Protein kinase activity in erythrocyte ghosts of patients with myotonic muscular dystrophy

Myotonic muscular dystrophy is a disorder of man that involves many organ systems. Physiological studies have suggested that the fundamental defect is of membrane origin. Heretofore, no reproducible metabolic abnormalities have been demonstrated. In the present studies erythrocyte ghosts are used as a convenient source of purified membranes that do not possess changes of denervation, dystrophy, and fibrosis that might complicate the interpretation of muscle membrane changes. The experiments demonstrated a significant difference in the phosphorylation of erythrocyte ghost protein by [γ ³²P]ATP, with endogenous protein kinase of erythrocyte membrane as the enzyme source. After ghosts were kept for 1 wk at -20° , phosphorylation of membrane protein in 8 controls was twice as high as endogenous protein kinase activity measured in fresh preparations. No stimulation was seen in prearations from 7 myotonic dystrophy patients from 3 different families. This reproducible difference in normal and myotonic membranes may represent an important new approach to studies of this debilitating inborn error of metabolism.