@article{OCHALA_CARPÉN_LARSSON_2009, title={Maintenance of muscle mass, fiber size, and contractile function in mice lacking the Z-disc protein myotilin}, volume={114}, url={https://ujms.net/index.php/ujms/article/view/6204}, DOI={10.3109/03009730903276399}, abstractNote={<p><em>Background.</em>&nbsp;Myofibrillar myopathies constitute a rare group of congenital neuromuscular disorders, frequently associated with mutations in Z-disc proteins such as myotilin. Myotilin location and interactions with other Z-disc proteins are clearly defined, but its role in the regulation of muscle structure and function remains unknown. The present study aims at investigating this specific role of myotilin.</p> <p><em>Methods.</em>&nbsp;Skeletal and cardiac muscles were collected from adult mice with a targeted deletion of myotilin (myo<sup>-/-</sup>) and wild-type animals (myo<sup>+/+</sup>).</p> <p><em>Results and conclusion.</em>&nbsp;Similar skeletal and cardiac muscle weights were observed in myo<sup>-/-</sup>&nbsp;and myo<sup>+/+</sup>&nbsp;mice. At the muscle cell level, the size and force production of single membrane permeabilized fibers were identical between myo<sup>-/-</sup>&nbsp;and myo<sup>+/+</sup>&nbsp;rodents. Thus, myotilin does not have a significant influence on muscle mass, muscle fiber size, or regulation of muscle contraction. Alternatively, compensatory over-expressions of other elements including proteins from the same subfamily, or Z-disc proteins such as telethonin, or intermediate filaments may compensate for the lack of myotilin.</p&gt;}, number={4}, journal={Upsala Journal of Medical Sciences}, author={OCHALA JULIEN and CARPÉN OLLI and LARSSON LARS}, year={2009}, month={Nov.}, pages={235–241} }