ArticleThe Biochemical journal1992
Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits.
Article in The Biochemical journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 71 citations in OpenAlex.
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- Activity, abundance and expression of Ca²⁺-activated proteases in skeletal muscle of the aestivating frog, Cyclorana alboguttata.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015Article
- Effect of nutrient restriction and re-feeding on calpain family genes in skeletal muscle of channel catfish (Ictalurus punctatus).PloS one · 2013Article
- Effect of exercise training on calpain systems in lean and obese Zucker rats.International journal of biological sciences · 2008Article
- Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle.European journal of applied physiology · 2007Article
- Calpain, calpastatin activities and ratios during myocardial ischemia-reperfusion.Molecular and cellular biochemistry · 2002Article
- Poly A RNA status and expression of milli (m) and micro (μ) calpains in skeletal muscle of duchenne muscular dystrophy patients.Indian journal of clinical biochemistry : IJCB · 2002Article
- Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability.The Biochemical journal · 2000Article
- Role of calpain in skeletal-muscle protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle.The Biochemical journal · 1996Article
- Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+ -activated, and ubiquitin-proteasome proteolytic pathways.The Journal of clinical investigation · 1996Article
- Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging.The Journal of clinical investigation · 1995Article
- Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy.The Biochemical journal · 1995Article
- Proteolysis in illness-associated skeletal muscle atrophy: from pathways to networks.Critical reviews in clinical laboratory sciencesReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To investigate the role of calpains in myofibrillar protein degradation in skeletal muscle and the regulation of their activity in vivo, we studied the effects of fasting on gene expression of calpains and calpastatin in the skeletal muscle of rabbits. In response to fasting, myofibrillar protein degradation increased 2-fold and mRNA levels of calpain I, calpain II and calpastatin were also increased. However, calpain and calpastatin activities remained unchanged. To investigate this discrepancy, we analysed polysomal calpain mRNA. Results indicated that fasting caused a 2-fold increase in the loading of calpain I and II mRNAs on ribosomes. Thus transcription of genes encoding calpain may be increased during fasting to ensure adequate synthesis of the proteinases needed to mobilize muscle protein reserves. The effect of fasting on calpain and calpastatin mRNA expression is shared by cathepsin D and proteasome C2 but not by beta-actin, implying that fasting invokes control of several proteolytic systems in skeletal muscle and underscores the possibility that each proteolytic system plays a role in the adaptation of skeletal muscle to the fasted state.
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