The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Remodeling of ryanodine receptor complex causes “leaky” channels: A molecular mechanism for decreased exercise capacity
Open accessAbstract
During exercise, defects in calcium (Ca 2+ ) release have been proposed to impair muscle function. Here, we show that during exercise in mice and humans, the major Ca 2+ release channel required for excitation–contraction coupling (ECC) in skeletal muscle, the ryanodine receptor (RyR1), is progressively PKA-hyperphosphorylated, S -nitrosylated, and depleted of the phosphodiesterase PDE4D3 and the RyR1 stabilizing subunit calstabin1 (FKBP12), resulting in “leaky” channels that cause decreased exercise tolerance in mice. Mice with skeletal muscle-specific calstabin1 deletion or PDE4D deficiency exhibited significantly impaired exercise capacity. A small molecule (S107) that prevents depletion of calstabin1 from the RyR1 complex improved force generation and exercise capacity, reduced Ca 2+ -dependent neutral protease calpain activity and plasma creatine kinase levels. Taken together, these data suggest a possible mechanism by which Ca 2+ leak via calstabin1-depleted RyR1 channels leads to defective Ca 2+ signaling, muscle damage, and impaired exercise capacity.
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Quercetin Reduces Illness but Not Immune Perturbations after Intensive Exercise
NIEMAN, D. C., HENSON, D. A., GROSS, S. J., JENKINS, D. P., DAVIS, J. M., MURPHY, E. A., CARMICHAEL, M. D., DUMKE, C. L., UTTER, A. C., MCANULTY, S. R., et al. (2007) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e318076b566 · Cited by 193 · cited 1×
“Briefly, human subjects underwent an intensive cycling protocol consisting of three consecutive days of cycling for 3 hours at 70% VO2max (18).”
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Cited by
Protein S-nitrosylation in health and disease: a current perspective
Foster, M. W., Hess, D. T., & Stamler, J. S. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.007 · Cited by 752
Ryanodine receptor oxidation causes intracellular calcium leak and muscle weakness in aging
Andersson, D. C., Betzenhauser, M. J., Reiken, S., Meli, A. C., Umanskaya, A., Xie, W., Shiomi, T., Zalk, R., Lacampagne, A., & Marks, A. R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.014 · Cited by 424
Allen, D. G., Whitehead, N. P., & Froehner, S. C. (2016) · Physiological Reviews · doi:10.1152/physrev.00007.2015 · Cited by 426
RyR1 S-Nitrosylation Underlies Environmental Heat Stroke and Sudden Death in Y522S RyR1 Knockin Mice
Durham, W. J., Aracena-Parks, P., Long, C., Rossi, A. E., Goonasekera, S. A., Boncompagni, S., Galvan, D. L., Gilman, C. P., Baker, M. R., Shirokova, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.042 · Cited by 351
Age-induced oxidative stress: how does it influence skeletal muscle quantity and quality?
Baumann, C. W., Kwak, D., Liu, H. M., & Thompson, L. V. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00321.2016 · Cited by 169
Metadata
- Authors
- Bellinger, A. M., Reiken, S., Dura, M., Murphy, P. W., Deng, S.-X., Landry, D. W., Nieman, D., Lehnart, S. E., Samaru, M., LaCampagne, A., & Marks, A. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-02-12
- Volume
- 105
- Issue
- 6
- Pages
- 2198-2202
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2139337253
- Cited by
- 352
- References
- 1
- FWCI
- 10.67
- Type
- journal article
- Language
- en
- Open access
- green
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- Bellinger, A. M., Reiken, S., Dura, M., Murphy, P. W., Deng, S.-X., Landry, D. W., Nieman, D., Lehnart, S. E., Samaru, M., LaCampagne, A., & Marks, A. R. (2008). Remodeling of ryanodine receptor complex causes “leaky” channels: A molecular mechanism for decreased exercise capacity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0711074105
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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