Maintenance of muscle mass, fiber size, and contractile function in mice lacking the Z-disc protein myotilin
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Maintenance of muscle mass, fiber size, and contractile function in mice lacking the Z-disc protein myotilin. / Ochala, Julien; Carpn, Olli; Larsson, Lars.
I: Upsala Journal of Medical Sciences, Bind 114, Nr. 4, 2009, s. 235-241.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Maintenance of muscle mass, fiber size, and contractile function in mice lacking the Z-disc protein myotilin
AU - Ochala, Julien
AU - Carpn, Olli
AU - Larsson, Lars
PY - 2009
Y1 - 2009
N2 - Background. 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. Methods. Skeletal and cardiac muscles were collected from adult mice with a targeted deletion of myotilin (myo-/-) and wild-type animals (myo/). Results and conclusion. Similar skeletal and cardiac muscle weights were observed in myo-/- and myo / mice. At the muscle cell level, the size and force production of single membrane permeabilized fibers were identical between myo-/- and myo/ 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.
AB - Background. 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. Methods. Skeletal and cardiac muscles were collected from adult mice with a targeted deletion of myotilin (myo-/-) and wild-type animals (myo/). Results and conclusion. Similar skeletal and cardiac muscle weights were observed in myo-/- and myo / mice. At the muscle cell level, the size and force production of single membrane permeabilized fibers were identical between myo-/- and myo/ 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.
KW - Muscle
KW - Myotilin
KW - Single membrane permeabilized muscle fiber
KW - Telethonin
UR - http://www.scopus.com/inward/record.url?scp=72449143629&partnerID=8YFLogxK
U2 - 10.3109/03009730903276399
DO - 10.3109/03009730903276399
M3 - Journal article
C2 - 19878039
AN - SCOPUS:72449143629
VL - 114
SP - 235
EP - 241
JO - Upsala Journal of Medical Sciences, Supplement
JF - Upsala Journal of Medical Sciences, Supplement
SN - 0300-9726
IS - 4
ER -
ID: 245665197