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Lookup NU author(s): Dr Michael Cullen
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The discovery of dystrophin and its definition as the causative molecule in Duchenne Muscular Dystrophy has led to a renewed interest in the molecular structure of the muscle fiber plasma membrane and its association with the extracellular basal lamina. The original identification of dystrophin gave credence to the possibility that the plasma membrane of the muscle fiber may be highly organized and involved in maintaining appropriate homeostasis in this actively contracting cellular system. In this review, we examine the currently known members of the muscle fiber plasma membrane cytoskeleton and the interactions that occur between the different members of this complex using histological, electron microscopic, and confocal methods. From our studies and others cited in this review, it is clear that the dystrophin cytoskeletal complex is not completely understood and component molecules continue to be discovered. Perhaps equally importantly, currently defined molecules (such as alpha-actinin or neuronal nitric oxide synthase) are being recognized as being specifically associated with the complex. What is striking from all of the studies, to date, is that while we are able to identify members of the dystrophin cytoskeletal complex and while we are able to associate mutations of individual molecules with disease(s), we are still unable to truly define the roles of each of the molecules in maintaining the normal physiology of the muscle fiber. (C) 2000 Willey-Liss, Inc.
Author(s): Watkins SC, Cullen MJ, Hoffman EP, Billington L
Publication type: Article
Publication status: Published
Journal: Microscopy Research and Technique
Year: 2000
Volume: 48
Issue: 3-4
Pages: 131-141
ISSN (print): 1059-910X
ISSN (electronic): 1097-0029
Publisher: John Wiley & Sons
URL: http://dx.doi.org/10.1002/(SICI)1097-0029(20000201/15)48:3/4<131::AID-JEMT2>3.0.CO;2-G
DOI: 10.1002/(SICI)1097-0029(20000201/15)48:3/4<131::AID-JEMT2>3.0.CO;2-G
PubMed id: 10679961
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