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Compartmentalization of NO signaling cascade in skeletal muscles

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [1];  [1];  [1];  [2];  [3];  [4];  [5]
  1. Gerhard Domagk Institute of Pathology, University of Muenster, Muenster (Germany)
  2. Franz Volhard Clinic, Medical Faculty of the Charite, Humboldt University of Berlin, Berlin (Germany)
  3. Institute for Pharmacology and Toxicology, University of Muenster, Muenster (Germany)
  4. Institute for Pharmacology and Toxicology, Martin-Luther University Halle-Wittenberg, Halle/Saale (Germany)
  5. Institute of Anatomy, University of Leipzig, Leipzig (Germany)
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.
OSTI ID:
20709174
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 330; ISSN BBRCA9; ISSN 0006-291X
Country of Publication:
United States
Language:
English

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