TY - JOUR
T1 - Mutations in the beta-tropomyosin (TPM2) gene - a rare cause of nemaline myopathy
AU - Donner, Kati
AU - Ollikainen, Miina
AU - Ridanpää, Maaret
AU - Christen, Hans-Jürgen
AU - Goebel, Hans H.
AU - de Visser, Marianne
AU - Pelin, Katarina
AU - Wallgren-Pettersson, Carina
PY - 2002
Y1 - 2002
N2 - Nemaline myopathy is a clinically and genetically heterogeneous muscle disorder. In the nebulin gene we have detected a number of autosomal recessive mutations. Both autosomal dominant and recessive mutations have been detected in the genes for alpha -actin and alpha -tropomyosin 3. A recessive mutation causing nemaline myopathy among the Old Order Amish has recently been identified in the gene for slow skeletal muscle troponin T. As linkage studies had shown that at least one further gene exists for nemaline myopathy, we investigated another tropomyosin gene expressed in skeletal muscle, the beta -tropomyosin 2 gene. Screening 66 unrelated patients, using single strand conformation polymorphism analysis and sequencing, we found four polymorphisms and two heterozygous missense mutations. Both mutations affect conserved amino acids, and in both cases, the mutant allele is expressed. We speculate that the observed mutations affect the formation of the tropomyosin dimer and its actin-binding properties. (C) 2002 Elsevier Science B.V. All rights reserved
AB - Nemaline myopathy is a clinically and genetically heterogeneous muscle disorder. In the nebulin gene we have detected a number of autosomal recessive mutations. Both autosomal dominant and recessive mutations have been detected in the genes for alpha -actin and alpha -tropomyosin 3. A recessive mutation causing nemaline myopathy among the Old Order Amish has recently been identified in the gene for slow skeletal muscle troponin T. As linkage studies had shown that at least one further gene exists for nemaline myopathy, we investigated another tropomyosin gene expressed in skeletal muscle, the beta -tropomyosin 2 gene. Screening 66 unrelated patients, using single strand conformation polymorphism analysis and sequencing, we found four polymorphisms and two heterozygous missense mutations. Both mutations affect conserved amino acids, and in both cases, the mutant allele is expressed. We speculate that the observed mutations affect the formation of the tropomyosin dimer and its actin-binding properties. (C) 2002 Elsevier Science B.V. All rights reserved
U2 - https://doi.org/10.1016/S0960-8966(01)00252-8
DO - https://doi.org/10.1016/S0960-8966(01)00252-8
M3 - Article
C2 - 11738357
SN - 0960-8966
VL - 12
SP - 151
EP - 158
JO - Neuromuscular disorders
JF - Neuromuscular disorders
IS - 2
ER -