The effect of amino acids, monoamines and polyamines on pyruvate dehydrogenase activity in mitochondria from rat adipocytes

  title={The effect of amino acids, monoamines and polyamines on pyruvate dehydrogenase activity in mitochondria from rat adipocytes},
  author={Frederick L. Kiechle and Halina Malinski and Diane M. Dandurand and Janet B. McGill},
  journal={Molecular and Cellular Biochemistry},
SummaryThe ability of polyamines and other cationic compounds including monoamines, amino acids, poly-L-arginine, poly-D-lysine and poly-L-lysine, to alter pyruvate dehydrogenase (PDH) activity in mitochondria from rat epididymal adipocytes was determined. PDH was assayed with the substrate [1-14C] pyruvate in the presence of 0.05 mM Ca2+ and Mg2+. Nine of the fourteen compounds tested at 0.1 mM caused a significant increase (procaine, 3-(β-morpholinopropionyl) benzo[b]thiophene [VII], spermine… 
Ca2+-independent effects of spermine on pyruvate dehydrogenase complex activity in energized rat liver mitochondria incubated in the absence of exogenous Ca2+ and Mg2+
These results provide the first evidence that, when transported in RLM, spermine can interact in various ways with PDC, showing dose-dependent behaviour.
Lactic acidosis and mitochondrial dysfunction in two children with peroxisomal disorders
These two patients with generalized peroxisomal disorders exhibited an increase in intracellular acyl-CoA species accompanied by decreased PDH activity and clinical lactic/pyruvic acidaemia, which is known to alter mitochondrial function.


Actions of polyamines on lipid and glucose metabolism of fat cells.
Sensitivity of pyruvate dehydrogenase phosphate phosphatase to magnesium ions. Similar effects of spermine and insulin.
It is concluded that insulin is more likely to alter the interaction of the pyruvate dehydrogenase system with some other polybasic intramitochondrial component whose action can be mimicked by spermine.
Polyamine stimulation of protein phosphatase-2A from rat liver using a non-protein phosphoester substrate.
Kinetic analysis indicated that the activation of phosphatase by polyamines was accomplished by an increase in Vmax of the enzyme, by a mechanism independent of that achieved by other cations.
Polyamines stimulate the phosphorylation of phosphatidylinositol in membranes from A431 cells.
The results do not suggest an involvement of the EGF receptor in the growth-factor-dependent formation of phosphatidylinositol phosphates, and it is proposed that the phosphorylation of phosphate by polyamines might be a mechanism to replenish the pool of inositolphospholipids.
Glycerolipid biosynthesis in rat adipose tissue. IX. Activation of diglyceride acyltransferase by spermine.
The results suggest that the activation of DGAT by spermine may reside in its ability to preserve the membrane integrity of microsomal membranes, to maintain the optimal and noninhibitory levels of palmitoyl-CoA and to provide a cationic environment required for the optimal activity of this enzyme.
Role of membranes and energy-producing reactions in cellular processing of insulin in primary cultures of rat hepatocytes.
Polyamines in rat adipocytes: Their localization and their effects on the insulin receptor binding