; Matos, Victor Araújo Ferreira; Machado, Richele Janaína AraújoO crescente número de DCV no mundo torna fundamental o desenvolvimento de estudos que investiguem os métodos de avaliação do risco cardiovascular no âmbito da atenção primária, visando facilitar o diagnóstico através de instrumentos mais acessíveis e rápidos. O objetivo desta pesquisa foi comparar o risco cardiovascular de pacientes adultos e idosos a partir da utilização de duas versões do Escore de Risco de Framingham. O estudo foi do tipo transversal desenvolvido com adultos e idosos atendidos no período de 2002 a 2016 no ambulatório de nutrição da UFRN. Foram avaliados: risco cardiovascular, idade cardíaca e o perfil de marcadores cardiometabólicos (glicemia de jejum, pressão arterial sistólica, colesterol e IMC). Para o cálculo do risco cardiovascular foram utilizados os seguintes dados: idade, sexo, pressão arterial sistólica, uso de medicamento anti-hipertensivo, tabagismo, diabetes, colesterol total e colesterol HDL (método tradicional) ou altura e peso (método simplificado). Foram avaliados 62 indivíduos (masculino n= 17, feminino n=45), idade: 49,1± 12,1 anos, IMC: 32,4± 7,3, pressão arterial: 127,3± 15,7, glicemia: 103,5± 41,0. O risco cardiovascular foi classificado como baixo (<10%), intermediário (10-20%) e alto (>20%). Para verificar as diferenças entre os escores de Framingham tradicional (COL) versus simplificado (IMC) para o risco cardiovascular e idade cardíaca fora utilizado o teste t para amostras independentes, o nível de significância aceito foi de 5%. Não houve diferença estatisticamente significativa entre o risco cardiovascular (p=0,201) e a idade cardíaca (p=0,445) entre os dois métodos. A avaliação do risco cardiovascular em ambos os métodos demonstrou maioria (63% e 58%) com baixo risco para tradicional e simplificado respectivamente. Com isso, é possível concluir que o método simplificado não apresentou diferença com relação à avaliação do risco cardiovascular e estimativa da idade cardíaca quando comparado com o tradicional que utiliza dados bioquímicos, podendo o simplificado ser uma alternativa para avaliação de indivíduos atendidos à nível primário de atenção em saúde por ser rápido, acessível, prático e fidedigno auxiliando na identificação dos indivíduos mais propensos e direcionando-os ao tratamento adequado precocemente.Artigo Characterization and pharmacological properties of a novel multifunctional kunitz inhibitor from erythrina velutina seeds(PloS One, 2013-05) Morais, Ana Heloneida de Araújo; Machado, Richele Janaína Araújo; Monteiro, Norberto de Kássio Vieira; Migliolo, Ludovico; Silva, Osmar Nascimento; Pinto, Michele Flaviane Soares; Oliveira, Adeliana; Franco, Octávio Luiz; Kiyota, Sumika; Bemquerer, Marcelo Porto; Uchôa, Adriana Ferreira; Santos, Elizeu Antunes dosInhibitors of peptidases isolated from leguminous seeds have been studied for their pharmacological properties. The present study focused on purification, biochemical characterization and anti-inflammatory and anticoagulant evaluation of a novel Kunitz trypsin inhibitor from Erythrina velutina seeds (EvTI). Trypsin inhibitors were purified by ammonium sulfate (30–60%), fractionation followed by Trypsin-Sepharose affinity chromatography and reversed-phase high performance liquid chromatography. The purified inhibitor showed molecular mass of 19,210.48 Da. Furthermore, a second isoform with 19,228.16 Da was also observed. The inhibitor that showed highest trypsin specificity and enhanced recovery yield was named EvTI (P2) and was selected for further analysis. The EvTI peptide fragments, generated by trypsin and pepsin digestion, were further analyzed by MALDI-ToF-ToF mass spectrometry, allowing a partial primary structure elucidation. EvTI exhibited inhibitory activity against trypsin with IC50 of 2.261028 mol.L21 and constant inhibition (Ki) of 1.061028 mol.L21 , by a non-competitive mechanism. In addition to inhibit the activity of trypsin, EvTI also inhibited factor Xa and neutrophil elastase, but do not inhibit thrombin, chymotrypsin or peptidase 3. EvTI was investigated for its anti-inflammatory and anticoagulant properties. Firstly, EvTI showed no cytotoxic effect on human peripheral blood cells. Nevertheless, the inhibitor was able to prolong the clotting time in a dose-dependent manner by using in vitro and in vivo models. Due to antiinflammatory and anticoagulant EvTI properties, two sepsis models were here challenged. EvTI inhibited leukocyte migration and specifically acted by inhibiting TNF-a release and stimulating IFN-a and IL-12 synthesis. The data presented clearly contribute to a better understanding of the use of Kunitz inhibitors in sepsis as a bioactive agent capable of interfering in blood coagulation and inflammationArtigo Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation(Acta Chromatographica, 2019-06) Morais, Ana Heloneida de Araújo; Maciel, Bruna Leal Lima; Medeiros, Amanda Fernandes de; Rocha, Maria Gabriela Ferreira; Serquiz, Alexandre Coelho; Machado, Richele Janaína Araújo; Lima, Vanessa Cristina Oliveira; Carvalho, Fabiana Maria Coimbra de; Costa, Izael de Sousa; Santos, Elizeu Antunes dosTrypsin inhibitors have been described in peanuts and their derived industrialized foods, demonstrating diversity and thermoresistance. Given their most varied applications, these enzymatic protease inhibitors have been isolated and characterized for their potential use as bioinsecticides, herbal medicines, or medicines, but it is not simple. There are still no reports in the literature of the isolation and characterization of trypsin inhibitors in cultivar cavalo rosa (CCR) peanut, a common variety in Brazil. However, there are biological activities related to trypsin inhibitors from peanut-derived products. In this study, we isolated and characterized a novel trypsin inhibitor in CCR peanuts (Arachis hypogaea L.) under different processing conditions using a simple improved isolation. Raw and toasted peanut inhibitor was isolated by ammonium sulfate fractionation and trypsin-cyanogen bromide-activated SepharoseW 4B (CNBr-SepharoseW 4B) chromatography. The inhibitors from raw and toasted peanut were called AhTI1 and AhTI2, respectively, with potent anti-trypsin activity. Activity at different temperatures and pH was evaluated, and both samples were similarly stable under tested conditions. Minimum concentration for inhibition to occur (IC50) was 2.78 × 10−10 M and 2.39 × 10−10 M for AhTI1 and AhTI2, and inhibition constant (Ki) was 3.26 × 10−10 M and 1.54 × 10−10 M, respectively, showing non-competitive reversible kinetics. We concluded that AhTI1 and AhTI2 presented highly specific to trypsin and stable to toasting, different temperatures, and pH ranging. These are important characteristics in the process of developing bioinsecticides or biopharmaceuticals. Thus, this may be an interesting molecule, aiming at its biotechnological application, and it was obtained using a simple and easy isolation processArtigo Characterization of novel trypsin inhibitor in raw and toasted peanuts using a simple improved isolation(Acta Chromatographica, 2019-06) Maciel, Bruna Leal Lima; Medeiros, Amanda Fernandes de; Rocha, Maria Gabriela Ferreira; Serquiz, Alexandre Coelho; Machado, Richele Janaína Araújo; Lima, Vanessa Cristina Oliveira; Carvalho, Fabiana Maria Coimbra de; Costa, Izael de Sousa; Santos, Elizeu Antunes dos; Morais, Ana Heloneida de AraújoTrypsin inhibitors have been described in peanuts and their derived industrialized foods, demonstrating diversity and thermoresistance. Given their most varied applications, these enzymatic protease inhibitors have been isolated and characterized for their potential use as bioinsecticides, herbal medicines, or medicines, but it is not simple. There are still no reports in the literature of the isolation and characterization of trypsin inhibitors in cultivar cavalo rosa (CCR) peanut, a common variety in Brazil. However, there are biological activities related to trypsin inhibitors from peanut-derived products. In this study, we isolated and characterized a novel trypsin inhibitor in CCR peanuts (Arachis hypogaea L.) under different processing conditions using a simple improved isolation. Raw and toasted peanut inhibitor was isolated by ammonium sulfate fractionation and trypsin-cyanogen bromide-activated SepharoseW 4B (CNBr-SepharoseW 4B) chromatography. The inhibitors from raw and toasted peanut were called AhTI1 and AhTI2, respectively, with potent anti-trypsin activity. Activity at different temperatures and pH was evaluated, and both samples were similarly stable under tested conditions. Minimum concentration for inhibition to occur (IC50) was 2.78 × 10−10 M and 2.39 × 10−10 M for AhTI1 and AhTI2, and inhibition constant (Ki) was 3.26 × 10−10 M and 1.54 × 10−10 M, respectively, showing non-competitive reversible kinetics. We concluded that AhTI1 and AhTI2 presented highly specific to trypsin and stable to toasting, different temperatures, and pH ranging. These are important characteristics in the process of developing bioinsecticides or biopharmaceuticals. Thus, this may be an interesting molecule, aiming at its biotechnological application, and it was obtained using a simple and easy isolation process