Regulation of protein turnover in skeletal and cardiac muscle

Sugden, Peter H.; Fuller, SJ

doi:10.1042/bj2730021

Cited by 194 publications

(102 citation statements)

References 357 publications

(427 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The primary metabolic function of glucocorticoids is to moderate the demand for glucose by some tissues while concomitantly stimulating hepatic gluconeogenesis to increase glucose delivery to skeletal muscle and the brain. Increased secretion of glucocorticoids also suppresses muscle protein synthesis (Sugden and Fuller 1991). Glucocorticoids serve another important role by attenuating the cellular reaction to stress and/or trauma (i.e.…”

Section: Stress Responsementioning

confidence: 99%

Factors affecting beef palatability — farmgate to chilled carcass

Ferguson¹,

Bruce²,

Thompson³

et al. 2001

Aust. J. Exp. Agric.

116

View full text Add to dashboard Cite

Abstract. The potential eating quality of beef is set by the intrinsic structural and compositional characteristics of muscle. However, the extrinsic factors that prevail during the production of the animal, slaughter and processing of its carcass and finally, cooking can produce changes in these structural and compositional characteristics that ultimately manifest as large variations in beef palatability. The conditions that apply in the 24-48 h immediately before and after slaughter are recognised as having the largest influence on beef palatability. This review specifically examines the critical pre-and post-slaughter factors and discusses their putative effects on biochemical and physical changes in muscle and the consequences to beef palatability. Areas for future research within this domain are also discussed.

show abstract

Section: Stress Responsementioning

confidence: 99%

Factors affecting beef palatability — farmgate to chilled carcass

Ferguson¹,

Bruce²,

Thompson³

et al. 2001

Aust. J. Exp. Agric.

116

View full text Add to dashboard Cite

show abstract

“…Muscle protein turnover rate may be affected by numerous hormones (auto-, para-or endocrine) and metabolically related agents (see for review Sugden and Fuller, 1991). The only known factor, added to the medium, which may be involved in the protein turnover rate is the insulin in the culture medium.…”

Section: Fibre Morphologymentioning

confidence: 99%

Effects of strain on contractile force and number of sarcomeres in series of Xenopus laevis single muscle fibres during long-term culture

Jaspers¹,

Feenstra

Verheyen

et al. 2004

J Muscle Res Cell Motil

View full text Add to dashboard Cite

The aim of the present study is to test whether mechanical strain uniquely regulates muscle fibre atrophy/ hypertrophy and adaptation of the number of sarcomeres in series within mature muscle fibres in vitro. Mature single muscle fibres from Xenopus laevis illiofibularis muscle were cultured (4-97 days) while kept at negative strain (20% below passive slack length, 'short fibres') or at positive strain (5% over passive slack length, Ôlong fibresÕ). Before and after culture the number of sarcomeres in series was determined using laser diffraction. During culture, twitch and tetanic force characteristics were measured every day.Survival time of long fibres was substantially less than that of short fibres. Of the long fibres 40% died or became inexcitable within 1 week, whereas this did not occur for short fibres. During culture, twitch and tetanic force of all short fibres increased substantially. Regression analysis showed that the post-culture number of sarcomeres in series was not significantly changed compared to the number before culture. It is concluded that culture at negative strain does not result in atrophy or a reduction of the number of sarcomeres in series, even after 97 days. For the long fibres we did not detect any hypertrophy as tetanic force remained stable or decreased slowly, while twitch force varied. Regression analysis of the change of the number of sarcomeres in series as a function of the culture time showed a positive slope (P ¼ 0.054). Two out of four long fibres that were cultured for at least 2 weeks showed an increase in the number of sarcomeres of 4-5%. Compared with in vivo adaptation to mechanical stimuli this is much less than would be expected. The data suggest that strain may not be the only factor that regulates hypertrophy and the number of sarcomeres in series.

show abstract

“…IGF-1 and insulin enhance protein synthesis, and suppress protein degradation in skeletal muscle (4). Appropriate exercise also regulates skeletal muscle protein turnover (5,6).…”

mentioning

confidence: 99%

Regulation of Skeletal Muscle Protein Degradation and Synthesis by Oral Administration of Lysine in Rats

Sato

Ito

Nagasawa

2013

J Nutr Sci Vitaminol

View full text Add to dashboard Cite

Summary Several catabolic diseases and unloading induce muscle mass wasting, which causes severe pathological progression in various diseases and aging. Leucine is known to attenuate muscle loss via stimulation of protein synthesis and suppression of protein degradation in skeletal muscle. The aim of this study was to investigate the effects of lysine intake on protein degradation and synthesis in skeletal muscle. Fasted rats were administered 22.8-570 mg Lys/100 g body weight and the rates of myofibrillar protein degradation were assessed for 0-6 h after Lys administration. The rates of myofibrillar protein degradation evaluated by MeHis release from the isolated muscles were markedly suppressed after administration of 114 mg Lys/100 g body weight and of 570 mg Lys/100 g body weight. LC3-II, a marker of the autophagic-lysosomal pathway, tended to decrease (p50.05, 0.08) after Lys intake (114 mg/100 g body weight). However, expression of ubiquitin ligase E3 atrogin-1 mRNA and levels of ubiquitinated proteins were not suppressed by Lys intake. Phosphorylation levels of mTOR, S6K1 and 4E-BP1 in the gastrocnemius muscle were not altered after Lys intake. These results suggest that Lys is able to suppress myofibrillar protein degradation at least partially through the autophagic-lysosomal pathway, not the ubiquitin-proteasomal pathway, whereas Lys might be unable to stimulate protein synthesis within this time frame.

show abstract

Regulation of protein turnover in skeletal and cardiac muscle

Cited by 194 publications

References 357 publications

Factors affecting beef palatability — farmgate to chilled carcass

Factors affecting beef palatability — farmgate to chilled carcass

Effects of strain on contractile force and number of sarcomeres in series of Xenopus laevis single muscle fibres during long-term culture

Regulation of Skeletal Muscle Protein Degradation and Synthesis by Oral Administration of Lysine in Rats

Contact Info

Product

Resources

About

Regulation of protein turnover in skeletal and cardiac muscle

Cited by 194 publications

References 357 publications

Factors affecting beef palatability &mdash; farmgate to chilled carcass

Factors affecting beef palatability &mdash; farmgate to chilled carcass

Effects of strain on contractile force and number of sarcomeres in series of Xenopus laevis single muscle fibres during long-term culture

Regulation of Skeletal Muscle Protein Degradation and Synthesis by Oral Administration of Lysine in Rats

Contact Info

Product

Resources

About

Factors affecting beef palatability — farmgate to chilled carcass

Factors affecting beef palatability — farmgate to chilled carcass