358 research outputs found
Role of ubiquitin-proteasome-dependent proteolytic process in degradation of muscle proteic from diabetic rabbits.
The activity of ATP, ubiquitin (Ub)-dependent proteases partially purified from skeletal muscle (psoas) from alloxan diabetic
rabbits was determined at different periods of insulin deficiency. Two days after alloxan injection, no change was observed in
the activity of ATP, Ub-dependent proteases, but this activity increased 3 and 5 days after diabetes induction, attaining 181%
of control values on the 5th day. However, after this early rise, the activity of muscle ATP, Ub-dependent proteases decreased,
returning to values that did not differ significantly from controls 7 and 10 days after alloxan injection. After 15 days, the activity
of these proteases was 57% lower than in muscle from control rabbits. Both the initial increase and the subsequent fall in
the activity of the enzymes were prevented by insulin treatment of alloxan diabetic rabbits. The data suggest that Ub-proteasomedependent
proteolysis have an important role in the control of muscle protein degradation and may be regulated by insulin
Increased Glyceride-Glycerol Synthesis in Liver and Brown Adipose Tissue of Rat: In-Vivo Contribution of Glycolysis and Glyceroneogenesis
We have previously shown that a high-protein, carbohydrate-free diet can decrease the production of glycerol-3-phosphate (G3P) from glucose and increase glyceroneogenesis in both brown (BAT) and epididymal (EAT) adipose tissue. Here, we utilized an in-vivo approach to examine the hypothesis that there is reciprocal regulation in the G3P synthesis from glucose (via glycolysis) and glyceroneogenesis in BAT, EAT and liver of fasted rats and cafeteria diet-fed rats. Glyceroneogenesis played a prominent role in the generation of G3P in the liver (similar to 70 %) as well as in BAT and EAT (similar to 80 %) in controls rats. The cafeteria diet induced an increase in the total glyceride-glycerol synthesis and G3P synthesis from glucose and a decrease in glyceroneogenesis in BAT; this diet did not affect either the total glyceride-glycerol synthesis or G3P generation from glyceroneogenesis or glycolysis in the liver or EAT. Fasting induced an increase in total glyceride-glycerol synthesis and glyceroneogenesis and a decrease in G3P synthesis from glucose in the liver but did not affect either the total glyceride-glycerol synthesis or G3P synthesis from glyceroneogenesis in BAT and EAT, despite a reduction in glycolysis in these tissues. These data demonstrate that reciprocal changes in the G3P generation from glucose and from glyceroneogenesis in the rat liver and BAT occur only when the synthesis of glycerides-glycerol is increased. Further, our data suggest that this increase may be essential for the systemic recycling of fatty acids by the liver from fasted rats and for the maintenance of the thermogenic capacity of BAT from cafeteria diet-fed rats.Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)Conselho Nacional de Pesquisa (CNPq)Conselho Nacional de Pesquisa (CNPq
Role of adrenoceptors and cAMP on the catecholamine-induced inhibition of proteolysis in rat skeletal muscle
Fatty acid synthesis and generation of glycerol-3-phosphate in brown adipose tissue from rats fed a cafeteria diet
In vivo fatty acid synthesis and the pathways of glycerol-3-phosphate (G3P) production were investigated in brown adipose tissue (BAT) from rats fed a cafeteria diet for 3 weeks. In spite of BAT activation, the diet promoted an increase in the carcass fatty acid content. Plasma insulin levels were markedly increased in cafeteria diet-fed rats. Two insulin-sensitive processes, in vivo fatty acid synthesis and in vivo glucose uptake (which was used to evaluate G3P generation via glycolysis) were increased in BAT from rats fed the cafeteria diet. Direct glycerol phosphorylation, evaluated by glycerokinase (GyK) activity and incorporation of [U-(14)C]glycerol into triacylglycerol (TAG)-glycerol, was also markedly increased in BAT from these rats. In contrast, the cafeteria diet induced a marked reduction of BAT glyceroneogenesis, evaluated by phosphoenolpyruvate carboxykinase-C activity and incorporation of [1-(14)C]pyruvate into TAG-glycerol. BAT denervation resulted in an approximately 50% reduction of GyK activity, but did not significantly affect BAT in vivo fatty acid synthesis, in vivo glucose uptake, or glyceroneogenesis. The data suggest that the supply of G3P for BAT TAG synthesis can be adjusted independently from the sympathetic nervous system and solely by reciprocal changes in the generation of G3P via glycolysis and via glyceroneogenesis, with no participation of direct phosphorylation of glycerol by GyK
Management of dynamic production networks from a critical chain perspective
Collaborative networks are typically assumed to bring clear benefits and competitive advantage to the participating members. However, as the networks are typically formed by heterogeneous and autonomous enterprises, the development of methodologies that facilitates the management process is an important element for the wide adoption of this paradigm. Departing from a brief presentation of Critical Chain Project Management Concepts, this paper introduces an approach of these concepts to collaborative networks and discusses its potential application in the context of a dynamic production networks. Finally, experimental results based on data from a network in construction industry are presented.info:eu-repo/semantics/publishedVersio
Effects of a high protein diet on the evolution of diabetes in streptozotocin-induced and spontaneously diabetic âBBâ wistar rats
Glyceroneogenesis Is Reduced and Glucose Uptake Is Increased in Adipose Tissue from Cafeteria DietâFed Rats Independently of Tissue Sympathetic Innervation
Dietetic supplementation with branched chain amino acids attenuates the severity of streptozotocin-induced diabetes in rats
Heliotropic responses of soybean cultivars at three phenological stages and under two water regimes
CL 316,243, a selective ÎČ3-adrenergic agonist, inhibits protein breakdown in rat skeletal muscle
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