Abnormal protein metabolism in skin fibroblasts in vitro from patients with Duchenne muscular dystrophy.
Rates of protein turnover have been measured on a statistical basis in Duchenne muscular dystrophy and normal skin fibroblasts populations in vitro. At comparable numbers of cumulative population doublings, protein synthesis was significantly reduced by about 24% in DMD fibroblasts as compared to normal fibroblasts (p less than 0.01, N = 12). Degradation of short lived proteins was significantly enhanced by about 60% (p less than 0.05, N = 18), and the degradation of long lived proteins was significantly increased by about 28% (p less than 0.05, N = 18) in DMD fibroblast populations in vitro. The enhanced degradation of long lived proteins in DMD fibroblasts can be reduced to basal levels of degradation by the use of the protease inhibitors leupeptin and Ep475 (p less than 0.05, N = 9).
D000293:Adolescent; D002478:Cells, Cultured; D002648:Child; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D007930:Leucine / Q000378:metabolism; D008297:Male; D009136:Muscular Dystrophies / Q000378:metabolism*; D014176:Protein Biosynthesis; D011506:Proteins / Q000378:metabolism*; D012016:Reference Values; D012867:Skin / Q000378:metabolism*; D014316:Tritium
D011506:Proteins; D014316:Tritium; D007930:Leucine