Reactive Nitrogen and Oxygen Species Metabolism in Rat Heart Mitochondria under Administration of Nitric Oxide Donor in Vivo

Author(s):  
Olga V. Akopova ◽  
Yulia P. Korkach ◽  
Anatolii V. Kotsuruba ◽  
Lyudmila I. Kolchinskaya ◽  
Vadim F. Sagach
2012 ◽  
Vol 58 (2) ◽  
pp. 3-15 ◽  
Author(s):  
OV Akopova ◽  
◽  
IuP Korkach ◽  
AV Kotsiuruba ◽  
LI Kolchyns'ka ◽  
...  

Amino Acids ◽  
2002 ◽  
Vol 22 (4) ◽  
pp. 381-389 ◽  
Author(s):  
S. Manzo-Ávalos ◽  
V. Pérez-Vázquez ◽  
J. Ramírez ◽  
L. Aguilera-Aguirre ◽  
J. C. González-Hernández ◽  
...  

2011 ◽  
Vol 169 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Alireza Imani ◽  
Mahdieh Faghihi ◽  
Sayyed Shahabeddin Sadr ◽  
Somayeh Sadeghi Niaraki ◽  
Ali Mohammad Alizadeh

1996 ◽  
Vol 328 (1) ◽  
pp. 85-92 ◽  
Author(s):  
Juan José Poderoso ◽  
Marı́a Cecilia Carreras ◽  
Constanza Lisdero ◽  
Natalia Riobó ◽  
Francisco Schöpfer ◽  
...  

1976 ◽  
Vol 158 (2) ◽  
pp. 289-294 ◽  
Author(s):  
D R Parr ◽  
E J Harris

1. Very low concentrations of Pb2+ decrease the capacity of rat heart mitochondria, oxidizing pyruvate plus malate, to remove Ca2+ from the medium. 2. The primary effect is on the rate of Ca2+ sequestration; this is reflected in the overall extent of Ca2+ removal. 3. Pb2+ has at least two separate actions. Below about 0.5 nmol/mg of protein, it acts solely by competing with Ca2+ (Ki = 0.4 muM); above this concentration it also inhibits the production or use of respiratory energy, so that at 1 nmol of Pb2+/mg of protein, Ca2+ removal is almost completely abolished. 4. Pb2+ inhibits coupled and uncoupled respiratory O2 use by mitochondria oxidizing pyruvate plus malate, but at higher concentrations than those that affect Ca2+ removal; similar concentrations of Pb2+ inhibit pyruvate uptake, but not malate uptake, by the mitochondria. 5. Mg2+ only decreases Ca2+ removal by competition, and is a far-less effective competitor than Pb2+ (Ki = 0.15 mM). It is possible that the primary cause of the second effect of Pb2+ is displacement of membrane Mg2+. 6. The consequences of these results are discussed in terms of the possible involvement of heart mitochondria in excitation-contraction coupling, and the Pb2+ levels that might occur in heart tissue in vivo.


2001 ◽  
Vol 280 (3) ◽  
pp. H977-H983 ◽  
Author(s):  
Ernest A. Boehm ◽  
Barney E. Jones ◽  
George K. Radda ◽  
Richard L. Veech ◽  
Kieran Clarke

The physiological role of mitochondrial uncoupling proteins (UCPs) in heart and skeletal muscle is unknown, as is whether mitochondrial uncoupling of oxidative phosphorylation by fatty acids occurs in vivo. In this study, we found that UCP2 and UCP3 protein content, determined using Western blotting, was increased by 32 and 48%, respectively, in hyperthyroid rat heart mitochondria. Oligomycin-insensitive respiration rate, a measure of mitochondrial uncoupling, was increased in all mitochondria in the presence of palmitate: 36% in controls and 71 and 100% with 0.8 and 0.9 mM palmitate, respectively, in hyperthyroid rat heart mitochondria. In the isolated working heart, 0.4 mM palmitate significantly lowered cardiac output by 36% and cardiac efficiency by 38% in the hyperthyroid rat heart. Thus increased mitochondrial UCPs in the hyperthyroid rat heart were associated with increased uncoupling and decreased myocardial efficiency in the presence of palmitate. In conclusion, a physiological effect of UCPs on fatty acid oxidation has been found in heart at the mitochondrial and whole organ level.


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