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Alterations of Membrane Phosphorylation in Erythrocyte Membranes from Patients with Duchenne Muscular Dystrophy

Published online by Cambridge University Press:  18 September 2015

J.D. Vickers*
Affiliation:
MRC Group in Developmental Neurobiology, Department of Neurosciences, McMaster University Medical Centre, Hamilton, Ontario, Canada
A.J. McComas
Affiliation:
MRC Group in Developmental Neurobiology, Department of Neurosciences, McMaster University Medical Centre, Hamilton, Ontario, Canada
M.P. Rathbone
Affiliation:
MRC Group in Developmental Neurobiology, Department of Neurosciences, McMaster University Medical Centre, Hamilton, Ontario, Canada
*
McMaster University, Dept. of Neuroscience, 1200 Main St. W., Hamilton, Ontario, Canada L8S 4J9
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The phosphorylation of spectrin, hand 3 protein, and the phospholipids of erythrocyte membranes (ghosts) was examined in 10 patients with Duchenne muscular dystrophy (DMD) and in healthy age- and sex-matched controls. The rales of phosphorylation of spectrin and band 3 protein were significantly higher in ghosts prepared from patient blood than from control blood at both 30° C and 37° C. However, the mean increases in the rate of phosphorylation of both spectrin and band 3 protein in response to a temperature change from 30° C to 37° C were identical in gliosis from patient and controls. Phosphorylation of phospholipid and its temperature response did not differ between patients and controls. These results complement previous observations of differences in erythrocytes from patients with DMD. The similarity of the changes in phosphorylation of both spectrin and band 3 protein indicates a common cause, possibly their lipid environment.

Type
Research Article
Copyright
Copyright © Canadian Neurological Sciences Federation 1978

References

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