ArticleJournal of muscle research and cell motility2001
Inactivation of sarcoplasmic reticulum Ca(2+)-atpase in low-frequency stimulated rat muscle.
Article in Journal of muscle research and cell motility, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 23 citations in OpenAlex.
- Vitamin E management of oxidative damage-linked dysfunctions of hyperthyroid tissues.Cellular and molecular life sciences : CMLS · 2013Review
- The effects of eccentric contraction on myofibrillar proteins in rat skeletal muscle.European journal of applied physiology · 2010Article
- Time course of changes in in vitro sarcoplasmic reticulum Ca2+-handling and Na+-K+-ATPase activity during repetitive contractions.Pflugers Archiv : European journal of physiology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Continuous low-frequency stimulation (CLFS) by implanted electrodes for 12-24 h led to a significant (approximately 30%) decrease in the activity of sarcoplasmic reticulum Ca(2+)-ATPase in fast-twitch extensor digitorum longus (EDL) and tibialis anterior (TA) muscles of intact rats. The decline in catalytic activity after 24 h of CLFS was accompanied by an approximately twofold increase in dinitrophenylhydrazine-reactive carbonyl groups of the enzyme. It also correlated with an immunochemically determined 30% decrease in Ca2(+)-ATPase protein. Recovery studies after 12 h of CLFS revealed a relatively slow (48-72 h) re-establishment of normal catalytic activity. These findings suggest that the 30% decline of Ca(2+)-ATPase activity in low-frequency stimulated rat muscle led to an irreversible modification by protein oxidation. The decrease in Ca(2+)-ATPase protein most likely resulted from the degradation of inactive Ca(2+)-ATPase molecules. The relatively slow recovery of Ca(2+)-ATPase activity suggests that de novo synthesis of the enzyme may be necessary to re-attain normal activity.
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