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Red Cell Glycolysis in the Myo dystrophic Child
Author(s) -
Bosia A.,
Pescarmona G. P.,
Abese P.
Publication year - 1971
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1971.tb00551.x
Subject(s) - glycolysis , pyruvate kinase , red cell , hexokinase , phosphofructokinase , biochemistry , dihydroxyacetone phosphate , adenine nucleotide , aldolase a , phosphoglycerate kinase , ouabain , inosine monophosphate , fructose , biology , incubation , intracellular , chemistry , nucleotide , metabolism , enzyme , sodium , medicine , organic chemistry , gene
. Assay of seven glycolytic enzymes, steady‐state levels of glycolytic metabolites, oxidized and reduced glutathione, inorganic phosphate, adenine nucleotides, sodium and potassium, and various incubation experiments were performed on red cells isolated from children with Duchenne‐Erb muscular dystrophy. The activity of hexokinase, aldolase, pyruvate kinase, and the levels of glucose‐6‐phosphate, ADP and intracellular inorganic phosphate were significantly increased. Long term incubation (15 h at 4° C) showed a phosphofructokinase activation; during shorter incubation (3 h at pH 7.6 and 38° C) similar behaviour of glycolytic metabolites, 2,3‐diphosphoglycerate and adenine nucleotides was observed in both normal and dystrophic red cells, while the lactate output was greater in the latter. The regulation of phosphoglycerate kinase and pyruvate kinase in vivo followed a normal pattern. Addition of ouabain to red cells incubated in a low‐potassium buffer was followed by increase of ATP in the normal and a decrease in the dystrophic red cell. Ouabain had no effect on glycolytic metabolites in the dystrophic cell, whereas sharp increases of fructose‐1,6‐diphosphate and dihydroxyacetone‐phosphate were observed in the normal cell.