Effects of nitric oxide on force-generating proteins of skeletal muscle

Galler, Stefan; Hilber, Karlheinz; Göbesberger, Alfred

doi:10.1007/s004240050391

Cited by 54 publications

(56 citation statements)

References 19 publications

(30 reference statements)

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“…Nitric oxide (NO) is known to decrease shortening velocities in both vertebrate skeletal and cardiac muscle fibres (Galler et al, 1997;Perkins et al, 1997). Recently, Evangelista et al demonstrated that NO acts directly on skeletal and alpha-cardiac myosin heavy chains by S-nitrosylating cysteine residues in the myosin heavy chain, resulting in slowed actin velocity in an in vitro motility assay and increased myosin force production in a laser trap (Evangelista et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Muscular tissues of the squid Doryteuthis pealeii express identical myosin heavy chain isoforms: an alternative mechanism for tuning contractile speed

Shaffer

Kier

2012

Journal of Experimental Biology

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SUMMARYThe speed of muscle contraction is largely controlled at the sarcomere level by the ATPase activity of the motor protein myosin. Differences in amino acid sequence in catalytically important regions of myosin yield different myosin isoforms with varying ATPase activities and resulting differences in cross-bridge cycling rates and interfilamentary sliding velocities. Modulation of whole-muscle performance by changes in myosin isoform ATPase activity is regarded as a universal mechanism to tune contractile properties, especially in vertebrate muscles. Invertebrates such as squid, however, may exhibit an alternative mechanism to tune contractile properties that is based on differences in muscle ultrastructure, including variable myofilament and sarcomere lengths. To determine definitively whether contractile properties of squid muscles are regulated via different myosin isoforms (i.e. different ATPase activities), the nucleotide and amino acid sequences of the myosin heavy chain from the squid Doryteuthis pealeii were determined from the mantle, arm, tentacle, fin and funnel retractor musculature. We identified three myosin heavy chain isoforms in squid muscular tissues, with differences arising at surface loop 1 and the carboxy terminus. All three isoforms were detected in all five tissues studied. These results suggest that the muscular tissues of D. pealeii express identical myosin isoforms, and it is likely that differences in muscle ultrastructure, not myosin ATPase activity, represent the most important mechanism for tuning contractile speeds. Supplementary material available online at

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Section: Discussionmentioning

confidence: 99%

Muscular tissues of the squid Doryteuthis pealeii express identical myosin heavy chain isoforms: an alternative mechanism for tuning contractile speed

Shaffer

Kier

2012

Journal of Experimental Biology

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“…It was suggested that the decreased ATP turnover occurring after nitrate supplementation might be related to a reduced ATP requirement for actin-myosin cross-bridge cycling and/or calcium handling, given previous reports that NO slows actin-myosin cross-bridge cycling [59,60] and inhibits calcium-ATPase activity [61,62]. Interestingly, a recent murine model investigation reported greater force production, and increased expression of the calcium handling protein calsoquestrin 1 and the dihydropyridine receptor in type II muscle fibres following nitrate supplementation [9].…”

Section: Effect Of Nitrate Supplementation On Cardiorespiratory Variamentioning

confidence: 99%

Dietary nitrate supplementation enhances high-intensity running performance in moderate normobaric hypoxia, independent of aerobic fitness

et al. 2016

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Nitrate-rich beetroot juice (BRJ) increases plasma nitrite concentration, lowers the oxygen cost (V O2) of steady-state exercise and improves exercise performance in sedentary and moderately-trained, but rarely in well-trained individuals exercising at sea-level. BRJ supplementation may be more effective in a hypoxic environment, where the reduction of nitrite into nitric oxide (NO) is potentiated, such that well-trained and less well-trained individuals may derive a similar ergogenic effect.We conducted a randomised, counterbalanced, double-blind placebo controlled trial to determine the effects of BRJ on treadmill running performance in moderate normobaric hypoxia (equivalent to 2500 m altitude) in participants with a range of aerobic fitness levels. Twelve healthy males (V O2max ranging from 47.1 -76.8 ml·kg -1 ·min -1 ) ingested 138 ml concentrated BRJ (~ 15.2 mmol nitrate) or a nitrate-deplete placebo (PLA) (~ 0.2 mmol nitrate). Three hours later, participants completed steady-state moderate intensity running, and a 1500 m time-trial (TT) in a normobaric hypoxic chamber (FIO2 ~15 %). Plasma nitrite concentration was significantly greater following BRJ versus PLA 1 hour post supplementation, and remained higher in BRJ throughout the testing session (p < 0.01). Average V O2 was significantly lower (BRJ: 18.4 ± 2.0, PLA: 20.4 ± 12.6 ml·kg -1 ·min -1 ; p = 0.002), whilst arterial oxygen saturation (SaO2) was significantly greater (BRJ: 88.4 ± 2.7, PLA: 86.5 ± 3.3 %; p < 0.001) following BRJ. BRJ improved TT performance in all 12 participants by an average of 3.2 % (BRJ: 331.1 ± 45.3 vs. PL: 341.9 ± 46.1 s; p < 0.001). There was no apparent relationship between aerobic fitness and the improvement in performance following BRJ (r 2 = 0.05, p > 0.05). These findings suggests that a high nitrate dose in the form of a BRJ supplement may improve running performance in individuals with a range of aerobic fitness levels conducting moderate and high-intensity exercise in a normobaric hypoxic environment.

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“…Galler et al (21) showed NO-depressed muscle contrac-tion in regard to both mechanical properties and myofibrillar ATPase activity using the skinned fibers method. Aghdashi et al (22) hypothesized that oxidants and NO interact directly with Ca 2ϩ release channel (ryanodine receptor 1) in the Tsystem.…”

mentioning

confidence: 99%

α1-Syntrophin Gene Disruption Results in the Absence of Neuronal-type Nitric-oxide Synthase at the Sarcolemma but Does Not Induce Muscle Degeneration

Kameya

Miyagoe

Nonaka

et al. 1999

Journal of Biological Chemistry

165

164

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␣1-Syntrophin is a member of the family of dystrophin-associated proteins and is strongly expressed in the sarcolemma and the neuromuscular junctions. All three syntrophin isoforms have a PDZ domain that appears to participate in protein-protein interactions at the plasma membrane. ␣1-Syntrophin has additionally been shown to associate with neuronal nitric-oxide synthase (nNOS) through PDZ domains in vitro. These observations suggest that ␣1-syntrophin may work as a modular adaptor protein that can link nNOS or other signaling enzyme to the sarcolemmal dystrophin complex. In the sarcolemma, nNOS regulates the homeostasis of reactive free radical species and may contribute to the oxidative damage to muscle protein in muscle disease such as Duchenne muscular dystrophy. In this study, we generated ␣1-syntrophin knock-out mice to clarify the interaction between ␣1-syntrophin and nNOS in the skeletal muscle. We observed that nNOS, normally expressed in the sarcolemma, was largely absent from the sarcolemma, but considerably remained in the cytosol of the knock-out mice. Even though the distribution of nNOS was altered, the knock-out mice displayed no gross histological changes in the skeletal muscle. We also discovered that muscle contractile properties have not been influenced in the knock-out mice.

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Effects of nitric oxide on force-generating proteins of skeletal muscle

Cited by 54 publications

References 19 publications

Muscular tissues of the squid Doryteuthis pealeii express identical myosin heavy chain isoforms: an alternative mechanism for tuning contractile speed

Muscular tissues of the squid Doryteuthis pealeii express identical myosin heavy chain isoforms: an alternative mechanism for tuning contractile speed

Dietary nitrate supplementation enhances high-intensity running performance in moderate normobaric hypoxia, independent of aerobic fitness

α1-Syntrophin Gene Disruption Results in the Absence of Neuronal-type Nitric-oxide Synthase at the Sarcolemma but Does Not Induce Muscle Degeneration

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