Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization.
We studied the distribution of dystrophin at the sarcolemma of normal human muscle fibers using high resolution immunofluorescence and confocal laser scanning optical microscopy (CLSOM). We found that the dystrophin lattice is organized at the muscle plasma membrane in an array of thick bands interconnected by a finer network. The bands encircle the muscle fiber perpendicular to the long axis of the fiber and they matched the sites of attachment of the sarcomeres to the plasma membrane. Dystrophin co-localized with vinculin, and dystrophin and vinculin co-localized with alpha-actinin at the region of the I-band. Dystrophin may be one of the proteins involved in the linkage of the sarcomeres to the extracellular matrix.
Minetti
C
C
Department of Neurology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.
Beltrame
F
F
Marcenaro
G
G
Bonilla
E
E
D000185:Actinin / Q000032:analysis; D000293:Adolescent; D000328:Adult; D002462:Cell Membrane / Q000737:chemistry; D016189:Dystrophin / Q000032:analysis*; D006801:Humans; D007834:Lasers; D008853:Microscopy / Q000379:methods; D008856:Microscopy, Fluorescence; D009132:Muscles / Q000737:chemistry*; D012016:Reference Values; D012518:Sarcomeres / Q000378:metabolism*; D016596:Vinculin / Q000032:analysis
D016189:Dystrophin; D000185:Actinin; D016596:Vinculin