Role of parvalbumin in fatigue-induced changes in force and cytosolic calcium transients in intact single mouse myofibers.
Role of parvalbumin in fatigue-induced changes in force and cytosolic calcium transients in intact single mouse myofibers.
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小清蛋白在疲劳引起的完整单只小鼠肌纤维中力和胞质钙瞬变变化中的作用。
DOI:
10.1152/japplphysiol.00861.2021
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发表时间:
2022
期刊:
影响因子:
--
通讯作者:
Hogan,MichaelC
中科院分区:
文献类型:
--
作者:
Nogueira,Leonardo;Gilmore,NatalieK;Hogan,MichaelC
One of the most important cytosolic Ca2+buffers present in mouse fast-twitch myofibers, but not in human myofibers, is parvalbumin (PV). Previous work using conventional PV gene (PV) knockout (PV-KO) mice suggests that lifelongPVablation increases fatigue resistance, possibly due to compensations in mitochondrial volume. In this work,PVablation was induced only in adult mice (PV-KO), and contractile and cytosolic Ca2+responses during fatigue were studied in isolated muscle and intact single myofibers. Results were compared with control littermates (PV-Ctr). We hypothesized that the reduced myofiber cytosolic Ca2+buffering developed only in adult PV-KO mice leads to a larger cytosolic free Ca2+concentration ([Ca2+]c) during repetitive contractions, increasing myofiber fatigue resistance. Extensor digitorum longus (EDL) muscles from PV-KO mice had higher force in unfused stimulations (∼50%,P< 0.05) and slowed relaxation (∼46% higher relaxation time,P< 0.05) versus PV-Ctr, but muscle fatigue resistance or fatigue-induced changes in relaxation were not different between genotypes (P> 0.05). In intact single myofibers from flexor digitorum brevis (FDB) muscles, basal and tetanic [Ca2+]cduring fatiguing contractions were higher in PV-KO (P< 0.05), accompanied by a greater slowing in estimated sarcoplasmic reticulum (SR) Ca2+-pumping versus PV-Ctr myofibers (∼84% reduction,P< 0.05), but myofiber fatigue resistance was not different between genotypes (P> 0.05). Our results demonstrate that although the estimated SR Ca2+uptake was accelerated in PV-KO, the total energy demand by the major energy consumers in myofibers, the cross-bridges, and SR Ca2+ATPase were not altered enough to affect the energy supply for contractions, and therefore fatigue resistance remained unaffected.NEW & NOTEWORTHYParvalbumin (PV) is a cytosolic Ca2+buffer that is present in mouse myofibers but not in human muscle. We show that inducible knockout ofPVleads to increases in myofiber cytosolic free Ca2+concentrations and slowing of Ca2+pumping during fatigue versus control mice. However,PVablation does not interfere with fatigue-induced slowing in relaxation or fatigue resistance. These data support the use of mouse muscle as a suitable model to investigate human muscle fatigue.
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DOI:
10.1152/ajpregu.00687.2005
发表时间:
2006-06
期刊:
American journal of physiology. Regulatory, integrative and comparative physiology
影响因子:
--
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DOI:
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发表时间:
1995
影响因子:
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