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Experiments have been performed to determine if fibroblasts from patients with Duchenne muscular dystrophy (DMD) are defective in a process of membrane repair. Normal and DMD fibroblasts were treated with phospholipase C from Clostridium perfringens to degrade plasma membrane phosphatidylcholine, and then phosphatidylcholine synthesis was measured as the incorporation of [3H]choline into lipid. Phosphatidylcholine synthesis was stimulated by phospholipase C treatment to a similar extent in normal and DMD fibroblasts. The activity of CTP: phosphocholine cytidylyltransferase, the enzyme regulating phosphatidylcholine synthesis in phospholipase C-treated mammalian cells, was also stimulated to the same extent in both cell types. The subcellular location of the cytidylyltransferase was changed by phospholipase C treatment from mostly cytosolic to mostly particulate in both normal and DMD fibroblasts. It appears, therefore, that at least one type of membrane repair system functions normally in DMD fibroblasts.
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Accepted: January 27, 1984
Received: October 27, 1983
☆This research was supported in part by a grant from the Muscular Dystrophy Association. E.M. was supported by a scholarship from the Minority Access to Research Careers Program, National Institutes of Health.
☆This is paper number 9661 from the Purdue Agricultural Experiment Station.
© 1984 Published by Elsevier Inc.