Relative synthesis rate of individual muscle proteins: a new approach

Schreurs, V.V.A.M.; Boekholt, H.A.; Koopmanschap, R.E.; Rotterdam, Walter van

doi:10.18174/njas.v33i3.16843

Cited by 5 publications

(6 citation statements)

References 6 publications

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“…RNA and protein ratio called the RNA unit [ 58 ] and the protein synthesis per RNA unit has been defi ned as the "activity" of RNA [ 58 ] and shown as a stable indicator of protein synthesis or eff ectiveness of the translation process in cell in physiological conditions [ 61 , 108 ] . About 4 decades ago, it was shown that the protein turnover rate depends on the type of muscle [ 28 ] and even functionally related proteins such as myofi brillar proteins have diff erent speed of renewal [ 79 ] . It was shown that a relationship exists between the turnover rate of myofi brillar protein and quantity of mitochondria in muscle [ 28 , 98 ] .…”

Section: Protein Synthesis and Degradation In Muscle Fi Bresmentioning

confidence: 99%

Muscle Protein Turnover in Endurance Training: a Review

2011

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There has been much debate about skeletal muscle capacity to adapt to long-lasting endurance exercise. Exercise in the aerobic zone of metabolism does not result in hypertrophy of skeletal muscle fibres but increases their oxidative capacity. The duration and intensity of an exercise session determines the time period of depressed muscle protein synthesis and increased degradation rate during the recovery period after exercise. Protein turnover characterizes the renewal processes of muscle proteins and the functional capacity of muscle. The turnover rate of myofibrillar proteins is slow in comparison with mitochondrial proteins and depends on the oxidative capacity of muscle fibres. The turnover rate of myofibrillar proteins in the same muscle is different and is also different within the myosin molecule between myosin heavy and light chain isoforms. The turnover rate of muscle proteins in endurance training shows the adaptation of skeletal muscle to long-lasting exercise via remodelling of muscle structures. Adaptational coordination between myofibrillar and mitochondrial compartments shows the physiological role and adaptational capacity of skeletal muscle to endurance training. It is challenging to use muscle protein turnover for the purposes of monitoring the training process of endurance athletes, optimizing training programs and preventing overtraining.

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Section: Protein Synthesis and Degradation In Muscle Fi Bresmentioning

confidence: 99%

Muscle Protein Turnover in Endurance Training: a Review

2011

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“…Turnover Rate of MHC. The relative specific activity, which characterizes the turnover rate of MHC protein fraction, was calculated as the ratio of the specific activity of the protein fraction (Sb) to the specific activity of total muscle-cell protein (Sa; Schreurs, Boekholt, Koopmanschap, & van Rotterdam, 1985;Schreurs, Boekholt, & Koopmanschap, 1981) and expressed in percentages.…”

Section: Separation Of Total Muscle Cell Myofibrillar and Sarcoplasmentioning

confidence: 99%

Age-Related Changes in Skeletal-Muscle Myosin Heavy-Chain Composition: Effect of Mechanical Loading

Pehme

Alev²,

Kaasik³

et al. 2004

Journal of Aging and Physical Activity

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The purpose of this study was to investigate the effect of compensatory hypertrophy (CH), heavy-resistance exercise training (HRET), and simultaneous CH and HRET on fast-twitch skeletal-muscle myofibrillar-protein synthesis, myosin heavy-chain (MHC) turnover rate, and MHC-isoform composition in young and old rats. In young animals all treatments intensified myofibrillar-protein synthesis, whereas in old animals with CH protein synthesis remained unchanged. The relative content of MHC I and IID in plantaris muscle increases with age, and the relative content of MHC IIB decreases. HRET and simultaneous CH and HRET decreased the proportion of MHC IIB and IIA and increased that of MHC IID in young rat muscle. In old rat muscle, relative content of MHC IID decreased and that of MHC IIB increased. CH decreased relative content of MHC IIB in both age groups and of MHC IIA in old animals. Relative content of MHC IID increased in both groups, and of MHC IIA, in young animals. MHC in plantaris of young rats turned over much faster in all types of mechanical loading but in old rats only during HRET and its combination with CH.

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“…After four hours the animal was killed and tissues were weighed and sampled. The specific activity (SA) of total tissue protein and individual muscle proteins was ex amined in protein fractions obtained by SDS gel filtration (Schreurs et al, 1983(Schreurs et al, , 1985.…”

Section: Methodsmentioning

confidence: 99%

Relation of protein synthesis and amino acid oxidation: effects of protein deprivation.

Schreurs¹,

Mensink²,

Boekholt³

et al. 1985

NJAS

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For up to 3 weeks 10 male rats weighing about 300 g were given diets which had 20% protein or were free from protein but supplied similar amounts of energy. The rats were killed at intervals; the last 2 were given L-[U-14C]tyrosine by infusion 4 h before they were killed. The deprived rats showed restricted amino acid oxidation and a decreased rate of protein synthesis. Amino acid oxidation continued by an uneven loss of proteins from the tissues. In muscle the composition and relative synthesis rate of the constituent proteins were not affected. Liver and kidney, compared with other tissues tended to maintain a relatively high rate of protein turnover. (Abstract retrieved from CAB Abstracts by CABI’s permission)

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Relative synthesis rate of individual muscle proteins: a new approach

Cited by 5 publications

References 6 publications

Muscle Protein Turnover in Endurance Training: a Review

Muscle Protein Turnover in Endurance Training: a Review

Age-Related Changes in Skeletal-Muscle Myosin Heavy-Chain Composition: Effect of Mechanical Loading

Relation of protein synthesis and amino acid oxidation: effects of protein deprivation.

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