Caveolin-3 and nitric oxide synthase I in healthy and diseased skeletal muscle

Acta histochemica
R Gossrau

Abstract

Recently, it has been shown for mouse skeletal muscle that caveolin-3 is localized in the sarcolemma and cofractionates with the original dystrophin complex (DC). In order to find out whether caveolin-3 is a further component of the recently established and enlarged nitric oxide synthase (NOS) I-DC and whether members of this complex interact with and are potentially regulated by caveolin-3, mammalian and non-mammalian healthy and diseased (dystrophic) skeletal muscles were investigated using caveolin-3, NOS I, DC components and myosin immunohistochemistry as well as NOS I-associated diaphorase histochemistry. In healthy mammalian skeletal muscle, caveolin-3 was colocalized with the DC components in all extra- and intrafusal fibers. By contrast, NOS I was absent in type I extrafusal fibers of certain species. In patients with Duchenne muscular dystrophy and mdx mice the components of the NOS I-DC were not detected in all extra- and intrafusal fiber types, while caveolin-3 was found unchanged. In healthy non-mammalian skeletal muscle, i.e. of birds, reptiles and fishes, caveolin-3 immunoreactivity was lacking in the sarcolemma as was alpha-sarcoglycan; the other NOS I-DC components were either present or absent. In conclusion, a...Continue Reading

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Citations

Sep 12, 2001·Advanced Drug Delivery Reviews·J CouetM C Drolet
Oct 1, 2002·Meat Science·Robert G Brannan, Eric A Decker
Feb 26, 2000·Acta Physiologica Scandinavica·B C Kone
Mar 26, 2014·Journal of Anatomy·Kevin PeikertChristian Albrecht May
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Jan 12, 2001·Physiological Reviews·J S Stamler, G Meissner
Apr 22, 2018·Nitric Oxide : Biology and Chemistry·Oliver BaumAndreas Zakrzewicz

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