Nitric oxide synthase (NOS) I during postnatal development in rat and mouse skeletal muscle

Christova, Tatjana; Grozdanovic, Zarko; Gossrau, Reinhart

doi:10.1016/s0065-1281(97)80025-6

Cited by 16 publications

(7 citation statements)

References 17 publications

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“…Stars Nerve fibers, arrows junctional sarcolemma, arrowheads extrajunctional sarcolemma. Bars 20 m ies of NOS I development in rat and mouse skeletal muscles, where low initial enzyme concentrations can be reliably detected by catalytic histochemistry but not by immunohistochemistry (Christova et al 1997). The positive findings obtained by the histochemical procedure may be due to an amplification of the residual NOS I activity.…”

Section: Discussionmentioning

confidence: 99%

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Grozdanovic

Gossrau

1997

Cell and Tissue Research

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Nitric oxide synthase I (NOS I) has been localized to the skeletal muscle sarcolemma in a variety of vertebrate species including man. It is particularly enriched at neuromuscular junctions. Recently, the N-methyl-D-aspartate (NMDA) receptor subunit 1 (NMDAR-1) has been detected in the postjunctional sarcolemma of rat diaphragm, providing a clue as to the possible source of Ca2+ ions that are necessary for NOS I activation. To address this possibility, we studied the distribution of NMDAR-1 and NOS I in mouse and rat skeletal muscles by immunohistochemistry and enzyme histochemistry. NMDAR-1 and NOS I were closely associated at neuromuscular junctions primarily of type II muscle fibers. NOS I was also present in the extrajunctional sarcolemma of this fiber type. Dystrophin, beta-dystroglycan, alpha-sarcoglycan, and spectrin were found normally expressed in both the junctional and extrajunctional sarcolemma of both fiber types. By contrast, in the muscle sarcolemma of MDX mice, dystrophin and dystrophin-associated proteins were reduced or absent. NOS I immunoreactivity was lost from the extrajunctional sarcolemma and barely detectable in the junctional sarcolemma. NOS I activity was clearly demonstrable in the junctional sarcolemma by NADPH diaphorase histochemistry, especially when the two-step method was used. NMDAR-1 was not altered. These data suggest that different mechanisms act to attach NOS I to the junctional versus extrajunctional sarcolemma. It may further be postulated that NMDA receptors are involved not only in the regulation but also sarcolemmal targeting of NOS I at neuromuscular junctions of type II fibers. The evidence that glutamate may function as a messenger molecule at vertebrate neuromuscular junction is discussed.

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Section: Discussionmentioning

confidence: 99%

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Grozdanovic

Gossrau

1997

Cell and Tissue Research

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“…nNOS has been detected in various skeletal muscles including human gastrocnemius, omohyoideus, quadriceps, sternocleidomastoideus, urethral sphincter and vastus lateralis muscle (42,72,89,98,144), rat and/or mouse diaphragm, deltoideus, extensor digitorum longus (EDL), gastrocnemius, levator labii, soleus, quadriceps and tibialis anterior muscle (28,35,42,44,47,53,62,91,111,118,122,193,199), and in the skeletal muscles in a variety of other species including gerbils, guinea pigs, hamsters, turtles, chicken, pigeons, and goldfish (80,85,88,90).…”

Section: Mature Skeletal Musclementioning

confidence: 99%

Physiology of Nitric Oxide in Skeletal Muscle

Stamler

Meissner

2001

Physiological Reviews

936

773

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In the past five years, skeletal muscle has emerged as a paradigm of "nitric oxide" (NO) function and redox-related signaling in biology. All major nitric oxide synthase (NOS) isoforms, including a muscle-specific splice variant of neuronal-type (n) NOS, are expressed in skeletal muscles of all mammals. Expression and localization of NOS isoforms are dependent on age and developmental stage, innervation and activity, history of exposure to cytokines and growth factors, and muscle fiber type and species. nNOS in particular may show a fast-twitch muscle predominance. Muscle NOS localization and activity are regulated by a number of protein-protein interactions and co- and/or posttranslational modifications. Subcellular compartmentalization of the NOSs enables distinct functions that are mediated by increases in cGMP and by S-nitrosylation of proteins such as the ryanodine receptor-calcium release channel. Skeletal muscle functions regulated by NO or related molecules include force production (excitation-contraction coupling), autoregulation of blood flow, myocyte differentiation, respiration, and glucose homeostasis. These studies provide new insights into fundamental aspects of muscle physiology, cell biology, ion channel physiology, calcium homeostasis, signal transduction, and the biochemistry of redox-related systems.

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“…NOS and NO have been associated with neuromuscular transmission and muscle contractility as well as with mitochondrial respiration and carbohydrate metabolism (Reid 1998;Grozdanovic and Baumgarten 1999). Recent studies of NOS and NO in skeletal muscle indicate that altered expression of NOS and production of NO may have manifold consequences for normal muscle development and function as well as for the pathophysiology of muscle fiber damage in neuromuscular diseases (Christova et al 1997;Wehling et al 2001;Anderson and Vargas 2003).…”

Section: Introductionmentioning

confidence: 99%

Involvement of CAPON and Nitric Oxide Synthases in Rat Muscle Regeneration After Peripheral Nerve Injury

et al. 2007

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Carboxy-terminal PDZ ligand of nNOS (CAPON) protein, as an adaptor, binds to nNOS via the PDZ domain helping regulate neuronal nitric oxide synthase (nNOS) activity at post-synaptic sites in neurons (Jaffrey et al., Neuron, 20, 115-124, 1998). Recently, it has been reported that CAPON is present in mouse muscle and may be involved in mouse muscle growth, injury, and repair possibly by regulating the stability, activity, or position of nNOS (Segalat et al., Experimental Cell Research, 302, 170-179, 2005). The present study was to explore the expression patterns and roles of CAPON as well as NOS in rat muscle regeneration after nerve injury. Normal Sprague-Dawley rats were subjected to right sciatic nerve crush injury. Walking track analysis, real time polymerase chain reaction, Western blotting, in situ hybridization, immunocytochemistry, and co-immunoprecipitation techniques were used. It revealed that CAPON mRNA increased, which peaked on days 1 and 28, whereas nNOS mRNA underwent a downregulation in the ipsilateral gastrocnemius muscles after sciatic nerve injury. Their proteins approximately paralleled the mRNA expression. CAPON and nNOS were identified in the activated satellite cells or myotubes and their in vivo interaction was verified. However, eNOS and iNOS proteins suffered an upregulation and were detected in activated satellite cells or myotubes. These data suggest that CAPON and all these three isoforms of NOS might be involved in muscle regeneration after nerve injury. Further study is necessary for a better understanding of the potential functional link between CAPON, NOS, and muscle regeneration, with possible application to therapy for skeletal muscle repair from nerve injury.

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Nitric oxide synthase (NOS) I during postnatal development in rat and mouse skeletal muscle

Cited by 16 publications

References 17 publications

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle

Physiology of Nitric Oxide in Skeletal Muscle

Involvement of CAPON and Nitric Oxide Synthases in Rat Muscle Regeneration After Peripheral Nerve Injury

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