Lack of correlation between hepatic mitochondrial membrane structure and functions in ethanol-fed rats

Science ◽  
1982 ◽  
Vol 216 (4552) ◽  
pp. 1319-1321 ◽  
Author(s):  
E. Gordon ◽  
J Rochman ◽  
M Arai ◽  
C. Lieber
Author(s):  
A.A. Akhrem ◽  
V.N. Lapko ◽  
A.G. Lapko ◽  
S.P. Martsev ◽  
V.M. Shkumatov ◽  
...  

2020 ◽  
Vol 1862 (11) ◽  
pp. 183442 ◽  
Author(s):  
Artem G. Veiko ◽  
Szymon Sekowski ◽  
Elena A. Lapshina ◽  
Agnieszka Z. Wilczewska ◽  
Karolina H. Markiewicz ◽  
...  

2021 ◽  
Vol 67 (5) ◽  
pp. 54-63
Author(s):  
L.M. Gunina ◽  
◽  
I.L. Rybina ◽  
Yu.A. Ataman ◽  
V.L. Voitenko ◽  
...  

Blood oxygen transport regulation by physical activity increase within training dynamics is provided with different mechanisms: from the quantitative and qualitative erythron restructure (including endogenous erythropoietin rise and main erythrocyte index shifts) to change in haemoglobin affinity to oxygen, its heterogeneous structure and blood flow growth as a result of endothelium hyperpolarisation. However, the erythrocyte itself remains a key performer in blood velocity control, due to its structure and functions. This review summarizes the data of modern scientific literature on the characteristics of erythrocytes, which make these cells one of the key links in the oxygen transport system of the blood. The focus on this property of erythrocytes during physical activity is based on the fact that the athlete’s muscles must be supplied with enough oxygen to ensure high performance. Specific training and extra-training factors affecting the content of erythrocytes have been determined. The membrane structure is treated as a significant erythrocyte part in determining its deformation and microvascular blood transport. Enzymes associated with the erythrocyte membrane and affecting cell viability and performance are described. Besides, it is stressed on monitoring erythrocyte indices via modern equipment and assessing lipid peroxidation, which leads to disorders in erythrocyte membrane structure and functions.


1980 ◽  
Vol 58 (10) ◽  
pp. 1147-1155 ◽  
Author(s):  
E. A. Hosein ◽  
Hung Lee ◽  
Ilan Hofmann

Arrhenius plots were generated on the activity of rat liver mitochondrial cytochrome c oxidase from Metrecal–sucrose fed controls and Metrecal–alcohol fed experimentals. Chronic alcohol feeding resulted in diminished specific activity of cytochrome c oxidase and abolition of the discontinuity temperature at 17.5 °C found in the controls. Twenty-four hours after alcohol withdrawal, a discontinuity temperature reappeared at 14.4 °C; at 48 h it increased to 22.6 °C and returned to normal (17.4 °C) at 72 h. Such liver mitochondria also showed a decreased capacity to oxidize the acetyl group of acetyl carnitine immediately following prolonged alcohol feeding. When the assay was performed following withdrawal from alcohol 24 h later, oxidation was enhanced and this effect persisted for another 48 h. These latter results revealed a diminished capacity of such mitochondria to oxidize short chain fatty acids during alcohol feeding and the reverse during alcohol withdrawal.These results, complemented by thermographic data obtained through differential scanning calorimetry (DSC) reinforced the view that chronic alcoholic feeding induced adaptive changes in the fluidity of rat liver mitochondrial membrane lipids. Moreover, they demonstrated that in the microenvironment of the membrane-bound enzymes on withdrawal from ethanol, the membrane readapts to the new conditions without alcohol. This involved modulation of membrane structure and function and at the same time demonstrated a role for the membrane in the expression of tolerance and functional dependence on alcohol.


Author(s):  
G. LENAZ ◽  
E. BERTOLI ◽  
L. LANDI ◽  
G. PARENTI-CASTELLI ◽  
P. PASQUALI ◽  
...  

1984 ◽  
Vol 62 (9) ◽  
pp. 1747-1750
Author(s):  
R. Richard Plaskon ◽  
Gary L. Anderson

This study reports steady-state measurements of the fluorescence polarization of 1,6-diphenyl-1,3,5-hexatriene (DPH) within flight muscle mitochondrial membrane fragments from adult houseflies (Musca domestica) grown at 15 and 25 °C. Growth temperature of the houseflies is shown to have no effect on the polarization of DPH's fluorescence, whereas the temperature sensitivity of fluorescence polarization (Δ polarization) is 16% higher in flies grown at 25 °C than in those grown at 15 °C. Since the fluorescence polarization of DPH gives an indication of the degree of order within membranes, these results suggest that houseflies have the ability to alter the temperature dependence of their flight muscle mitochondrial membrane structure in response to a change in temperature. Little attention has been directed to the effects of growth temperature on Δ polarization values and this study suggests a procedure for detecting the existence of changes in this quantity.


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