scholarly journals Treatment with Aconitum Lizhong Pill down-regulates liver energy charge in rats with Spleen Yang Deficiency syndrome

2010 ◽  
Vol 18 (35) ◽  
pp. 3782 ◽  
Author(s):  
Wen-Tong Zhang ◽  
Han-Qing Tang ◽  
A-Na Lu ◽  
Xin Zhao ◽  
Guo-Zhang Li ◽  
...  
2000 ◽  
Vol 279 (6) ◽  
pp. R2048-R2056 ◽  
Author(s):  
Mauricio Díaz-Muñoz ◽  
Olivia Vázquez-Martínez ◽  
Raúl Aguilar-Roblero ◽  
Carolina Escobar

Restricted feeding schedules entrain behavioral and physiological circadian rhythms, which depend on a food-entrainable oscillator (FEO). The mechanism of the FEO might depend on digestive and endocrine processes regulating energy balance. The present study characterizes the dynamics of circulating corticosterone, insulin, and glucagon and regulatory parameters of liver metabolism in rats under restricted feeding schedules. With respect to ad libitum controls, food-restricted rats showed 1) an increase in corticosterone and glucagon and a decrease in insulin before food access, indicating a predominant catabolic state; and 2) a reduction in lactate-to-pyruvate and β-hydroxybutyrate-to-acetoacetate ratios, indicating an oxidized cytoplasmic and mitochondrial redox state in the liver metabolism. All these changes were reversed after feeding. Moreover, liver energy charge in food-restricted rats did not show a significant modification before feeding, despite an increase in adenine nucleotides, but showed an important decrease after food intake. Variations detected in the liver of food-restricted rats are different from those prevailing under 24-h fasting. These observations suggest “anticipatory activity” of the liver metabolism to optimize the processing of nutrients to daily feeding. Data also suggest a possible relationship of the liver and endocrine signals with the FEO.


2017 ◽  
Author(s):  
Edna Roche ◽  
Anne McGowan ◽  
Olympia Koulouri ◽  
Marc-Olivier Turgeon ◽  
Adeline K Nicholas ◽  
...  

2019 ◽  
Author(s):  
Alisher M Kariev ◽  
Michael Green

Quantum calculations on 976 atoms of the voltage sensing domain of the K<sub>v</sub>1.2 channel, with protons in several positions, give energy, charge transfer, and other properties. Motion of the S4 transmembrane segment that accounts for gating current in standard models is shown not to occur; there is H<sup>+ </sup>transfer instead. The potential at which two proton positions cross in energy approximately corresponds to the gating potential for the channel. The charge displacement seems approximately correct for the gating current. Two mutations are accounted for (Y266F, R300cit, cit =citrulline). The primary conclusion is that voltage sensing depends on H<sup>+</sup> transfer, not motion of arginine charges.


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