Structural and functional properties of mitochondrial anion carriers.
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Animals↗
Biomedical subjects
V Zara
Publications and source records attributed to V Zara.
Immunological characterization of the mitochondrial 2-oxoglutarate carrier from liver and heart. Organ specificity.
Antibodies have been prepared against the 2-oxoglutarate transport proteins purified from bovine heart and rat liver mitochondria. The anti-heart antiserum cross-reacts with the 2-oxoglutarate carrier (OGC) from beef, pig, rat and rabbit heart, but not with the OGC from liver of the same animals. Conversely, the anti-liver antiserum recognizes the carrier protein from liver of all species tested but not from heart. Immunoinactivation of oxoglutarate transport activity by the antibodies is also tissue specific. Peptide maps of purified OGC show structural differences between the carrier from heart and liver of the same animal species. These results indicate the existence of isoforms of the OGC in heart and liver.
Animals↗
Effect of anthracycline antibiotics on the reconstituted mitochondrial tricarboxylate carrier.
The effect of anthracycline antibiotics on the activity of the partially purified and reconstituted tricarboxylate carrier system of the rat liver mitochondria was studied. It was found that the citrate/citrate exchange activity is inhibited by Br-daunomycin and with less potency by doxorubicin, daunomycin, epirubicin and idarubicin. The inhibition of the citrate transport activity is concentration and time-dependent. Cardiolipin protects against the inhibition by Br-daunomycin and the reconstituted citrate transport activity depends upon the ratio of cardiolipin/Br-daunomycin.
Animals↗
Inhibition and labelling of the mitochondrial 2-oxoglutarate carrier by eosin-5-maleimide.
Unlike hydrophobic maleimides, eosin-5-maleimide and to a lesser extent other relatively polar maleimides inhibit the 2-oxoglutarate carrier of bovine heart mitochondria. The impermeable eosin-5-maleimide labels the 2-oxoglutarate carrier in intact mitochondria but not in submitochondrial particles. 2-Oxoglutarate protects the carrier against inactivation by eosin-5-maleimide and decreases the fluorescence associated with the purified protein. Other anions which are not substrates of the carrier have no protective effect. It is concluded that sulfhydryl groups essential for the activity of the 2-oxoglutarate carrier are located at the cytosolic face of the inner mitochondrial membrane. They appear to be present at the substrate-binding site and located in a hydrophilic environment.
Biological Transport↗
Inhibition of the mitochondrial tricarboxylate carrier by arginine-specific reagents.
The effect of arginine-specific reagents on the activity of the partially purified and reconstituted tricarboxylate carrier of the inner mitochondrial membrane has been studied. It has been found that 1,2-cyclohexanedione, 2,3-butanedione, phenylglyoxal and phenylglyoxal derivatives inhibit the reconstituted citrate/citrate exchange activity. The inhibitory potency of the phenylglyoxal derivatives increases with increasing hydrophilic character of the molecule. Citrate protects the tricarboxylate carrier against inactivation caused by the arginine-specific reagents. Other tricarboxylates, which are not substrates of the carrier, have no protective effect. The results indicate that at least one essential arginine residue is located at the substrate-binding site of the tricarboxylate carrier and that the vicinity of the essential arginine(s) has a hydrophilic character.
Animals↗