Hypothyroidism leads to a decreased expression of mitochondrial F0F1-ATP synthase in rat liver.
In liver mitochondria isolated from hypothyroid rats, the rate of ATP synthesis is lower than in mitochondria from normal rats. Oligomycin-sensitive ATP hydrolase activity and passive proton permeability were significantly lower in submitochondrial particles from hypothyroid rats compared to those isolated from normal rats. In mitochondria from hypothyroid rats, the changes in catalytic activities of F0F1-ATP synthase are accompanied by a decrease in the amount of immunodetected beta-F1, F0 1-PVP, and OSCP subunits of the complex. Northern blot hybridization shows a decrease in the relative cytosolic content of mRNA for beta-F1 subunit in liver of hypothyroid rats. Administration of 3,5,3'-triodo-L-thyronine to the hypothyroid rats tends to remedy the functional and structural defects of F0F1-ATP synthase observed in the hypothyroid rats. The results obtained indicate that hypothyroidism leads to a decreased expression of F0F1-ATP synthase complex in liver mitochondria and this contributes to the decrease of the efficiency of oxidative phosphorylation.
Guerrieri
F
F
Institute of Medical Biochemistry and Chemistry and Center for the Study of Mitochondria and Energy Metabolism (CNR), University of Bari, Italy.
Kalous
M
M
Adorisio
E
E
Turturro
N
N
Santoro
G
G
Drahota
Z
Z
Cantatore
P
P
D000818:Animals; D007037:Hypothyroidism / Q000201:enzymology*; D008297:Male; D008930:Mitochondria, Liver / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000096:biosynthesis*; D051381:Rats; D017208:Rats, Wistar
D006180:Proton-Translocating ATPases