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1.
J Sci Food Agric ; 97(2): 556-563, 2017 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-27097820

RESUMO

BACKGROUND: Inulin and other fructans are synthesized and stored in mezcal agave (Agave salmiana). Fructans provide several health benefits and have excellent technological properties, but only few data report their physiological effect when added in the diet. RESULTS: Here, we studied the physiological effects of fructans obtained from A. salmiana when added in the diet of Wistar rats. Results showed favorable changes on Wistar rats when the fructans was added to their diet, including the decrease of the pH in the feces and the increase of the number of lactic acid bacteria (CFU g-1 ) (Lactobacillus spp. and Bifidobacterium spp.), even these changes were enhanced with the synbiotic diet (fructans plus B. animalis subsp. lactis). Synbiotic diet, developed changes in the reduction of cholesterol and triglycerides concentrations in serum, with statistical differences (P < 0.05). Histological analysis of colon sections showed that synbiotic diet promoted colon cells growth suggesting that fructans from A. salmiana confer beneficial health effects through gut microbiota modulation. CONCLUSION: Our data underline the advantage of targeting the gut microbiota by colonic nutrients like specific structure of fructans from A. salmiana, with their beneficial effects. More studies are necessary to define the role of fructans to develop more solid therapeutic solutions in humans. © 2016 Society of Chemical Industry.


Assuntos
Agave/química , Disbiose/prevenção & controle , Frutanos/uso terapêutico , Frutas/química , Microbioma Gastrointestinal , Extratos Vegetais/uso terapêutico , Prebióticos , Agave/crescimento & desenvolvimento , Animais , Bifidobacterium/crescimento & desenvolvimento , Bifidobacterium/isolamento & purificação , Bifidobacterium animalis/crescimento & desenvolvimento , Colo/citologia , Colo/microbiologia , Colo/patologia , Disbiose/sangue , Disbiose/microbiologia , Disbiose/patologia , Fezes/química , Fezes/microbiologia , Liofilização , Frutanos/isolamento & purificação , Frutas/crescimento & desenvolvimento , Concentração de Íons de Hidrogênio , Hiperlipidemias/sangue , Hiperlipidemias/microbiologia , Hiperlipidemias/patologia , Hiperlipidemias/prevenção & controle , Mucosa Intestinal/citologia , Mucosa Intestinal/microbiologia , Mucosa Intestinal/patologia , Lactobacillus/crescimento & desenvolvimento , Lactobacillus/isolamento & purificação , Masculino , México , Extratos Vegetais/isolamento & purificação , Distribuição Aleatória , Ratos Wistar , Simbióticos
2.
J Mol Biol ; 426(4): 908-20, 2014 Feb 20.
Artigo em Inglês | MEDLINE | ID: mdl-24333015

RESUMO

Oxidative phosphorylation (OXPHOS) in mitochondria takes place at the inner membrane, which folds into numerous cristae. The stability of cristae depends, among other things, on the mitochondrial intermembrane space bridging complex. Its components include inner mitochondrial membrane protein mitofilin and outer membrane protein Sam50. We identified a conserved, uncharacterized protein, C1orf163 [SEL1 repeat containing 1 protein (SELRC1)], as one of the proteins significantly reduced after the knockdown of Sam50 and mitofilin. We show that C1orf163 is a mitochondrial soluble intermembrane space protein. Sam50 depletion affects moderately the import and assembly of C1orf163 into two protein complexes of approximately 60kDa and 150kDa. We observe that the knockdown of C1orf163 leads to reduction of levels of proteins belonging to the OXPHOS complexes. The activity of complexes I and IV is reduced in C1orf163-depleted cells, and we observe the strongest defects in the assembly of complex IV. Therefore, we propose C1orf163 to be a novel factor important for the assembly of respiratory chain complexes in human mitochondria and suggest to name it RESA1 (for RESpiratory chain Assembly 1).


Assuntos
Membranas Mitocondriais/metabolismo , Proteínas Mitocondriais/metabolismo , Sequência de Aminoácidos , Complexo IV da Cadeia de Transporte de Elétrons/metabolismo , Técnicas de Silenciamento de Genes , Células HeLa , Humanos , Proteínas de Membrana/genética , Proteínas de Membrana/metabolismo , Proteínas do Complexo de Importação de Proteína Precursora Mitocondrial , Proteínas Mitocondriais/genética , Dados de Sequência Molecular , Proteínas Musculares/genética , Proteínas Musculares/metabolismo , Fosforilação Oxidativa , Transporte Proteico , Solubilidade
3.
Metabolites ; 2(4): 940-58, 2012 Nov 16.
Artigo em Inglês | MEDLINE | ID: mdl-24957769

RESUMO

Protein complexes are classified and have been charted in several large-scale screening studies in prokaryotes. These complexes are organized in a factory-like fashion to optimize protein production and metabolism. Central components are conserved between different prokaryotes; major complexes involve carbohydrate, amino acid, fatty acid and nucleotide metabolism. Metabolic adaptation changes protein complexes according to environmental conditions. Protein modification depends on specific modifying enzymes. Proteins such as trigger enzymes display condition-dependent adaptation to different functions by participating in several complexes. Several bacterial pathogens adapt rapidly to intracellular survival with concomitant changes in protein complexes in central metabolism and optimize utilization of their favorite available nutrient source. Regulation optimizes protein costs. Master regulators lead to up- and downregulation in specific subnetworks and all involved complexes. Long protein half-life and low level expression detaches protein levels from gene expression levels. However, under optimal growth conditions, metabolite fluxes through central carbohydrate pathways correlate well with gene expression. In a system-wide view, major metabolic changes lead to rapid adaptation of complexes and feedback or feedforward regulation. Finally, prokaryotic enzyme complexes are involved in crowding and substrate channeling. This depends on detailed structural interactions and is verified for specific effects by experiments and simulations.

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