Effect of exercise on sarcoplasmic reticulum Ca&amp;lt;sup&amp;gt;2+&amp;lt;/sup&amp;gt; transport in muscle of mouse lines long-term selected for different Performance traits

Küchenmeister, U.; Langhammer, Martina; Renne, Ulla; Nürnberg, Gerd; Ender, K.

doi:10.5194/aab-44-441-2001

Cited by 2 publications

(2 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In particular, exercise attenuates Ca 2+ uptake and SR Ca 2+ -ATPase activity (Byrd et al 1989a(Byrd et al , 1989bLuckin et al 1991;Gollnick et al 1991;Booth et al 1997) or SR Ca 2+ release (Favero et al 1993;Westerblad et al 1998, Ortenblad et al 2000. Kuchenmeister et al (2001) reported that pre-slaughter stress in pigs also influenced Ca 2+ uptake. In sheep, pre-slaughter exercise elicited an 18% reduction in Ca 2+ uptake, but this was not found to be significantly different to the uptake rates in the non-exercised controls.…”

Section: Pre-slaughter Stressmentioning

confidence: 99%

Regulation of post-mortem glycolysis in ruminant muscle

Ferguson

Gerrard²

2014

Anim. Prod. Sci.

View full text Add to dashboard Cite

Abstract. As a tissue, muscle has the unique ability to switch its metabolic source of ATP, the energy currency underpinning muscle function. During oxygen debt, such as that occurring immediately following the death of animals, anaerobic metabolism is initiated in an attempt to restore homeostasis within the muscle. The cascade of biochemical events that are initiated is paramount in the context of meat quality. This review revisits this reasonably well-known subject but takes a new perspective by drawing on the understanding outside the traditional discipline of meat science. Our understanding of the intrinsic regulators of glycolytic flux has improved but knowledge gaps remain. Further efforts to understand how the glycolytic enzyme kinetics are influenced by both pre-and post-slaughter factors will be beneficial in the ongoing quest to maximise fresh meat quality.

show abstract

Section: Pre-slaughter Stressmentioning

confidence: 99%

Regulation of post-mortem glycolysis in ruminant muscle

Ferguson

Gerrard²

2014

Anim. Prod. Sci.

View full text Add to dashboard Cite

show abstract

“…In some physiological and mainly pathological states muscle growth is determined solely at the catabolic side (eg. muscular atrophy after denervation and tenotomy, chemically and hormonally induced changes) (KÜCHENMEISTER et al, 2001;KÜCHEN-MEISTER and KUHN, 2003) The process of protein catabolism involves a nonlysosomal and lysosomal route of intracellular protein catabolism. The calciumdependent neutral proteolytic system consisting of µ-and m-calpain and their natural inhibitor calpastatin, do not degrade any of the major myofibrillar proteins like myosin and actin (THOMPSON and PALMER, 1998;GOLL et al, 1998;JOHARI et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Skeletal muscle and liver protein degradation in mice divergently selected for low and high body weight over 108 generations

Rosochacki

Wirth-Dzieciolowska

Zimowska³

et al. 2005

Arch. Anim. Breed.

View full text Add to dashboard Cite

Experiment was carried out on 111 and 13-14 weeks old mice divergently selected for low (L) and high (C) body weight over 108 generations. In leg muscle and liver cathepsin D (CatD) was determined as pepstatin sensitive activity (PSCatD), and as pepstatin-insensitive (PIA) and leupeptin-insensitive (LIA) acid autolytic activities (AAA) were measured. In leg muscle and liver all measured activities were higher in L as compared to C and control (K) mice. The percent of inhibition of LIA was lower in L then C mice in both examined tissues. In the leg muscles, in L mice protein catabolism was mostly influenced by CatD, but in the liver CatD was mostly active in K mice. CatD, PSCatD, AAA and LIA in leg muscle of L mice as compare to K were higher in female (F) by 68 %, 68.5 %, 91.3 % and 94.5 %, respectively, and in male (M) mice by 43.4 %, 54 %, 47.1 % and 64 %, respectively. The percent of inhibition by leupeptin in AAA was higher in C mice by 61.9 % in F and by 40 % in M mice. In the liver, PIA was higher by about 45 % in L and by 28.5 % in C mice as compare to K ones. There were about 36% of 30.00-39.99 µm muscle fibrils in M mice and in males of L group 40.00-49.99 µm fibrils appeared at 25% (absent in 3 weeks mice). In female, all measured fibril diameters were in higher percent in L than in C group. RNA variables were higher by about 25% (in average) in C as compare to K and L groups. Functional cell size (FCS) was lowered in L and C group as compared to K by about 10 % (in average). These results indicate on faster proteins turnover in L than in C group of mice. Key Words: mice; long term selection, body weight, proteolytic enzyme activity, muscle DNA-RNA, liver DNA-RNA, fibre size Die prozentuale Hemmung der LIA-Werte war in beiden Geweben in der L-Gruppe niedriger als in der C-Gruppe. Im Schenkelmuskel der L-Mäuse wurde der Proteinkatabolismus überwiegend durch die CatD beeinflusst. In der Leber war die CatD aktiver in der K-Gruppe. Die Aktivität von CatD, PSCatD, AAA und LIA war im Schenkelmuskel der L-Mäuse höher als bei den K-Mäusen. Bei den weiblichen Tieren der L-Gruppe waren die entsprechenden Messwerte um 68,0%, 68,5%, 91,3% bzw. 94,5% höher als bei der Kontrollgruppe. Bei den männlichen Tieren der gleichen Gruppe erhöhten sich die analogen Werte jedoch nur um 43,3%, 54,0%, 47,1%, bzw. 64,0%. Die prozentuale Hemmung der LIA bezüglich der AAA war in der C-Gruppe höher (Weibchen 61,9%; Männchen 40,0%). In der Leber war die Aktivität der PIA bei der L-Gruppe um 45,0% und bei der C-Gruppe um 28,5% höher als bei der Kontrollgruppe. Im Alter von drei Monaten fanden sich in der K-Gruppe bei den männlichen Mäusen 36,0% mehr Fibrillen in der Muskelfaser mit einem Durchmesser von 30,00-39,99 µm, bei der L-Gruppe nur * Supported by Projects No PBZ-KBN-036/P06/07, S.V.9 and S/IIŚ/26/01 ROSOCHACKI et al.: Skeletal muscle and liver protein degradation in mice divergently selected for low and high body weight 506 25,0% mehr Fasern mit einem Durchmesser von 40,00-49,99 µm, die bei den Mäusen im Alter von dre...

show abstract

Effect of exercise on sarcoplasmic reticulum Ca<sup>2+</sup> transport in muscle of mouse lines long-term selected for different Performance traits

Cited by 2 publications

References 31 publications

Regulation of post-mortem glycolysis in ruminant muscle

Regulation of post-mortem glycolysis in ruminant muscle

Skeletal muscle and liver protein degradation in mice divergently selected for low and high body weight over 108 generations

Contact Info

Product

Resources

About