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.
Department of Experimental Pathology, UMDS, Guy's Hospital, London, UK.
M G
MG
Dunckley
K E
KE
Wells
T A
TA
Piper
D J
DJ
Wells
G
G
Dickson
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