β<sub>2</sub>-Agonist administration increases sarcoplasmic reticulum Ca<sup>2+</sup>-ATPase activity in aged rat skeletal muscle

Schertzer, Jonathan D.; Plant, David R.; Ryall, James G.; Beitzel, Felice; Stupka, Nicole; Lynch, Gordon S.

doi:10.1152/ajpendo.00399.2004

Cited by 42 publications

(40 citation statements)

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“…37 Total protein concentration of each sample was determined in triplicate by the method of Bradford. An equal amount of protein for each sample (50 mg) was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred electrophoretically to a polyvinylidene difluoride membrane and blocked for 1 h in phosphate-buffered saline (PBS) containing 10% non-fat milk.…”

Section: Elisa Sds-page and Western Blottingmentioning

confidence: 99%

“…In a separate group of animals, TA muscles were surgically excised, rinsed with PBS to remove excess blood and homogenized in PBS, as described previously. 37 Samples were centrifuged at 5000 g and the Non-viral IGF-I gene transfer enhances skeletal muscle regeneration JD Schertzer and GS Lynch supernatant fractions were assayed for IGF-I by ELISA according the manufacturer's instructions (Quantikine IGF-I immunoassay, MG100, R&D Systems, Minneapolis, MN, USA).…”

Section: Elisa Sds-page and Western Blottingmentioning

confidence: 99%

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Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury

Schertzer

Lynch

2006

Gene Ther

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Section: Elisa Sds-page and Western Blottingmentioning

confidence: 99%

Section: Elisa Sds-page and Western Blottingmentioning

confidence: 99%

Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury

Schertzer

Lynch

2006

Gene Ther

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“…The elevated resting [Ca 2 + ] i is caused by effects on mitochondrial enzymes and increased Ca 2 + extrusion (Gonzalez et al, 2003;Schertzer et al, 2005;Fraysse et al, 2006). These effects are consistent with age-associated reductions in SR Ca 2 + uptake (Schertzer et al, 2005) and SR Ca 2 + release (Wang et al, 2000). Unfortunately, very few studies have examined whether muscles in old humans also exhibit impaired muscle Ca 2 + regulation, but experiments using single muscle fibers found reduced SR Ca 2 + release due to uncoupling of the dihydropyridine receptor and SR ryanodine receptor in muscle fibers from older (65-75 years) compared with younger individuals (25-35 years) (Delbono et al, 1995).…”

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confidence: 59%

“…One of the contributing factors is that the loss of muscle mass in aging is preceded by a slowing in the maximal rate of relaxation of the twitch and tetanus (Ryall et al, 2004;Schertzer et al, 2005;Russ et al, 2011) and a reduction in both peak tetanic intracellular Ca 2 + concentration ([Ca 2 + ] i ) and maximal tetanic force (Gonzalez et al, 2003;Ryall et al, 2004;Schertzer et al, 2005;Russ et al, 2011). The reduced peak tetanic [Ca 2 + ] i is attributed to an elevated resting [Ca 2 + ] i , which is 25% and 74% higher in soleus and extensor digitorum longus (EDL) muscles from old (27-30 months) compared with young rats (4-6 months), respectively (Fraysse et al, 2006).…”

mentioning

confidence: 99%

“…It may also be attributed to compromised stress-induced activation of Ca 2 + sparks, which facilitate SR Ca 2 + release under conditions of membrane deformation in muscles from young healthy mice, but which are absent in muscles from aged mice (Weisleder et al, 2006). The elevated resting [Ca 2 + ] i is caused by effects on mitochondrial enzymes and increased Ca 2 + extrusion (Gonzalez et al, 2003;Schertzer et al, 2005;Fraysse et al, 2006). These effects are consistent with age-associated reductions in SR Ca 2 + uptake (Schertzer et al, 2005) and SR Ca 2 + release (Wang et al, 2000).…”

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Parvalbumin Gene Transfer Impairs Skeletal Muscle Contractility in Old Mice

et al. 2012

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Sarcopenia is the progressive age-related loss of skeletal muscle mass associated with functional impairments that reduce mobility and quality of life. Overt muscle wasting with sarcopenia is usually preceded by a slowing of the rate of relaxation and a reduction in maximum force production. Parvalbumin (PV) is a cytosolic Ca 2 + buffer thought to facilitate relaxation in muscle. We tested the hypothesis that restoration of PV levels in muscles of old mice would increase the magnitude and hasten relaxation of submaximal and maximal force responses. The tibialis anterior (TA) muscles of young (6 month), adult (13 month), and old (26 month) C57BL/6 mice received electroporation-assisted gene transfer of plasmid encoding PV or empty plasmid (pcDNA3.1). Contractile properties of TA muscles were assessed in situ 14 days after transfer. In old mice, muscles with increased PV expression had a 40% slower rate of tetanic force development ( p < 0.01), and maximum twitch and tetanic force were 22% and 16% lower than control values, respectively ( p < 0.05). Muscles with increased PV expression from old mice had an 18% lower maximum specific (normalized) force than controls, and absolute force was *26% lower at higher stimulation frequencies (150-300 Hz, p < 0.05). In contrast, there was no effect of increased PV expression on TA muscle contractile properties in young and adult mice. The impairments in skeletal muscle function in old mice argue against PV overexpression as a therapeutic strategy for ameliorating aspects of contractile dysfunction with sarcopenia and help clarify directions for therapeutic interventions for age-related changes in skeletal muscle structure and function.

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Oxidative stress‐induced dysregulation of excitation–contraction coupling contributes to muscle weakness

Qaisar

Bhaskaran

Premkumar

et al. 2018

J cachexia sarcopenia muscle

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BackgroundWe have previously shown that the deletion of the superoxide scavenger, CuZn superoxide dismutase, in mice (Sod1 −/− mice) results in increased oxidative stress and an accelerated loss of skeletal muscle mass and force that mirror the changes seen in old control mice. The goal of this study is to define the effect of oxidative stress and ageing on muscle weakness and the Excitation Contraction (EC) coupling machinery in age‐matched adult (8–10 months) wild‐type (WT) and Sod1 −/− mice in comparison with old (25–28 months) WT mice.Methods In vitro contractile assays were used to measure muscle contractile parameters. The activity of the sarcoplasmic reticulum Ca2+ ATPase (SERCA) pump was measured using an NADH‐linked enzyme assay. Immunoblotting and immunofluorescence techniques were used to measure protein expression, and real‐time reverse transcription PCR was used to measure gene expression.ResultsThe specific force generated by the extensor digitorum longus muscle was reduced in the Sod1 −/− and old WT mice compared with young WT mice along with significant prolongation of time to peak force, increased half relaxation time, and disruption of intracellular calcium handling. The maximal activity of the SERCA calcium uptake pump was significantly reduced in gastrocnemius muscle from both old WT (≈14%) and adult Sod1 −/− (≈33%) mice compared with young WT mice along with increased expression of sarcolipin, a known inhibitor of SERCA activity. Protein levels of the voltage sensor and calcium uptake channel proteins dihydropyridine receptor α1 and SERCA2 were significantly elevated (≈45% and ≈57%, respectively), while the ratio of calstabin, a channel stabilizing protein, to ryanodine receptor was significantly reduced (≈21%) in Sod1 −/− mice compared with young WT mice. The changes in calcium handling were accompanied by substantially elevated levels of global protein carbonylation and lipid peroxidation.ConclusionsOur data suggest that the muscle weakness in Sod1 −/− and old WT mice is in part driven by reactive oxygen species‐mediated EC uncoupling and supports a role for reduced SERCA pump activity in compromised muscle function. The novel quantitative mechanistic data provided here can lead to potential therapeutic interventions of SERCA dysfunction for sarcopenia and muscle diseases.

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β₂-Agonist administration increases sarcoplasmic reticulum Ca²⁺-ATPase activity in aged rat skeletal muscle

Cited by 42 publications

References 37 publications

Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury

Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury

Parvalbumin Gene Transfer Impairs Skeletal Muscle Contractility in Old Mice

Oxidative stress‐induced dysregulation of excitation–contraction coupling contributes to muscle weakness

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β2-Agonist administration increases sarcoplasmic reticulum Ca2+-ATPase activity in aged rat skeletal muscle

Cited by 42 publications

References 37 publications

Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury

Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury

Parvalbumin Gene Transfer Impairs Skeletal Muscle Contractility in Old Mice

Oxidative stress‐induced dysregulation of excitation–contraction coupling contributes to muscle weakness

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β₂-Agonist administration increases sarcoplasmic reticulum Ca²⁺-ATPase activity in aged rat skeletal muscle