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


Journal Article

Myotonic muscular dystrophy is a disorder of humans 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 we used erythrocyte ghosts 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. Our experiments demonstrated a significant difference in the phosphorylation of erythrocyte ghost protein by [gamma-(32)P]ATP, with endogenous protein kinase of erythrocyte membrane as the enzyme source. After ghosts were kept for 1 week at -20 degrees , phosphorylation of membrane protein in eight controls was twice as high as endogenous protein kinase activity measured in fresh preparations. No stimulation was seen in preparations from seven myotonic dystrophy patients from three 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.

Full Text

Cited Authors

  • Roses, AD; Appel, SH

Published Date

  • June 1, 1973

Published In

Volume / Issue

  • 70 / 6

Start / End Page

  • 1855 - 1859

PubMed ID

  • 4352659

Pubmed Central ID

  • 4352659

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.70.6.1855


  • eng