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Compartmentalization of NO signaling cascade in skeletal muscles.

Authors
  • Buchwalow, Igor B
  • Minin, Evgeny A
  • Samoilova, Vera E
  • Boecker, Werner
  • Wellner, Maren
  • Schmitz, Wilhelm
  • Neumann, Joachim
  • Punkt, Karla
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
May 06, 2005
Volume
330
Issue
2
Pages
615–621
Identifiers
PMID: 15796928
Source
Medline
License
Unknown

Abstract

Skeletal muscle functions regulated by NO are now firmly established. However, the literature on the compartmentalization of NO signaling in myocytes is highly controversial. To address this issue, we examined localization of enzymes engaged in L-arginine-NO-cGMP signaling in the rat quadriceps muscle. Employing immunocytochemical labeling complemented with tyramide signal amplification and electron microscopy, we found NO synthase expressed not only in the sarcolemma, but also along contractile fibers, in the sarcoplasmic reticulum and mitochondria. The expression pattern of NO synthase in myocytes showed striking parallels with the enzymes engaged in L-arginine-NO-cGMP signaling (arginase, phosphodiesterase, and soluble guanylyl cyclase). Our findings are indicative of an autocrine fashion of NO signaling in skeletal muscles at both cellular and subcellular levels, and challenge the notion that the NO generation is restricted to the sarcolemma.

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