Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats

Lowe, Dawn A.; Husom, Aimee D.; Ferrington, Deborah A.; Thompson, La Dora V.

doi:10.1016/j.mad.2004.07.002

Cited by 29 publications

(31 citation statements)

References 38 publications

(58 reference statements)

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“…The clearest difference was in Ca 2ϩ regulation: the decrease in Ca 2ϩ regulation of force and myofibrillar ATPase was much more pronounced in peroxidetreated (Figs. 3 and 5) than aged (42,44) muscle. EPR studies revealed the structural basis of this difference: the fraction of myosin heads in the strongly bound structural state in relaxed muscle significantly increased after H 2 O 2 treatment (Fig.…”

Section: Comparison Of Changes In Muscle Function Associated With In mentioning

confidence: 81%

Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers

Próchniewicz

Lowe

Spakowicz

et al. 2008

American Journal of Physiology-Cell Physiology

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109

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To understand the molecular mechanism of oxidation-induced inhibition of muscle contractility, we have studied the effects of hydrogen peroxide on permeabilized rabbit psoas muscle fibers, focusing on changes in myosin purified from these fibers. Oxidation by 5 mM peroxide decreased fiber contractility (isometric force and shortening velocity) without significant changes in the enzymatic activity of myofibrils and isolated myosin. The inhibitory effects were reversed by treating fibers with dithiothreitol. Oxidation by 50 mM peroxide had a more pronounced and irreversible inhibitory effect on fiber contractility and also affected enzymatic activity of myofibrils, myosin, and actomyosin. Peroxide treatment also affected regulation of contractility, resulting in fiber activation in the absence of calcium. Electron paramagnetic resonance of spin-labeled myosin in muscle fibers showed that oxidation increased the fraction of myosin heads in the strong-binding structural state under relaxing conditions (low calcium) but had no effect under activating conditions (high calcium). This change in the distribution of structural states of myosin provides a plausible explanation for the observed changes in both contractile and regulatory functions. Mass spectroscopy analysis showed that 50 mM but not 5 mM peroxide induced oxidative modifications in both isoforms of the essential light chains and in the heavy chain of myosin subfragment 1 by targeting multiple methionine residues. We conclude that 1) inhibition of muscle fiber contractility via oxidation of myosin occurs at high but not low concentrations of peroxide and 2) the inhibitory effects of oxidation suggest a critical and previously unknown role of methionines in myosin function.

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Section: Comparison Of Changes In Muscle Function Associated With In mentioning

confidence: 81%

Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers

Próchniewicz

Lowe

Spakowicz

et al. 2008

American Journal of Physiology-Cell Physiology

Self Cite

109

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“…This result indicates a decrease in the energetic efficiency, a partial uncoupling between ATPase activity and force generation, during contraction in aged muscle. In contrast, under unloaded shortening conditions (isotonic) in the same muscle, aging results in a decrease (16%) in the myofibrillar ATPase activity and a similar decrease in the shortening velocity (Lowe et al, 2004a). These findings (ATPase activity under isometric and isotonic conditions) suggest that the age-related inhibition of contractility may in part be due to changing actin-myosin interactions.…”

Section: Age and Myosin Atpase Activitymentioning

confidence: 84%

Age-related muscle dysfunction

Thompson

2009

Experimental Gerontology

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200

170

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Aging is associated with a progressive decline of muscle mass, strength, and quality, a condition described as sarcopenia of aging. Despite the significance of skeletal muscle atrophy, the mechanisms responsible for the deterioration of muscle performance are only partially understood. The purpose of this review is to highlight cellular, molecular and biochemical changes that contribute to age-related muscle weakness. Keywordsactin; myosin; aged muscle; enzymatic activity; oxidative modifications SarcopeniaAging is associated with a progressive decline of muscle mass, strength, and quality, a condition described as sarcopenia. These age-related changes are observed in healthy, active adults who are 50 years and older (Hughes et al., 2002). The prevalence of sarcopenia in older adults under the age of 70 years is about 25% and increases to 40% in adults 80 years or older (Baumgartner et al., 1998). Sarcopenia represents a risk factor for frailty, loss of independence, and physical disability (Roubenoff, 2000). Loss of mobility resulting from muscle loss predicts major physical disability and mortality, and is associated with poor quality of life, social needs, and health care needs (Fried and Guralnik, 1997). The economic impact of sarcopenia and its detrimental correlates are immense (Janssen et al., 2004). Thus, understanding the mechanisms leading to muscle dysfunction (e.g., weakness) at advanced age represents a high public health priority. The purpose of this article is to highlight cellular, molecular, and biochemical changes that contribute to age-related muscle dysfunction. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Muscle physiology-short reviewFor skeletal muscle, the control of force has to be accurate and precise with the contractile machinery being switched on and off rapidly to allow for complex coordinated movements. Action potentials initiated at the neuromuscular junction propagate along the length of the fiber and the transverse tubules. As the wave of depolarization passes down the transverse tubules there is an interaction with the sarcoplasmic reticulum that results in the release of calcium, initiating the interaction of actin and myosin and muscle contraction. This process is known as excitation-contraction coupling. Thus, age-related structural changes or chemical modifications in proteins that affect excitation-contraction coupling are likely to influence muscle function.The basic contractile unit of muscle, the myofibril, consists of a linear array of sarcomeres, which contains interdigitating myosin and actin fila...

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“…Skinned muscle fibers from old rodents show a reduction in specific muscle force, indicating a probable impairment in the muscle contractile machinery [41]. It has been shown that old muscle fibers show only a slight decrease in the actin-myosin filament ratio [42], however, the activity of myosin ATPase is substantially reduced [43]. Myosin but not actin oxidative modification levels are also increased in old muscles [22].…”

Section: Discussionmentioning

confidence: 99%

Sod1 gene ablation in adult mice leads to physiological changes at the neuromuscular junction similar to changes that occur in old wild-type mice

Ivannikov

Remmen

2015

Free Radical Biology and Medicine

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Reactive oxygen species (ROS) are believed to be important mediators of muscle atrophy and weakness in aging and many degenerative conditions. However, the mechanisms and physiological processes specifically affected by elevated ROS in neuromuscular units that contribute to muscle weakness during aging are not well defined. Here we investigate the effects of chronic oxidative stress on neurotransmission and excitation-contraction (EC) coupling mechanisms in the levator auris longus (LAL) muscle from young (4–8 months) and old (22–28 months) wild type mice and young adult Sod1−/− mice. The frequency of spontaneous neurotransmitter release and the amplitude of evoked neurotransmitter release in young Sod1−/− and old wild type LAL neuromuscular junctions were significantly reduced from the young wild type values, and those declines were mirrored by decreases in synaptic vesicle pool size. Presynaptic cytosolic calcium concentration and mitochondrial calcium uptake amplitudes showed substantial increases in stimulated young Sod1−/− and old axon terminals. Surprisingly, LAL muscle fibers from old mice showed a greater excitability than fibers from either young wild type or young Sod1−/− LAL muscle fibers. Both evoked excitatory junction potential (EJP) and spontaneous mini EJP amplitudes were considerably higher in LAL muscles from old mice than in fibers from young Sod1−/− LAL muscle. Despite a greater excitability, sarcoplasmic calcium influx in both old wild type and young Sod1−/− LAL muscle fibers was significantly smaller. Sarcoplasmic reticulum calcium levels were also smaller in both mice, but the difference was not statistically significant in muscle fibers from old wild type mice. The protein ratio of triad calcium channels – RyR1/DHPR was not different in all groups. However, fibers from both Sod1−/− and old mice had substantially elevated levels of protein carbonylation and S-nitrosylation modifications. Overall, our results suggest that young Sod1−/− recapitulate many neuromuscular and muscle fiber changes seen in old mice. We also conclude that muscle weakness in old mice might in part be driven by ROS mediated EC uncoupling, while both EC uncoupling and reduced neurotransmitter release contribute to muscle weakness in Sod1−/− mice.

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Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats

Cited by 29 publications

References 38 publications

Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers

Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers

Age-related muscle dysfunction

Sod1 gene ablation in adult mice leads to physiological changes at the neuromuscular junction similar to changes that occur in old wild-type mice

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