NO message from muscle

Grozdanovic, Zarko

doi:10.1002/jemt.1165

Cited by 47 publications

(29 citation statements)

References 45 publications

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“…Following contraction, skeletal muscle fibers appear to release significant amounts of superoxide anion together with nitric oxide into the external medium (56,57,76,77). However, in skinned muscle fibers, exogenous H 2 O 2 stimulates contractions induced by caffeine but not by action potentials (78).…”

Section: Discussionmentioning

confidence: 99%

A Transverse Tubule NADPH Oxidase Activity Stimulates Calcium Release from Isolated Triads via Ryanodine Receptor Type 1 S -Glutathionylation

Hidalgo

Pecchi

Barrientos

et al. 2006

Journal of Biological Chemistry

171

147

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We report here the presence of an NADPH oxidase (NOX) activity both in intact and in isolated transverse tubules and in triads isolated from mammalian skeletal muscle, as established by immunochemical, enzymatic, and pharmacological criteria. Immunohistochemical determinations with NOX antibodies showed that the gp91 phox membrane subunit and the cytoplasmic regulatory p47 phox subunit co-localized in transverse tubules of adult mice fibers with the ␣ 1s subunit of dihydropyridine receptors. Western blot analysis revealed that isolated triads contained the integral membrane subunits gp91 phox and p22 phox , which were markedly enriched in isolated transverse tubules but absent from junctional sarcoplasmic reticulum vesicles. Isolated triads and transverse tubules, but not junctional sarcoplasmic reticulum, also contained varying amounts of the cytoplasmic NOX regulatory subunits p47 phox and p67 phox . NADPH or NADH elicited superoxide anion and hydrogen peroxide generation by isolated triads; both activities were inhibited by NOX inhibitors but not by rotenone. NADH diminished the total thiol content of triads by one-third; catalase or apocynin, a NOX inhibitor, prevented this effect. NADPH enhanced the activity of ryanodine receptor type 1 (RyR1) in triads, measured through [ 3 H]ryanodine binding and calcium release kinetics, and increased significantly RyR1 S-glutathionylation over basal levels. Preincubation with reducing agents or NOX inhibitors abolished the enhancement of RyR1 activity produced by NADPH and prevented NADPH-induced RyR1 S-glutathionylation. We propose that reactive oxygen species generated by the transverse tubule NOX activate via redox modification the neighboring RyR1 Ca 2؉ release channels. Possible implications of this putative mechanism for skeletal muscle function are discussed.The NADPH oxidases (NOX) 3 are flavoprotein enzymes that use NADPH as electron donor to mediate the univalent reduction of molecular oxygen to superoxide anion (1), a free radical that by spontaneous or enzymatically catalyzed dismutation is readily converted into H 2 O 2 . The phagocytic NOX isoform (NOX2) was first discovered as a pivotal component of the neutrophil respiratory burst (2, 3). The functional NOX2 enzyme is composed of two integral plasma membrane subunits, gp91 phox and p22phox , which make up cytochrome b 558 , plus three cytosolic regulatory subunits: p40 phox , p47 phox , and p67 phox (2, 4). A variety of tissues, including endothelial cells (5), smooth muscle cells (6), neurons (7-9), and astrocytes (7, 10), possess nonphagocytic NOX homologues (11,12). Several reports indicate that NOX2 and its homologues have a central role in the generation of reactive oxygen species (ROS) in response to diverse physiological extracellular stimuli (13-17). Moreover, membrane depolarization stimulates NOX activity in phagocytes (18) and endothelial cells (19,20). NOX stimulation is also apparent following agonist-induced stimulation of N-methyl-D-aspartate receptors in hippocampal neurons (21). Some N...

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Section: Discussionmentioning

confidence: 99%

A Transverse Tubule NADPH Oxidase Activity Stimulates Calcium Release from Isolated Triads via Ryanodine Receptor Type 1 S -Glutathionylation

Hidalgo

Pecchi

Barrientos

et al. 2006

Journal of Biological Chemistry

171

147

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“…The best-known effect of NO on skeletal muscle metabolism is its capacity to inhibit mitochondrial respiration directly by interfering with electron transport chain complexes in several ways; (1) NO inhibits cytochrome c oxidase activity by competing with O 2 , (2) NO inhibits electron transfer between cytochrome b and c (both belonging to Complex III) and increases mitochondrial production of O 2 N 2 , and (3) NO inhibits electron transfer and NADH-dehydrogenase function at the level of Complex I (Grozdanovic, 2001;Sarti et al, 2012a).…”

Section: Regulation Of Mitochondrial Electron Transport Chain Complexesmentioning

confidence: 99%

The role of nNOS and PGC-1α in skeletal muscle cells

Baldelli

Barbato

Tatulli

et al. 2014

Journal of Cell Science

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Neuronal nitric oxide synthase (nNOS) and peroxisome proliferator activated receptor c co-activator 1a (PGC-1a) are two fundamental factors involved in the regulation of skeletal muscle cell metabolism. nNOS exists as several alternatively spliced variants, each having a specific pattern of subcellular localisation. Nitric oxide (NO) functions as a second messenger in signal transduction pathways that lead to the expression of metabolic genes involved in oxidative metabolism, vasodilatation and skeletal muscle contraction. PGC1a is a transcriptional coactivator and represents a master regulator of mitochondrial biogenesis by promoting the transcription of mitochondrial genes. PGC-1a can be induced during physical exercise, and it plays a key role in coordinating the oxidation of intracellular fatty acids with mitochondrial remodelling. Several lines of evidence demonstrate that NO could act as a key regulator of PGC-1a expression; however, the link between nNOS and PGC-1a in skeletal muscle remains only poorly understood. In this Commentary, we review important metabolic pathways that are governed by nNOS and PGC-1a, and aim to highlight how they might intersect and cooperatively regulate skeletal muscle mitochondrial and lipid energetic metabolism and contraction.

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“…Much previous work has examined the possibility that ROS are mediators of contraction-induced damage to skeletal muscle (see Reznick et al 1998 (a) Roles of NO in skeletal muscle NO within, and released from, skeletal muscle cells has a number of general functions (Grozdanovic 2001). The functions of many cellular proteins are modified by NO, including soluble guanyl cyclase and mitochondrial respiratory chain complexes.…”

Section: Functions Of Ros In Skeletal Musclementioning

confidence: 99%

Reactive oxygen species and redox-regulation of skeletal muscle adaptations to exercise

Jackson

2005

Phil. Trans. R. Soc. B

110

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Skeletal muscle has been shown to generate a complex set of reactive oxygen and nitrogen species (ROS) both at rest and during contractile activity. The primary ROS generated are superoxide and nitric oxide and the pattern and magnitude of their generation is influenced by the nature of the contractile activity. It is increasingly clear that the ROS generated by skeletal muscle play an important role in influencing redox-regulated processes that control, at least some of, the adaptive responses to contractile activity. These processes are also recognized to be modified during ageing and in some disease states, providing the potential that interventions affecting ROS activity may influence muscle function or viability in these situations.

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NO message from muscle

Cited by 47 publications

References 45 publications

A Transverse Tubule NADPH Oxidase Activity Stimulates Calcium Release from Isolated Triads via Ryanodine Receptor Type 1 S -Glutathionylation

A Transverse Tubule NADPH Oxidase Activity Stimulates Calcium Release from Isolated Triads via Ryanodine Receptor Type 1 S -Glutathionylation

The role of nNOS and PGC-1α in skeletal muscle cells

Reactive oxygen species and redox-regulation of skeletal muscle adaptations to exercise

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