Biodisponibilidade de ferro em diferentes compostos para leitões desmamados aos 21 dias de idade

Avaliou-se a biodisponibilidade de ferro de diferentes compostos visando sua utilização em dietas para leitões desmamados. Utilizaram-se 44 leitões (7 não-anêmicos e 37 anêmicos) desmamados aos 21 dias de idade (7,3 ± 1,8 kg) e distribuídos em dois grupos: grupo não-anêmico e grupo anêmico. Durante sete dias, os animais do grupo não-anêmico receberam dieta com FeSO4.7H2O (sulfato ferroso hepta-hidratado) na dose de 100 mg/kg e os do grupo anêmico, dieta sem ferro (<15 mg/kg ração). No sétimo dia, depois de determinada a concentração de hemoglobina sanguínea e diagnosticada a anemia, os leitões foram agrupados segundo o produto do peso (kg) × hemoglobina (g/dL) e alojados individualmente, durante 13 dias, em gaiolas para estudos de digestibilidade, onde foram alimentados com seis rações à base de milho e leite em pó: três rações-padrão com FeSO4.7H2O em quantidade equivalente a 80, 150 e 200 mg Fe/kg de ração; duas rações experimentais com ferro (150 mg/kg) na forma de FeSO4 microencapsulado com carboximetilcelulose ou de ferro quelado com metionina; e uma controle com ferro (100 mg/kg). O consumo de ração foi medido diariamente. Nos dias 0, 3, 6, 9 e 13 do período de repleção, os animais foram pesados para avaliação do desempenho e o sangue foi coletado para determinação da concentração de hemoglobina. Ao final do ensaio, os animais foram sacrificados e o fígado foi coletado para determinação das concentrações de ferro total, ferro heme e ferro não-heme. As concentrações hepáticas de ferro heme, ferro não-heme e ferro total não diferiram entre os animais, entretanto, os do grupo controle apresentaram excesso de ferro total no fígado, relacionado à dose de ferro injetada nos leitões após o desmame. em comparação ao FeSO4.7H2O não encapsulado, os compostos de ferro microencapsulado com carboximetilcelulose e de ferro quelado com metionina promovem melhor conversão alimentar em leitões desmamados.

Orchidectomy enhances the effects of phenylephrine in rat isolated portal vein

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Cloning and Identification of a Complete cDNA Coding for a Bactericidal and Antitumoral Acidic Phospholipase A(2) from Bothrops jararacussu Venom

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

In vivo uptake of a haem analogue Zn protoporphyrin IX by the human malaria parasite P. falciparum-infected red blood cells

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Neuroglobin and cytoglobin: two new members of globin family

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Fish hemoglobins

Vertebrate hemoglobin, contained in erythrocytes, is a globular protein with a quaternary structure composed of 4 globin chains (2 alpha and 2 beta) and a prosthetic group named heme bound to each one. Having myoglobin as an ancestor, hemoglobin acquired the capacity to respond to chemical stimuli that modulate its function according to tissue requirements for oxygen. Fish are generally submitted to spatial and temporal O2 variations and have developed anatomical, physiological and biochemical strategies to adapt to the changing environmental gas availability. Structurally, most fish hemoglobins are tetrameric; however, those from some species such as lamprey and hagfish dissociate, being monomeric when oxygenated and oligomeric when deoxygenated. Fish blood frequently possesses several hemoglobins; the primary origin of this finding lies in the polymorphism that occurs in the globin loci, an aspect that may occasionally confer advantages to its carriers or even be a harmless evolutionary remnant. on the other hand, the functional properties exhibit different behaviors, ranging from a total absence of responses to allosteric regulation to drastic ones, such as the Root effect.

Structural aspects, thermal behavior, and stability of a self-assembled supramolecular polymer derived from flunixin-meglumine supramolecular adducts

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Quimiometria como ferramenta analitica para definição das condiçoes de ensaio da enzima peroxidase de soja

Enzimas Peroxidases são heme-proteínas encontradas nos diferentes organismos vivos, especialmente vegetais, apresentam importante papel fisiológico/bioquímico como proteção contra microorganismos invasores. A soja, um dos mais importantes produtos para o agronegócio brasileiro apresenta na casca de suas sementes (subproduto) alta atividade de peroxidase, denominada soybean peroxidase,com potencial de utilização em métodos analíticos clínicos. A proposta do trabalho foi aplicar o planejamento fatorial para otimização das condições extração da enzima, definição das condições ótimas de atividade (pH e temperatura), utilizando metodologia de superfície de resposta. Os dados obtidos com clara definição foram: i) extração em pó cetonico, ii) meio reacional: pH 3,3, volume da amostra contendo a enzima 330 µL - 340 µL, peróxido de hidrogênio 4,2 mmol.L-1 150 µL, tempo de reação 20 segundos, temperatura 50º C, substrato guaiacol 30mmol.L-1 300 µL, e 0,1 mol.L-1 de NaCl. O uso da dessa metodologia para definição das condições de extração e estudos cinético-enzimáticos da peroxidase de soja foram eficientes e mais precisos, comparado a metodologia de variações/repetições (tentativa e erro).

5-AMINOLEVULINIC ACID-INDUCED ALTERATIONS OF OXIDATIVE-METABOLISM IN SEDENTARY AND EXERCISE-TRAINED RATS

5-Aminolevulinic acid (ALA), a heme precursor that accumulates in acute intermittent porphyria patients and lead-exposed individuals, has previously been shown to autoxidize with generation of reactive oxygen species and to cause in vitro oxidative damage to rat liver mitochondria. We now demonstrate that chronically ALA-treated rats (40 mg/kg body wt every 2 days for 15 days) exhibit decreased mitochondrial enzymatic activities (superoxide dismutase, citrate synthase) in liver and soleus (type I, red) and gastrocnemius (type IIb, white) muscle fibers. Previous adaptation of rats to endurance exercise, indicated by augmented (cytosolic) CuZn-superoxide dismutase (SOD) and (mitochondrial) Mn-SOD activities in several organs, does not protect the animals against liver and soleus mitochondrial damage promoted by intraperitoneal injections of ALA. This is suggested by loss of citrate synthase and Mn-SOD activities and elevation of serum lactate levels, concomitant to decreased glycogen content in soleus and the red portion of gastrocnemius (type IIa) fibers of both sedentary and swimming-trained ALA-treated rats. In parallel, the type IIb gastrocnemius fibers, which are known to obtain energy mainly by glycolysis, do not undergo these biochemical changes. Consistently, ALA-treated rats under swimming training reach fatigue significantly earlier than the control group. These results indicate that ALA may be an important prooxidant in vivo.

Proteinase-activated receptor-2 (PAR2) agonist causes periodontitis in rats

Proteinase-activated receptor-2 (PAR2) is a G-protein-coupled receptor that mediates cellular responses to extracellular proteinases. Since PAR2 is expressed by oral epithelial cells, osteoblasts, and gingival fibroblasts, where its activation releases interleukin-8, we hypothesized that PAR2 activation may participate in periodontal disease in vivo. We investigated the role of PAR2 activation in periodontal disease in rats. Radiographic and enzymatic (myeloperoxidase) analysis revealed that topical application of PAR2 agonist causes periodontitis but also exacerbates existing periodontitis, leading to significant alveolar bone loss and gingival granulocyte infiltration. Inhibition of matrix metalloproteinase (MMP) and cyclo-oxygenase (COX) decreased PAR2 agonist-induced periodontitis. More specifically, the overexpression of COX-1, COX-2, MMP-2, and MMP-9 in gingival tissues suggests that they are involved in PAR 2-induced periodontitis. In conclusion, PAR2 agonist causes periodontitis in rats through a mechanism involving prostaglandin release and MMP activation. Inhibition of PAR2 may represent a novel approach to modulate host response in periodontitis.

Effect of fortification of drinking water with iron plus ascorbic acid or with ascorbic acid alone on hemoglobin values and anthropometric indicators in preschool children in day-care centers in Southeast Brazil

Background. Iron-deficiency anemia currently is the most frequently occurring nutritional disorder worldwide. Previous Brazilian studies have demonstrated that drinking water fortified with iron and ascorbic acid is an adequate vehicle for improving the iron supply for children frequenting day-care centers. Objective. The objective of this study was to clarify the role of ascorbic acid as a vehicle for improving iron intake in children in day-care centers in Brazil. Methods. A six-month study was conducted on 150 children frequenting six day-care centers divided into two groups of three day-care centers by drawing lots: the iron-C group (3 day-care centers, n = 74), which used water fortified with 10 mg elemental iron and 100 mg ascorbic acid per liter, and the comparison group (3 day-care centers, n = 76), which used water containing only 100 mg ascorbic acid per liter. Anthropometric measurements and determinations of capillary hemoglobin were performed at the beginning of the study and after six months of intervention. The food offered at the day-care centers was also analyzed. Results. The fo od offered at the day-care center was found to be deficient in ascorbic acid, poor in heme iron, and adequate in non-heme iron. Supplementation with fortified drinking water resulted in a decrease in the prevalence of anemia and an increase in mean hemoglobin levels associated with height gain in both groups. Conclusions. Fortification of drinking water with iron has previously demonstrated effectiveness in increasing iron supplies. This simple strategy was confirmed in the present study. The present study also demonstrated that for populations receiving an abundant supply of non-heme iron, it is possible to control anemia in a simple, safe, and inexpensive manner by adding ascorbic acid to drinking water. © 2005, The United Nations University.

Alpha-glucosidase promotes hemozoin formation in a blood-sucking bug: An evolutionary history

Background: Hematophagous insects digest large amounts of host hemoglobin and release heme inside their guts. In Rhodnius prolixus, hemoglobin-derived heme is detoxified by biomineralization, forming hemozoin (Hz). Recently, the involvement of the R. prolixus perimicrovillar membranes in Hz formation was demonstrated. Methodology/Principal Findings: Hz formation activity of an α-glucosidase was investigated. Hz formation was inhibited by specific α-glucosidase inhibitors. Moreover, Hz formation was sensitive to inhibition by Diethypyrocarbonate, suggesting a critical role of histidine residues in enzyme activity. Additionally, a polyclonal antibody raised against a phytophagous insect α-glucosidase was able to inhibit Hz formation. The α-glucosidase inhibitors have had no effects when used 10 h after the start of reaction, suggesting that α-glucosidase should act in the nucleation step of Hz formation. Hz formation was seen to be dependent on the substrate-binding site of enzyme, in a way that maltose, an enzyme substrate, blocks such activity. dsRNA, constructed using the sequence of α-glucosidase gene, was injected into R. prolixus females' hemocoel. Gene silencing was accomplished by reduction of both α-glucosidase and Hz formation activities. Insects were fed on plasma or hemin-enriched plasma and gene expression and activity of α-glucosidase were higher in the plasma plus hemin-fed insects. The deduced amino acid sequence of α-glucosidase shows a high similarity to the insect α-glucosidases, with critical histidine and aspartic residues conserved among the enzymes. Conclusions/Significance: Herein the Hz formation is shown to be associated to an a-glucosidase, the biochemical marker from Hemipteran perimicrovillar membranes. Usually, these enzymes catalyze the hydrolysis of glycosidic bond. The results strongly suggest that α-glucosidase is responsible for Hz nucleation in the R. prolixus midgut, indicating that the plasticity of this enzyme may play an important role in conferring fitness to hemipteran hematophagy, for instance. © 2009 Mury et al.

Modulação pelo haplótipo Bantu da resposta ao uso de hidroxiureia em anemia falciforme

Pós-graduação em Genética - IBILCE

Detecção in silico, isolamento e caracterização estrutural dos constitutintes micromoleculares antimaláricos e antioxidantes em galhosmdemGarcina gardneriana (Clusiaceae)

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Desenvolvimento de um biosensor amperométrico para a detecção do vírus da Hepatite C

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)