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XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

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Posters<br />

54.<br />

IDEBENONE ACTIvaTION OF GLYCEROL-3-PHOSPHATE OXIDATION IN<br />

LIVER MITOCHONDRIA frOM CONTROL AND HYPERTHYROID raTS<br />

Hana Rauchová 1,2 , Martina Vokurková 1,2 and Tomáš Soukup 1<br />

1<br />

Institute of Physiology, Academy of Sciences of the Czech Republic,<br />

2<br />

Centre for Cardiovascular Research, Prague, Czech Republic<br />

A synthetically prepared analog of coenzyme Q (CoQ) with lower hydrophobicity, idebenone<br />

(IDE; hydroxydecyl-ubiquinone), was found to be very effective in animal experiments and<br />

human replacement therapy when the synthesis of CoQ was decreased. In our previous<br />

studies, we found that mitochondrial FAD-linked glycerol-3-phosphate dehydrogenase<br />

(GPDH; EC 1.1.99.5) from brown adipose tissue is activated by IDE. However, in most<br />

mammalian tissues expression of GPDH is highly depressed and enzyme activity is very<br />

low. Thyroid hormones are known to have a marked influence on GPDH activity; they<br />

especially induce GPDH activity in liver. The aim of our study was to test to what extent<br />

IDE can activate glycerol phosphate (GP) oxidation measured as oxygen uptake and GP<br />

cytochrome c oxidoreductase activity in mitochondria from control and hyperthyroid rat<br />

liver. We found the significant increase of GP-dependent oxygen uptake as well as the<br />

activation of enzyme activity. Our results indicate that IDE may be used for the activation<br />

of the GP shuttle catalyzing the interconversion between dihydroxyaceton phosphate and<br />

GP (formed by GPDH together with its cytosolic NADH-dependent counterpart) through<br />

which NADH from cytosol can be oxidized by the mitochondrial respiratory chain to contribute<br />

to the maintenance of the high rate of glycolysis. It might be important in the case<br />

when mitochondrial Complex I is impaired and energy production must be maintained.<br />

Acknowledgement: This work was supported by the GACR (303/09/0570) and Ministry<br />

of Education, Youth and Sport (1M6798582302 and AV0Z 50110509).<br />

174 <strong>XXII</strong>. Biochemistry Congress, Martin

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