Thin filament proteins mutations associated with skeletal myopathies: Defective regulation of muscle contraction |
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Authors: | Julien Ochala |
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Institution: | (1) Department of Neuroscience, Clinical Neurophysiology, University Hospital, Entrance 85, 3rd floor, SE-751 85 Uppsala, Sweden |
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Abstract: | In humans, more than 140 different mutations within seven genes (ACTA1, TPM2, TPM3, TNNI2, TNNT1, TNNT3, and NEB) that encode
thin filament proteins (skeletal α-actin, β-tropomyosin, γ-tropomyosin, fast skeletal muscle troponin I, slow skeletal muscle
troponin T, fast skeletal muscle troponin T, and nebulin, respectively) have been identified. These mutations have been linked
to muscle weakness and various congenital skeletal myopathies including nemaline myopathy, distal arthrogryposis, cap disease,
actin myopathy, congenital fiber type disproportion, rod-core myopathy, intranuclear rod myopathy, and distal myopathy, with
a dramatic negative impact on the quality of life. In this review, we discuss studies that use various approaches such as
patient biopsy specimen samples, tissue culture systems or transgenic animal models, and that demonstrate how thin filament
proteins mutations alter muscle structure and contractile function. With an enhanced understanding of the cellular and molecular
mechanisms underlying muscle weakness in patients carrying such mutations, better therapy strategies can be developed to improve
the quality of life. |
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Keywords: | Congenital myopathies Muscle weakness Atrophy Muscle contraction Thin filament proteins |
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