Purification and Characterization of Three Mitochondrial Substrate Carriers: the Phosphate, the 2-Oxoglutarate and the Dicarboxylate Carriers

  • F. Palmieri
  • G. Genchi
  • V. Zara
  • C. Indiveri
  • F. Bisaccia

Abstract

Since several substrates of the mitochondrial enzymes must be transported from the cytosol into the matrix and several products have to leave the mitochondria, the inner mitochondrial membrane has to be equipped with transport systems which catalyze metabolic flows between the inner and the outer compartment. The existence of at least 9 transport systems for metabolites has been documented in some detail by studies performed in intact mitochondria (LaNoue & Schoolwerth, 1979; Meijer & Van Dam, 1981; Palmieri et al, 1987). With the exception of the carrier for carnitine and acylcarnitine esters, the other carriers deal with the transport of anions: substrates of oxidative phosphorylation, ADP, ATP and phosphate, fuels of the tricarboxylic acid cycle, pyruvate, β-hydroxybutyrate and acetoacetate, dicarboxylates and tricarboxylates, and substrates of amino acid metabolism. This intense traffic of anions across the mitochondrial membrane is necessary, besides for oxidative phosphorylation, the tricarboxylic acid cycle and the amino acid metabolism, for the transfer of reducing equivalents in both directions and for important metabolic pathways, whose enzymes are partitioned between the cytosol and the mitochondria, such as gluconeogenesis, fatty acid synthesis, ketogenesis, β-oxidation of fatty acids and, in liver, urogenesis. Many of the properties of the proposed mitochondrial anion carriers, i.e. the high specificity, the existence of specific inhibitors, the saturation kinetics, the different distribution in various tissues and species and the inhibition by SH reagents have pointed to the protein nature of these transport systems. Their isolation, however, has been hindered for quite a long time.

Keywords

Lysine Cytosol Carnitine Benz Oxaloacetate 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1989

Authors and Affiliations

  • F. Palmieri
    • 1
    • 2
  • G. Genchi
    • 1
    • 2
  • V. Zara
    • 1
    • 2
  • C. Indiveri
    • 1
    • 2
  • F. Bisaccia
    • 1
    • 2
  1. 1.Department of Pharmaco-Biology, Laboratory of BiochemistryUniversity of BariItaly
  2. 2.CNR Unit for the Study of Mitochondria and BioenergeticsBariItaly

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