Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle

Staunton L, Jockusch H, Wiegand C, Albrecht T, Ohlendieck K (2011)
Molecular BioSystems 7(8): 2480-2489.

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Abstract
Myotonia is a symptom of various genetic and acquired skeletal muscular disorders and is characterized by hyperexcitability of the sarcolemma. Here, we have performed a comparative proteomic study of the genetic mouse models ADR, MTO and MTO*5J of human congenital myotonia in order to determine myotonia-specific changes in the global protein complement of gastrocnemius muscle. Proteomic analyses of myotonia in the mouse, which is caused by mutations in the gene encoding the muscular chloride channel Clc1, revealed a generally perturbed protein expression pattern in severely affected ADR and MTO muscle, but less pronounced alterations in mildly diseased MTO*5J mice. Alterations were found in major metabolic pathways, the contractile machinery, ion handling elements, the cellular stress response and cell signaling mechanisms, clearly confirming a glycolytic-to-oxidative transformation process in myotonic fast muscle. In the long-term, a detailed biomarker signature of myotonia will improve our understanding of the pathobiochemical processes underlying this disorder and be helpful in determining how a single mutation in a tissue-specific gene can trigger severe downstream effects on the expression levels of a very large number of genes in contractile tissues.
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Staunton L, Jockusch H, Wiegand C, Albrecht T, Ohlendieck K. Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle. Molecular BioSystems. 2011;7(8):2480-2489.
Staunton, L., Jockusch, H., Wiegand, C., Albrecht, T., & Ohlendieck, K. (2011). Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle. Molecular BioSystems, 7(8), 2480-2489.
Staunton, L., Jockusch, H., Wiegand, C., Albrecht, T., and Ohlendieck, K. (2011). Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle. Molecular BioSystems 7, 2480-2489.
Staunton, L., et al., 2011. Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle. Molecular BioSystems, 7(8), p 2480-2489.
L. Staunton, et al., “Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle”, Molecular BioSystems, vol. 7, 2011, pp. 2480-2489.
Staunton, L., Jockusch, H., Wiegand, C., Albrecht, T., Ohlendieck, K.: Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle. Molecular BioSystems. 7, 2480-2489 (2011).
Staunton, Lisa, Jockusch, Harald, Wiegand, Christiane, Albrecht, Timo, and Ohlendieck, Kay. “Identification of secondary effects of hyperexcitability by proteomic profiling of myotonic mouse muscle”. Molecular BioSystems 7.8 (2011): 2480-2489.
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42 References

Data provided by Europe PubMed Central.


Reichmann, Pfluegers Arch. 418(), 1991

Hicks, Am. J. Physiol. 2273(), 1997
Application of animal models: chronic electrical stimulation-induced contractile activity.
Ljubicic V, Adhihetty PJ, Hood DA., Can J Appl Physiol 30(5), 2005
PMID: 16293907
Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation.
Donoghue P, Doran P, Dowling P, Ohlendieck K., Biochim. Biophys. Acta 1752(2), 2005
PMID: 16140047
Multifaceted roles of glycolytic enzymes.
Kim JW, Dang CV., Trends Biochem. Sci. 30(3), 2005
PMID: 15752986
Proteomics of skeletal muscle glycolysis.
Ohlendieck K., Biochim. Biophys. Acta 1804(11), 2010
PMID: 20709194
Carbon dioxide transport and carbonic anhydrase in blood and muscle.
Geers C, Gros G., Physiol. Rev. 80(2), 2000
PMID: 10747205
The human PDI family: versatility packed into a single fold.
Appenzeller-Herzog C, Ellgaard L., Biochim. Biophys. Acta 1783(4), 2008
PMID: 18093543
Activity-dependent repression of muscle genes by NFAT.
Rana ZA, Gundersen K, Buonanno A., Proc. Natl. Acad. Sci. U.S.A. 105(15), 2008
PMID: 18408153
NFAT isoforms control activity-dependent muscle fiber type specification.
Calabria E, Ciciliot S, Moretti I, Garcia M, Picard A, Dyar KA, Pallafacchina G, Tothova J, Schiaffino S, Murgia M., Proc. Natl. Acad. Sci. U.S.A. 106(32), 2009
PMID: 19633193
Increased density of satellite cells in the absence of fibre degeneration in muscle of myotonic mice.
Schimmelpfeng J, Jockusch H, Heimann P., Cell Tissue Res. 249(2), 1987
PMID: 3621304

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