inosinic-acid and Anemia--Hemolytic--Congenital

inosinic-acid has been researched along with Anemia--Hemolytic--Congenital* in 1 studies

Other Studies

1 other study(ies) available for inosinic-acid and Anemia--Hemolytic--Congenital

Article	Year
The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. Haematologica, 2006, Volume: 91, Issue:5 Erythrocyte membrane leakage of Ca2+ in familial phosphofructokinase deficiency results in a compensatory increase of Ca2+-ATPase activity that depletes ATP and leads to diminished erythrocyte deformability and a higher rate of hemolysis. Lowered ATP levels in circulating erythrocytes are accompanied by increased IMP, indicating that activated AMP deaminase plays a role in this metabolic dysregulation. Exposure to a calmodulin antagonist significantly slows IMP accumulation during experimental energy imbalance in patients' cells to levels that are similar to those in untreated controls, implying that Ca2+-calmodulin is involved in erythrocyte AMP deaminase activation in familial phosphofructokinase deficiency. Therapies directed against activated isoform E may be beneficial in this compensated anemia. Topics: Adenosine Triphosphate; AMP Deaminase; Anemia, Hemolytic, Congenital; Calcium; Calcium-Transporting ATPases; Calmodulin; Cell Membrane Permeability; Enzyme Activation; Erythrocyte Deformability; Erythrocytes; Glycogen Storage Disease Type VII; Glycolysis; Humans; Hypoxanthine; Inosine Monophosphate; Isoenzymes; Models, Biological; p-Methoxy-N-methylphenethylamine	2006

Article

Year

The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency.

Haematologica, 2006, Volume: 91, Issue:5

Erythrocyte membrane leakage of Ca2+ in familial phosphofructokinase deficiency results in a compensatory increase of Ca2+-ATPase activity that depletes ATP and leads to diminished erythrocyte deformability and a higher rate of hemolysis. Lowered ATP levels in circulating erythrocytes are accompanied by increased IMP, indicating that activated AMP deaminase plays a role in this metabolic dysregulation. Exposure to a calmodulin antagonist significantly slows IMP accumulation during experimental energy imbalance in patients' cells to levels that are similar to those in untreated controls, implying that Ca2+-calmodulin is involved in erythrocyte AMP deaminase activation in familial phosphofructokinase deficiency. Therapies directed against activated isoform E may be beneficial in this compensated anemia.

Topics: Adenosine Triphosphate; AMP Deaminase; Anemia, Hemolytic, Congenital; Calcium; Calcium-Transporting ATPases; Calmodulin; Cell Membrane Permeability; Enzyme Activation; Erythrocyte Deformability; Erythrocytes; Glycogen Storage Disease Type VII; Glycolysis; Humans; Hypoxanthine; Inosine Monophosphate; Isoenzymes; Models, Biological; p-Methoxy-N-methylphenethylamine

2006