Ca2+ permeation and/or binding to CaV1.1 fine-tunes skeletal muscle Ca2+ signaling to sustain muscle function
| العنوان: | Ca2+ permeation and/or binding to CaV1.1 fine-tunes skeletal muscle Ca2+ signaling to sustain muscle function |
|---|---|
| المؤلفون: | George G. Rodney, Mark Knoblauch, Christine Beeton, Pumin Zhang, Robert T. Dirksen, Amy D. Hanna, Mary E. Dickinson, Susan L. Hamilton, Adan Dagnino-Acosta, Iskander I. Ismailov, Dimitra K. Georgiou, Ted Tran, Johanna T. Lanner, Viktor Yarotskyy, Alla D. Lyfenko, Michael W. Swank, Cheng Long, Chang Seok Lee, Keke Dong, Ross A. Poché |
| المصدر: | Skeletal Muscle |
| بيانات النشر: | Springer Science and Business Media LLC, 2015. |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | MAPK/ERK pathway, Physiology, mTORC1, CaV1.1, 03 medical and health sciences, Cav1.1, Protein synthesis and Skeletal muscle, 0302 clinical medicine, Ca2+/calmodulin-dependent protein kinase, medicine, Orthopedics and Sports Medicine, Molecular Biology, Fatigue, 030304 developmental biology, 0303 health sciences, biology, Research, Endoplasmic reticulum, Skeletal muscle, Cell Biology, Permeation, Coupling (electronics), medicine.anatomical_structure, biology.protein, Biophysics, Fiber type, CaM kinase II, 030217 neurology & neurosurgery |
| الوصف: | Background Ca2+ influx through CaV1.1 is not required for skeletal muscle excitation-contraction coupling, but whether Ca2+ permeation through CaV1.1 during sustained muscle activity plays a functional role in mammalian skeletal muscle has not been assessed. Methods We generated a mouse with a Ca2+ binding and/or permeation defect in the voltage-dependent Ca2+ channel, CaV1.1, and used Ca2+ imaging, western blotting, immunohistochemistry, proximity ligation assays, SUnSET analysis of protein synthesis, and Ca2+ imaging techniques to define pathways modulated by Ca2+ binding and/or permeation of CaV1.1. We also assessed fiber type distributions, cross-sectional area, and force frequency and fatigue in isolated muscles. Results Using mice with a pore mutation in CaV1.1 required for Ca2+ binding and/or permeation (E1014K, EK), we demonstrate that CaV1.1 opening is coupled to CaMKII activation and refilling of sarcoplasmic reticulum Ca2+ stores during sustained activity. Decreases in these Ca2+-dependent enzyme activities alter downstream signaling pathways (Ras/Erk/mTORC1) that lead to decreased muscle protein synthesis. The physiological consequences of the permeation and/or Ca2+ binding defect in CaV1.1 are increased fatigue, decreased fiber size, and increased Type IIb fibers. Conclusions While not essential for excitation-contraction coupling, Ca2+ binding and/or permeation via the CaV1.1 pore plays an important modulatory role in muscle performance. Electronic supplementary material The online version of this article (doi:10.1186/s13395-014-0027-1) contains supplementary material, which is available to authorized users. |
| تدمد: | 2044-5040 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3ca179b6b70d9f640dbc6687433ace8Test https://doi.org/10.1186/s13395-014-0027-1Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e3ca179b6b70d9f640dbc6687433ace8 |
| قاعدة البيانات: | OpenAIRE |
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Methods We generated a mouse with a Ca2+ binding and/or permeation defect in the voltage-dependent Ca2+ channel, CaV1.1, and used Ca2+ imaging, western blotting, immunohistochemistry, proximity ligation assays, SUnSET analysis of protein synthesis, and Ca2+ imaging techniques to define pathways modulated by Ca2+ binding and/or permeation of CaV1.1. We also assessed fiber type distributions, cross-sectional area, and force frequency and fatigue in isolated muscles. Results Using mice with a pore mutation in CaV1.1 required for Ca2+ binding and/or permeation (E1014K, EK), we demonstrate that CaV1.1 opening is coupled to CaMKII activation and refilling of sarcoplasmic reticulum Ca2+ stores during sustained activity. Decreases in these Ca2+-dependent enzyme activities alter downstream signaling pathways (Ras/Erk/mTORC1) that lead to decreased muscle protein synthesis. The physiological consequences of the permeation and/or Ca2+ binding defect in CaV1.1 are increased fatigue, decreased fiber size, and increased Type IIb fibers. Conclusions While not essential for excitation-contraction coupling, Ca2+ binding and/or permeation via the CaV1.1 pore plays an important modulatory role in muscle performance. 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