Journal
NEUROMUSCULAR DISORDERS
Volume 16, Issue 11, Pages 782-791Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.nmd.2006.07.023
Keywords
myosin heavy chain mutation; skinned muscle fibers; in vitro motility; shortening velocity; specific tension
Categories
Funding
- NCRR NIH HHS [M01 RR010732] Funding Source: Medline
- NIAMS NIH HHS [R01 AR047318, AR47318, R01 AR045627, AR45627] Funding Source: Medline
Ask authors/readers for more resources
The pathogenic events leading to the progressive muscle weakness in patients with a E706K mutation in the head of the myosin heavy chain (MyHC) IIa were analyzed at the muscle cell and motor protein levels. Contractile properties were measured in single muscle fiber segments using the skinned fiber preparation and a single muscle fiber in vitro motility assay. A dramatic impairment in the function of the IIa MyHC isoform was observed at the motor protein level. At the single muscle fiber level, on the other hand, a general decrease was observed in the number of preparations where the specific criteria for acceptance were fulfilled irrespective of MyHC isoform expression. Our results provide evidence that the pathogenesis of the MyHC IIa E706K myopathy involves defective function of the mutated myosin as well as alterations in the structural integrity of all muscle cells irrespective of MyHC isoform expression. (C) 2006 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available