Análise e identificaçăo de proteínas celulares e proteínas secretadas por Herbaspirillum seropedicae /

Orientador : Fábio de Oliveira PedrosaInclui bibliografia e anexo

An Experimental Model for Resistance Exercise in Rodents

This study aimed to develop an equipment and system of resistance exercise (RE), based on squat-type exercise for rodents, with control of training variables. We developed an operant conditioning system composed of sound, light and feeding devices that allowed optimized RE performance by the animal. With this system, it is not necessary to impose fasting or electric shock for the animal to perform the task proposed (muscle contraction). Furthermore, it is possible to perform muscle function tests in vivo within the context of the exercise proposed and control variables such as intensity, volume (sets and repetitions), and exercise session length, rest interval between sets and repetitions, and concentric strength. Based on the experiments conducted, we demonstrated that the model proposed is able to perform more specific control of other RE variables, especially rest interval between sets and repetitions, and encourages the animal to exercise through short-term energy restriction and “disturbing” stimulus that do not promote alterations in body weight. Therefore, despite experimental limitations, we believe that this RE apparatus is closer to the physiological context observed in humans

An Experimental Model for Resistance Exercise in Rodents

This study aimed to develop an equipment and system of resistance exercise (RE), based on squat-type exercise for rodents, with control of training variables. We developed an operant conditioning system composed of sound, light and feeding devices that allowed optimized RE performance by the animal. With this system, it is not necessary to impose fasting or electric shock for the animal to perform the task proposed (muscle contraction). Furthermore, it is possible to perform muscle function tests in vivo within the context of the exercise proposed and control variables such as intensity, volume (sets and repetitions), and exercise session length, rest interval between sets and repetitions, and concentric strength. Based on the experiments conducted, we demonstrated that the model proposed is able to perform more specific control of other RE variables, especially rest interval between sets and repetitions, and encourages the animal to exercise through short-term energy restriction and “disturbing” stimulus that do not promote alterations in body weight. Therefore, despite experimental limitations, we believe that this RE apparatus is closer to the physiological context observed in humans

Does Branched-Chain Amino Acids Supplementation Modulate Skeletal Muscle Remodeling through Inflammation Modulation? Possible Mechanisms of Action

Skeletal muscle protein turnover is modulated by intracellular signaling pathways involved in protein synthesis, degradation, and inflammation. The proinflammatory status of muscle cells, observed in pathological conditions such as cancer, aging, and sepsis, can directly modulate protein translation initiation and muscle proteolysis, contributing to negative protein turnover. In this context, branched-chain amino acids (BCAAs), especially leucine, have been described as a strong nutritional stimulus able to enhance protein translation initiation and attenuate proteolysis. Furthermore, under inflammatory conditions, BCAA can be transaminated to glutamate in order to increase glutamine synthesis, which is a substrate highly consumed by inflammatory cells such as macrophages. The present paper describes the role of inflammation on muscle remodeling and the possible metabolic and cellular effects of BCAA supplementation in the modulation of inflammatory status of skeletal muscle and the consequences on protein synthesis and degradation

Effects of leucine supplementation and resistance exercise on dexamethasone-induced muscle atrophy and insulin resistance in rats

Objective: We aimed to evaluate the effects of resistance exercise (RE) and leucine (LEU) supplementation on dexamethasone (DEXA)-induced muscle atrophy and insulin resistance.Methods: Male Wistar rats were randomly divided into DEXA(DEX), DEXA + RE (DEX-RE), DEXA + LEU (DEX-LEU), and DEXA + RE + LEU (DEX-RE-LEU) groups. Each group received DEXA 5 mg . kg(-1) . d(-1) for 7 d from drinking water and were pair-fed to the DEX group; LEU-supplemented groups received 0.135 g . kg(-1) . d(-1) through gavage for 7 d; the RE protocol was based on three sessions of squat-type exercise composed by three sets of 10 repetitions at 70% of maximal voluntary strength capacity.Results: the plantaris mass was significantly greater in both trained groups compared with the non-trained groups. Muscle cross-sectional area and fiber areas did not differ between groups. Both trained groups displayed significant increases in the number of intermediated fibers (IIa/IIx), a decreased number of fast-twitch fibers (IIb), an increased ratio of the proteins phospho(Ser2448)/ total mammalian target of rapamycin and phospho(Thr389)/total 70-kDa ribosomal protein S6 kinase. and a decreased ratio of phospho(Ser253)/total Forkhead box protein-3a. Plasma glucose was significantly increased in the DEX-LEU group compared with the DEX group and RE significantly decreased hyperglycemia. the DEX-LEU group displayed decreased glucose transporter-4 translocation compared with the DEX group and RE restored this response. LEU supplementation worsened insulin sensitivity and did not attenuate muscle wasting in rats treated with DEXA. Conversely, RE modulated glucose homeostasis and fiber type transition in the plantaris muscle.Conclusion: Resistance exercise but not LEU supplementation promoted fiber type transition and improved glucose homeostasis in DEXA-treated rats. (C) 2012 Elsevier Inc. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Univ São Paulo, Lab Appl Nutr & Metab, Sch Phys Educ & Sports, São Paulo, BrazilUniv São Paulo, Inst Biomed Sci, São Paulo, BrazilUniv São Paulo, Lab Mol & Cellular Physiol Exercise, Sch Phys Educ & Sports, São Paulo, BrazilUniv São Paulo, Sch Med, Lab Expt Hypertens, São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biosci, São Paulo, BrazilClermont Univ, UFR Med, UMR Nutr Humaine 1019, Clermont Ferrand, FranceINRA, UMR Unite Nutr Humaine 1019, F-63122 St Genes Champanelle, FranceUniversidade Federal de São Paulo, Dept Biosci, São Paulo, BrazilFAPESP: 08/51090-1FAPESP: 10/07062-3FAPESP: 10/10852-6FAPESP: 11/04690-6Web of Scienc

Análise proteômica das estirpes selvagem, ntrC- e nifA- de Herbaspirillum seropedicae /

Orientador : Fabio de Oliveira PedrosaDissertaçăo (mestrado) - Universidade Federal do Paraná, Setor de Ciencias Biológicas, Programa de Pós-Graduaçao em Bioquímica. Defesa: Curitiba, 2004Inclui bibliografi

Análise e identificaçăo de proteínas celulares e proteínas secretadas por Herbaspirillum seropedicae /

Orientador : Fábio de Oliveira PedrosaInclui bibliografia e anexo

Análise proteômica das estirpes selvagem, ntrC- e nifA- de Herbaspirillum seropedicae

Orientador : Fabio de Oliveira PedrosaDissertaçao (mestrado) - Universidade Federal do Paraná, Setor de Ciencias Biológicas, Programa de Pós-Graduaçao em Bioquímica. Defesa: Curitiba, 2004Inclui bibliografiaResumo: O termo "proteoma" refere-se ao conjunto de proteínas expressas por uma célula em uma determinada condição fisiológica. Foi realizada análise proteômica da estirpe selvagem (SMR1) e das estirpes mutantes SMR54 (nifA-) e DCP286A (ntrC-) de Herbaspirillum seropedicae. As proteínas foram fracionadas por meio de eletroforese bidimensional. A isoeletrofocalização foi realizada em tiras com gradiente imobilizado de pH nas faixas de pH 4 a 7 e pH 3 a 10 e a eletroforese na presença de SDS foi realizada em géis de poliacrilamida 12,5%. Foram realizadas análises da estirpe selvagem na condição de fixação de nitrogênio cultivada em baixo amônio (2mmol/L de NH4Cl) ou em alto amônio (20mmol/L de NH4Cl). Para as estirpes mutantes, incapazes de fixar nitrogênio, foram realizadas análises na condição de baixo amônio e alto amônio. Na estirpe selvagem (SMR1) ocorreu indução de 25 proteínas na condição de fixação de nitrogênio quando comparada com a mesma estirpe cultivada em alto amônio (20mmol/L de NH4Cl). Em condição de alto amônio foram induzidas 12 proteínas na estirpe mutante SMR54 (nifA-) e não ocorreu indução de nenhuma proteína na estirpe mutante DCP286A. Em condição de baixo amônio 3 proteínas foram induzidas na estirpe selvagem, 8 no mutante SMR54 e nenhuma no mutante DCP286A quando comparados com a estirpe selvagem nas mesmas condições. Um grande número de proteínas foi reprimido na condição de fixação de nitrogênio e baixa amônia na estirpe SMR1 e nos mutantes nas duas condições estudadas. As proteínas reprimidas no mutante SMR54 foram reprimidas também no mutante DCP286A porém, no último ocorreu repressão de um número maior de proteínas. Vinte e nove proteínas induzidas na estirpe SMR1 em condição de fixação de nitrogênio ou no mutante SMR54 cultivado em alto amônio (20mmol/L de NH4Cl) foram submetidas a espectrometria de massa utilizando MALDI-ToF, entretanto, os dados provenientes das massas trípticas não foram suficientes para sua identificação

Micronutrient And Physiologic Parameters Before And 6 Months After Rygb.

Bariatric surgery is considered an effective method for sustained weight loss, but may cause various nutritional complications. The aim of this study was to evaluate the nutritional status of minerals and vitamins, food consumption, and to monitor physiologic parameters in patients with obesity before and 6 months after Roux-en-Y gastric bypass surgery (RYGB). Thirty-six patients who had undergone RYGB were prospectively evaluated before and 6 months after surgery. At each phase their weight, height, body mass index (BMI), Electro Sensor Complex (ES Complex) data, food consumption, and total protein serum levels, albumin, prealbumin, parathyroid hormone (PTH), zinc (Zn), B12 vitamin (VitB12), iron (Fe), ferritin, copper (Cu), ionic calcium (CaI), magnesium (Mg), and folic acid were assessed. The mean weight loss from baseline to 6 months after surgery was 35.34±4.82%. Markers of autonomic nervous system balance (P<.01), stiffness index (P<.01), standard deviation of normal-to-normal R-R intervals (SDNN) (P<.01), and insulin resistance (P<.001) were also improved. With regard to the micronutrients measured, 34 patients demonstrated some kind of deficiency. There was a high percentage of Zn deficiency in both pre- (55.55%) and postoperative (61.11%) patients, and 33.33% of the patients were deficient in prealbumin postoperatively. The protein intake after 6 months of surgery was below the recommended intake (<70 g/d) for 88.88% of the patients. Laboratory analyses demonstrated an average decrease in total protein (P<.05), prealbumin (P = .002), and PTH (P = .008) between pre- and postsurgery, and a decrease in the percentage of deficiencies for Mg (P<.05), CaI (P<.05), and Fe (P = .021). Despite improvements in the autonomic nervous system balance, stiffness index markers and insulin resistance, we found a high prevalence of hypozincemia at 6 months post-RYGB. Furthermore, protein supplements were needed to maintain an adequate protein intake up to 6 months postsurgery.10944-5