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A more recent version of this article appeared on July 1, 2002
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Submitted on December 10, 2001
Revised on February 25, 2002
Accepted on April 12, 2002
1 Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201
2 Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030 (present address: Department of Cell and Structural Biology, University of Illinois, Urbana, IL 61801)
3 Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030
* Corresponding author. E-mail address: rbloch{at}umaryland.edu.
The sarcolemma of fast-twitch muscle is organized into "costameres", structures that are oriented transversely, over the Z and M lines of nearby myofibrils, and longitudinally, to form a rectilinear lattice. Here we examine the role of desmin, the major intermediate filament protein of muscle in organizing costameres. In control mouse muscle, desmin is enriched at the sarcolemmal domains that lie over nearby Z lines and that also contain ß-spectrin. In tibialis anterior muscle from mice lacking desmin due to homologous recombination, most costameres are lost. In myofibers from desmin -/- quadriceps, by contrast, many costameric structures are stable. Alternatively, Z line domains may be lost while domains oriented longitudinally or lying over M lines are retained. Experiments with pan-specific antibodies to intermediate filament proteins and to cytokeratins suggest that control and desmin -/- muscles express similar levels of cytokeratins. Cytokeratins concentrate at the sarcolemma at all three domains of costameres when the latter are retained in desmin -/- muscle and redistribute with ß-spectrin at the sarcolemma when costameres are lost. Our results suggest that desmin associates with and selectively stabilizes the Z line domains of costameres, but that cytokeratins associate with all three domains of costameres, even in the absence of desmin.
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