The influence of chronic ethanol feeding to rats on liver mitochondrial membrane structure and function

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.

2001 ◽  
Vol 29 (4) ◽  
pp. 436-441 ◽  
Author(s):  
D. Forsha ◽  
C. Church ◽  
P. Wazny ◽  
R. O. Poyton

The assembly of cytochrome c oxidase in the inner mitochondrial membranes of eukaryotic cells requires the protein products of a large number of nuclear genes. In yeast, some of these act globally and affect the assembly of several respiratory-chain protein complexes, whereas others act in a cytochrome c oxidase-specific fashion. Many of these yeast proteins have human counterparts, which when mutated lead to energy-related diseases. One of these proteins, Pet100p, is a novel molecular chaperone that functions to incorporate a subcomplex containing cytochrome c oxidase subunits VII, VIIa and VIII into holo-(cytochrome c oxidase). Here we report the topological disposition of Pet100p in the inner mitochondrial membrane and show that its C-terminal domain is essential for its function as a cytochrome c oxidase-specific ‘assembly facilitator’.


Science ◽  
1975 ◽  
Vol 188 (4185) ◽  
pp. 282-282
Author(s):  
A. D. Keith ◽  
D. Deamer ◽  
J. K. Raison

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