Differences in the distribution of synemin, paranemin, and plectin in skeletal muscles of wild-type and desmin knock-out mice
2000 (English)In: Histochemistry and Cell Biology, ISSN 0948-6143, E-ISSN 1432-119X, Vol. 114, no 1, 39-47 p.Article in journal (Refereed) Published
Mice lacking the gene encoding for the intermediate filament protein desmin have a surprisingly normal myofibrillar organization in skeletal muscle fibers, although myopathy develops in highly used muscles. In the present study we examined how synemin, paranemin, and plectin, three key cytoskeletal proteins related to desmin, are organized in normal and desmin knock-out (K/O) mice. We show that in wild-type mice, synemin, paranemin, and plectin were colocalized with desmin in Z-disc-associated striations and at the sarcolemma. All three proteins were also present at the myotendinous junctions and in the postsynaptic area of motor endplates. In the desmin K/O mice the distribution of plectin was unaffected, whereas synemin and paranemin were partly affected. The Z-disc-associated striations were in general no longer present in between the myofibrils. In contrast, at the myotendinous and neuromuscular junctions synemin and paranemin were still present. Our study shows that plectin differs from synemin and paranemin in its binding properties to the myofibrillar Z-discs and that the cytoskeleton in junctional areas is particularly complex in its organization.
Place, publisher, year, edition, pages
Springer, 2000. Vol. 114, no 1, 39-47 p.
Cytoskeleton, Desmin knock-out mice, Intermediate filament-associated proteins, Myotendinous junctions, Neuromuscular junctions
Other Basic Medicine Cell and Molecular Biology
IdentifiersURN: urn:nbn:se:umu:diva-81914PubMedID: 10959821OAI: oai:DiVA.org:umu-81914DiVA: diva2:658817