Congenital nemaline myopathy. II. Quantitative changes in α‐actinin and myosin in skeletal muscle
I Stuhlfauth, FGI Jennekens, J Willemse… - Muscle & Nerve …, 1983 - Wiley Online Library
I Stuhlfauth, FGI Jennekens, J Willemse, BM Jockusch
Muscle & Nerve: Official Journal of the American Association of …, 1983•Wiley Online LibrarySkeletal muscle obtained from 2 patients with congenital nemaline myopathy (CNM) and
from a healthy control was analyzed by 1‐and 2‐dimensional gel electrophoresis. In total
extracts, an increase of α‐actinin by a factor of 2: 3 was found for CNM muscle as compared
with the control. One‐and two‐dimensional gels revealed the presence of LCF3, the
smallest light chain associated with type 2 (fast) myosin in total extracts of normal control of
mixed fiber type. Both CNM samples showed the absence of this polypeptide. This result is …
from a healthy control was analyzed by 1‐and 2‐dimensional gel electrophoresis. In total
extracts, an increase of α‐actinin by a factor of 2: 3 was found for CNM muscle as compared
with the control. One‐and two‐dimensional gels revealed the presence of LCF3, the
smallest light chain associated with type 2 (fast) myosin in total extracts of normal control of
mixed fiber type. Both CNM samples showed the absence of this polypeptide. This result is …
Abstract
Skeletal muscle obtained from 2 patients with congenital nemaline myopathy (CNM) and from a healthy control was analyzed by 1‐ and 2‐ dimensional gel electrophoresis. In total extracts, an increase of α‐actinin by a factor of 2:3 was found for CNM muscle as compared with the control. One‐ and two‐dimensional gels revealed the presence of LCF3, the smallest light chain associated with type 2 (fast) myosin in total extracts of normal control of mixed fiber type. Both CNM samples showed the absence of this polypeptide. This result is consistent with the finding that muscle of the 2 patients exhibited nearly exclusively the ATPase activity indicative of type 1 (slow) myosin.
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