Navegando por Palavras-chave "apolipoprotein A-I"

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    The effect of nutritional intervention on the lipid profile and dietary intake of adolescents with juvenile systemic lupus erythematosus: a randomized, controlled trial
    (Sage Publications Ltd, 2018) Silva, S. G. L. da [UNIFESP]; Terreri, Maria Teresa Ramos Ascensão [UNIFESP]; Abad, Thais Tobaruela Ortiz [UNIFESP]; Machado, D. [UNIFESP]; Fonseca, Fernando Luiz Affonso [UNIFESP]; Hix, S.; Suano de Souza, Fabiola Isabel [UNIFESP]; Sarni, Roseli Oselka Saccardo [UNIFESP]; Len, Claudio Arnaldo [UNIFESP]
    Objective This study sought to evaluate the effects of a nutritional intervention on the lipid metabolism biomarkers associated with cardiovascular risk, and their variation over time, in juvenile systemic lupus erythematosus (JSLE) patients. This study also investigated the relationships between these biomarkers and dietary intake, nutritional status, disease variables, and medication used. Methods A total of 31 10- to 19-year-old female adolescents with JSLE for at least six months were analyzed. The participants were randomly allocated to two groups: nutritional intervention or control. The intervention group received verbal and printed nutritional instructions once per month over nine months. Before and after the intervention, the participants underwent assessments of anthropometry
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    Transthyretin is a metallopeptidase with an inducible active site
    (Portland Press Ltd, 2012-05-01) Liz, Marcia A.; Leite, Sergio C.; Juliano, Luiz [UNIFESP]; Saraiva, Maria J.; Damas, Ana M.; Bur, Daniel; Sousa, Monica M.; IBMC; Universidade Federal de São Paulo (UNIFESP); Univ Porto; Actel Pharmaceut Ltd
    TTR (transthyretin) was found recently to possess proteolytic competency besides its well-known transport capabilities. It was described as a cryptic serine peptidase cleaving multiple natural substrates (including beta-amyloid and apolipoprotein A-I) involved in diseases such as Alzheimer's disease and atherosclerosis. in the present study, we aimed to elucidate the catalytic machinery of TTR. All attempts to identify a catalytic serine residue were unsuccessful. However, metal chelators abolished TTR activity. Proteolytic inhibition by EDTA or 1,10-phenanthroline could be reversed with Zn2+ and Mn2+. These observations, supported by analysis of three-dimensional structures of TTR complexed with Zn2+, led to the hypothesis that TTR is a metallopeptidase. Site-directed mutagenesis of selected amino acids unambiguously confirmed this hypothesis. the TTR active site is inducible and constituted via a protein rearrangement resulting in similar to 7% of proteolytically active TTR at pH 7.4. the side chain of His(88) is shifted near His(90) and Gin(92) establishing a Zn2+-chelating pattern HXHXE not found previously in any metallopeptidase and only conserved in TTR of humans and some other primates. Point mutations of these three residues yielded proteins devoid of proteolytic activity. Glu(72) was identified as the general base involved in activation of the catalytic water. Our results unveil TTR as a metallopeptidase and define its catalytic machinery.