A functional membrane repair system in Duchenne muscular dystrophy fibroblasts.
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.
D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002478:Cells, Cultured; D002794:Choline / Q000378:metabolism; D019916:Choline-Phosphate Cytidylyltransferase; D003600:Cytosol / Q000201:enzymology; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D009136:Muscular Dystrophies / Q000201:enzymology*; D009713:Nucleotidyltransferases / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism*; D010738:Type C Phospholipases / Q000494:pharmacology
D010713:Phosphatidylcholines; D009713:Nucleotidyltransferases; D019916:Choline-Phosphate Cytidylyltransferase; D010738:Type C Phospholipases; D002794:Choline