The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Calcium's Role in Mechanotransduction during Muscle Development
Open accessAbstract
Mechanotransduction is a process where cells sense their surroundings and convert the physical forces in their environment into an appropriate response. Calcium plays a crucial role in the translation of such forces to biochemical signals that control various biological processes fundamental in muscle development. The mechanical stimulation of muscle cells may for example result from stretch, electric and magnetic stimulation, shear stress, and altered gravity exposure. The response, mainly involving changes in intracellular calcium concentration then leads to a cascade of events by the activation of downstream signaling pathways. The key calcium-dependent pathways described here include the nuclear factor of activated T cells (NFAT) and mitogen-activated protein kinase (MAPK) activation. The subsequent effects in cellular homeostasis consist of cytoskeletal remodeling, cell cycle progression, growth, differentiation, and apoptosis, all necessary for healthy muscle development, repair, and regeneration. A deregulation from the normal process due to disuse, trauma, or disease can result in a clinical condition such as muscle atrophy, which entails a significant loss of muscle mass. In order to develop therapies against such diseased states, we need to better understand the relevance of calcium signaling and the downstream responses to mechanical forces in skeletal muscle. The purpose of this review is to discuss in detail how diverse mechanical stimuli cause changes in calcium homeostasis by affecting membrane channels and the intracellular stores, which in turn regulate multiple pathways that impart these effects and control the fate of muscle tissue.
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Cites
The versatility and universality of calcium signalling
Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Role of cell shape in growth control
Folkman, J., & Moscona, A. (1978) · Nature · doi:10.1038/273345a0 · Cited by 2,422
Transcriptional regulation by calcium, calcineurin, and NFAT
Hogan, P. G., Chen, L., Nardone, J., & Rao, A. (2003) · Genes & Development · doi:10.1101/gad.1102703 · Cited by 1,991
Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
Schlaepfer, D. D., Hanks, S. K., Hunter, T., & Geer, P. V. D. (1994) · Nature · doi:10.1038/372786a0 · Cited by 1,595
Weaver, V. M., Petersen, O. W., Wang, F., Larabell, C. A., Briand, P., Damsky, C., & Bissell, M. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.1.231 · Cited by 1,483
Jaalouk, D. E., & Lammerding, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2597 · Cited by 1,396
Atrophy of the soleus muscle by hindlimb unweighting
Thomason, D. B., & Booth, F. W. (1990) · Journal of Applied Physiology · doi:10.1152/jappl.1990.68.1.1 · Cited by 631
Biochemical adaptation of human skeletal muscle to heavy resistance training and immobilization
MacDougall, J. D., Ward, G. R., Sale, D. G., & Sutton, J. R. (1977) · Journal of Applied Physiology · doi:10.1152/jappl.1977.43.4.700 · Cited by 312
Reorganization of microfilament structure induced by ac electric fields
Cho, M. R., Thatte, H. S., Lee, R. C., & Golan, D. E. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.13.8940302 · Cited by 73
Rana, B., Mischoulon, D., Xie, Y., Bucher, N. L. R., & Farmer, S. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.5858-5869.1994 · Cited by 34
Cited by
Role of YAP/TAZ in mechanotransduction
Dupont, S., Morsut, L., Aragona, M., Enzo, E., Giulitti, S., Cordenonsi, M., Zanconato, F., Le Digabel, J., Forcato, M., Bicciato, S., et al. (2011) · Nature · doi:10.1038/nature10137 · Cited by 5,979
The NLRP3 Inflammasome: an overview of mechanisms of activation and regulation
Kelley, N., Jeltema, D., Duan, Y., & He, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133328 · Cited by 3,539
Cell Movement Is Guided by the Rigidity of the Substrate
Lo, C.-M., Wang, H.-B., Dembo, M., & Wang, Y.-L. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76279-5 · Cited by 3,289
Piezo1 and Piezo2 Are Essential Components of Distinct Mechanically Activated Cation Channels
Coste, B., Mathur, J., Schmidt, M., Earley, T. J., Ranade, S., Petrus, M. J., Dubin, A. E., & Patapoutian, A. (2010) · Science · doi:10.1126/science.1193270 · Cited by 3,316
Flow-mediated endothelial mechanotransduction
Davies, P. F. (1995) · Physiological Reviews · doi:10.1152/physrev.1995.75.3.519 · Cited by 2,802
Metadata
- Authors
- Benavides Damm, T., & Egli, M.
- Venue
- Cellular Physiology and Biochemistry
- Publisher
- S. Karger AG
- Published
- 2014
- Volume
- 33
- Issue
- 2
- Pages
- 249-272
- ISSN
- 1015-8987 (ISSN-L)
- 1421-9778
- OpenAlex
- W2036145275
- Cited by
- 14,502
- References
- 12
- FWCI
- 363.21
- Type
- journal article
- Language
- en
- Open access
- gold
- Licence
- creativecommons.org/licenses/by-nc/3.0/ (vor)
- creativecommons.org/licenses/by-nc/3.0/ (tdm)
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