Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms

Talmadge, Robert J.; Roy, Roland R.

doi:10.1152/jappl.1993.75.5.2337

Cited by 744 publications

(595 citation statements)

References 32 publications

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“…Upon aging, the composition of the myosin heavy chain (MHC) isoforms, which are specific for muscle fibre types (Talmadge & Roy, 1993), showed a slight shift from glycolytic (type IIb) fibres to mixed oxidative glycolytic (type IIa and IIx) fibres in the quadriceps of the LF control group (Fig. S1).…”

Section: Resultsmentioning

confidence: 99%

Running‐wheel activity delays mitochondrial respiratory flux decline in aging mouse muscle via a post‐transcriptional mechanism

et al. 2017

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SummaryLoss of mitochondrial respiratory flux is a hallmark of skeletal muscle aging, contributing to a progressive decline of muscle strength. Endurance exercise alleviates the decrease in respiratory flux, both in humans and in rodents. Here, we dissect the underlying mechanism of mitochondrial flux decline by integrated analysis of the molecular network.Mice were given a lifelong ad libitum low‐fat or high‐fat sucrose diet and were further divided into sedentary and running‐wheel groups. At 6, 12, 18 and 24 months, muscle weight, triglyceride content and mitochondrial respiratory flux were analysed. Subsequently, transcriptome was measured by RNA‐Seq and proteome by targeted LC‐MS/MS analysis with 13C‐labelled standards. In the sedentary groups, mitochondrial respiratory flux declined with age. Voluntary running protected the mitochondrial respiratory flux until 18 months of age. Beyond this time point, all groups converged. Regulation Analysis of flux, proteome and transcriptome showed that the decline of flux was equally regulated at the proteomic and at the metabolic level, while regulation at the transcriptional level was marginal. Proteomic regulation was most prominent at the beginning and at the end of the pathway, namely at the pyruvate dehydrogenase complex and at the synthesis and transport of ATP. Further proteomic regulation was scattered across the entire pathway, revealing an effective multisite regulation. Finally, reactions regulated at the protein level were highly overlapping between the four experimental groups, suggesting a common, post‐transcriptional mechanism of muscle aging.

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Section: Resultsmentioning

confidence: 99%

Running‐wheel activity delays mitochondrial respiratory flux decline in aging mouse muscle via a post‐transcriptional mechanism

et al. 2017

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“…The protocol for analyzing the specimens was based on Talmadge and Roy (1993) and Mizunoya et al (2008) with modifications for single-fiber analyses (Staron, 1991). Eight histological sections (12 lm thick) were collected from each whole muscle sample and placed in a solution (0.5 mL) containing glycerol 10% (w/vol), 2-mercaptoethanol 5% (vol/vol), and sodium dodecylsulfate (SDS) 2.3% (w/ vol) in a Tris/HCl buffer 0.9% (pH 6.8; w/vol).…”

Section: Sds-pagementioning

confidence: 99%

High‐Intensity Resistance Training with Insufficient Recovery Time Between Bouts Induce Atrophy and Alterations in Myosin Heavy Chain Content in Rat Skeletal Muscle

Souza

Aguiar

Carani

et al. 2011

The Anatomical Record

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The aim of this study was to test whether high-intensity resistance training with insufficient recovery time between bouts, could result in a decrease of muscle fiber cross-sectional area (CSA), alter fiber-type frequencies and myosin heavy chain (MHC) isoform content in rat skeletal muscle. Wistar rats were divided into two groups: trained (Tr) and control (Co). Tr group were subjected to a high-intensity resistance training program (5 days/week) for 12 weeks, involving jump bouts into water, carrying progressive overloads based on percentage body weight. At the end of experiment, animals were sacrificed, superficial white (SW) and deep red (DR) portions of the plantaris muscle were removed and submitted to mATPase histochemical reaction and SDS-PAGE analysis. Throughout the experiment, both groups increased body weight, but Tr was lower than Co. There was a significant reduction in IIA and IID muscle fiber CSA in the DR portion of Tr compared to Co. Muscle fiber-type frequencies showed a reduction in Types I and IIA in the DR portion and IID in the SW portion of Tr compared to Co; there was an increase in Types IIBD frequency in the DR portion. Change in muscle fiber-type frequency was supported by a significant decrease in MHCI and MHCIIa isoforms accompanied by a significant increase in MHCIIb isoform content. MHCIId showed no significant differences between groups. These data show that high-intensity resistance training with insufficient recovery time between bouts promoted muscle atrophy and a transition from slow-to-fast contractile activity in rat plantaris muscle. Anat Rec, 294:1393Rec, 294: -1400Rec, 294: , 2011. V V C 2011 Wiley-Liss, Inc.

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“…Talmadge and Roy (1993) previously described a quantitative sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) protocol that clearly separates all four isoforms of MyHC (I, IIa, IIx and IIb) found in adult rat skeletal muscle using a Mini-Gel system. MyHC I isoform from the rat soleus muscle, and IIa, IIx and IIb isoforms from the extensor digitorum longus muscle were used.…”

Section: Myhc Isoform Electrophoresismentioning

confidence: 99%

“…Stacking and separating gel Preparation of separating gels and running buffers was performed as described previously by Talmadge and Roy (1993). The separating gel contained 30% glycerol, 8% acrylamide, 200 mM Tris-HCl (pH 5 8.8), 100 mM glycine and 0.4% SDS; the stacking gel contained 30% glycerol, 4% acrylamide, 70 mM Tris-HCl (pH 5 6.8), 4 mM EDTA and SDS.…”

Section: Myhc Isoform Electrophoresismentioning

confidence: 99%

Myosin heavy chain pattern in the Akhal-Teke horses

Leisson

Alev

Kaasik

et al. 2011

Animal

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This study investigates the myosin heavy chain (MyHC) isoform composition in the gluteus medius muscle of the Akhal-Teke horses using SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis). Fifteen horses aged between 1.5 and 23.5 years were used in this study and divided into three age groups: 1.5 to 4 (n= 6), 9 to 13 (n= 5) and 18.5 to 23.5 years (n= 4). The average content of the MyHC I isoform was 11.72 ± 1.07% (variation between individuals: 7.09% to 20.14%). The relative content of the MyHC IIa and IIx isoforms was subsequently 38.20 ± 1.46% (30.73% to 48.78%) and 50.07 ± 1.10% (43.8% to 56.78%) from the total MyHC. The MyHC pattern in the skeletal muscles of the Akhal-Teke horses shows that the muscles of these horses have a high capacity both for endurance and speed.

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Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms

Cited by 744 publications

References 32 publications

Running‐wheel activity delays mitochondrial respiratory flux decline in aging mouse muscle via a post‐transcriptional mechanism

Running‐wheel activity delays mitochondrial respiratory flux decline in aging mouse muscle via a post‐transcriptional mechanism

High‐Intensity Resistance Training with Insufficient Recovery Time Between Bouts Induce Atrophy and Alterations in Myosin Heavy Chain Content in Rat Skeletal Muscle

Myosin heavy chain pattern in the Akhal-Teke horses

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