Thin filament proteins mutations associated with skeletal myopathies: Defective regulation of muscle contraction
Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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Thin filament proteins mutations associated with skeletal myopathies : Defective regulation of muscle contraction. / Ochala, Julien.
I: Journal of Molecular Medicine, Bind 86, Nr. 11, 2008, s. 1197-1204.Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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TY - JOUR
T1 - Thin filament proteins mutations associated with skeletal myopathies
T2 - Defective regulation of muscle contraction
AU - Ochala, Julien
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
KW - Atrophy
KW - Congenital myopathies
KW - Muscle contraction
KW - Muscle weakness
KW - Thin filament proteins
U2 - 10.1007/s00109-008-0380-9
DO - 10.1007/s00109-008-0380-9
M3 - Review
C2 - 18574571
AN - SCOPUS:54249099032
VL - 86
SP - 1197
EP - 1204
JO - Journal of Molecular Medicine
JF - Journal of Molecular Medicine
SN - 0946-2716
IS - 11
ER -
ID: 245665265