Myofibrillar myopathies.
OBJECTIVE
The aim of this communication is to provide an up-to-date overview of myofibrillar myopathies (MFMs).


RESULTS
The most important recent advance in the MFMs has been the identification of mutation in Bag3 (Bcl-2-associated athanogene-3) as a new cause of MFM. Although, the typical clinical manifestations of MFMs are slowly progressive weakness, the patients with Bag3opathy may have had a rapidly progressive and more severe phenotype.


CONCLUSIONS
Several MFM disease genes have recently been recognized. The identified disease proteins (desmin, alphaB-crystallin, myotilin, Zasp, filamin C, and Bag3) interact with components or with chaperones of the Z-disk. In each case the molecular defect leads to a largely stereotyped cascade of structural perturbation of the muscle fiber architecture.
Selcen
Duygu
D
Department of Neurology, Division of Child Neurology and Neuromuscular Disease Research Laboratory, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA. Selcen.duygu@mayo.edu
D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism; D000818:Animals; D003459:Crystallins / Q000235:genetics / Q000378:metabolism; D003893:Desmin / Q000235:genetics / Q000378:metabolism; D006801:Humans; D060588:LIM Domain Proteins; D018485:Muscle Fibers, Skeletal / Q000473:pathology / Q000502:physiology; D009124:Muscle Proteins / Q000235:genetics; D009135:Muscular Diseases / Q000235:genetics / Q000473:pathology / Q000503:physiopathology; D009154:Mutation; D009210:Myofibrils / Q000473:pathology / Q000502:physiology
D048868:Adaptor Proteins, Signal Transducing; D003459:Crystallins; D003893:Desmin; C120696:LDB3 protein, human; D060588:LIM Domain Proteins; D009124:Muscle Proteins