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J Appl Physiol (April 25, 2003). doi:10.1152/japplphysiol.00358.2003
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Submitted on April 10, 2003
Accepted on April 23, 2003

Paradoxical absence of M lines and downregulation of creatine kinase in mouse extraocular muscle

Francisco H Andrade1*, Anita P Merriam2, Wei Guo2, Georgiana Cheng2, Colleen A McMullen1, Katrin Hayess3, Peter F M van der Ven3, and John D Porter4

1 Department of Neurology, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH, USA
2 Department of Ophthalmology, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH, USA
3 Department of Cell Biology, University of Potsdam, Potsdam, Germany
4 Department of Neurology, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH, USA; Department of Ophthalmology, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH, USA; Department of Neurosciences, Case Western Reserve University, Cleveland, OH, USA

* To whom correspondence should be addressed. E-mail: fha{at}po.cwru.edu.

The M lines are structural landmarks in striated muscles, necessary for sarcomeric stability and as anchoring sites for the M isoform of creatine kinase (CK-M). These structures, especially prominent in fast skeletal muscles, are missing in rodent extraocular muscle, a particularly fast and active muscle group. In this study, we tested the hypotheses that (1) myomesin and M-protein (cytoskeletal components of the M lines) and CK-M are downregulated in mouse extraocular muscle compared to the leg muscles gastrocnemius/soleus, and (2) the expression of other cytosolic and mitochondrial CK isoforms are correspondingly increased. As expected, mouse extraocular muscles expressed lower levels of myomesin, M-protein, and CK-M mRNA than the leg muscles. Immunocytochemically, myomesin and M-protein were not detected in the banding pattern typically seen in other skeletal muscles. Surprisingly, message abundance for the other known CK isoforms was also lower in the extraocular muscles. Moreover, total CK activity was significantly decreased compared to the leg muscles. Based on these data, we reject our second hypothesis and propose that other energy buffering systems may be more important in the extraocular muscles. The downregulation of major structural and metabolic elements and relative overexpression of two adenylate kinase isoforms suggest that the extraocular muscle group copes with its functional requirements using strategies not seen in typical skeletal muscles.




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