Biochemical abnormalities of erythrocyte membranes in Duchenne dystrophy. Adenosine triphosphatase and adenyl cyclase.
Adenosine triphosphatase (ATPase) activity in erythrocyte membranes from patients with Duchenne dystrophy was inhibited by ouabain less than in normal individuals in assay systems containing high or low contents of salt. Epinephrine and cyclic adenosine monophosphate increased total ATPase activity in all samples, and epinephrine restored ouabain sensitivity to the Duchenne membranes. Basal adenyl cyclase activity in about twice that of controls. Epinephrine stimulated adenyl cyclase activity of normal membranes two to three times, but did not stimulate the enzyme in Duchenne membranes. These differences may reflect a genetic abnormality of the membrane.
D000251:Adenosine Triphosphatases / Q000097:blood*; D000262:Adenylyl Cyclases / Q000097:blood*; D000328:Adult; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002648:Child; D000242:Cyclic AMP / Q000494:pharmacology; D004837:Epinephrine / Q000494:pharmacology; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D009136:Muscular Dystrophies / Q000097:blood / Q000201:enzymology*; D009994:Osmolar Concentration
D000242:Cyclic AMP; D000251:Adenosine Triphosphatases; D000262:Adenylyl Cyclases; D004837:Epinephrine