Independent localization of dystrophin N- and C-terminal regions to the sarcolemma of mdx mouse myofibres in vivo.
Dystrophin has been proposed to associate with the skeletal muscle membrane by way of a glycoprotein complex that interacts with its C-terminal domains. Transfection of mdx mouse myotubes in culture or myofibres in vivo with recombinant genes encoding human dystrophin deletion mutants shows, however, that not only the C terminus of dystrophin but also its N-terminal actin-binding domain can locate independently to the muscle sarcolemma. This observation suggests that lack of sarcolemma-associated dystrophin in Duchenne muscular dystrophy (DMD) muscle may result from enhanced degradation of truncated mutation products rather than their inability per se to associate with the sarcolemma.
Dunckley
M G
MG
Department of Experimental Pathology, UMDS, Guy's Hospital, London, UK.
Wells
K E
KE
Piper
T A
TA
Wells
D J
DJ
Dickson
G
G
D000818:Animals; D001692:Biological Transport; D002460:Cell Line; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D018076:DNA, Complementary / Q000235:genetics; D016189:Dystrophin / Q000235:genetics / Q000378:metabolism*; D005347:Fibroblasts; D005455:Fluorescent Antibody Technique; D006801:Humans; D051379:Mice; D018101:Mice, Inbred mdx / Q000378:metabolism*; D018485:Muscle Fibers, Skeletal / Q000378:metabolism* / Q000473:pathology; D009136:Muscular Dystrophies / Q000378:metabolism; D009137:Muscular Dystrophy, Animal / Q000378:metabolism* / Q000473:pathology; D011994:Recombinant Proteins / Q000378:metabolism; D012508:Sarcolemma / Q000378:metabolism*
D018076:DNA, Complementary; D016189:Dystrophin; D011994:Recombinant Proteins