Accumulation and assembly of myosin in hypertrophic cardiomyopathy with the 403 Arg to Gln beta-myosin heavy chain mutation.
The sarcomeric proteins and organization of cardiac myofibrils appeared intact in multiple unrelated patients with hypertrophic cardiomyopathy. In two subjects demonstrating the missense mutation at position 403 (Arg to Gln) in the beta-myosin heavy chain gene, total myosin and immunoreactive beta-myosin heavy chain levels were similar to those found in other patients with hypertrophic cardiomyopathy and various disease control subjects. No alteration in expression of the cardiac alpha-myosin heavy chain gene was observed. These results are consistent with the examined myosin heavy chain mutation, permitting proper accumulation and assembly of myosin while primarily impairing contractile function. The characteristic myocyte disarray would appear likely to be a secondary consequence of the mutations.
Vybiral
T
T
Department of Neurology, Baylor College of Medicine, Houston, Tex. 77030.
Deitiker
P R
PR
Roberts
R
R
Epstein
H F
HF
D000293:Adolescent; D000328:Adult; D000368:Aged; D002312:Cardiomyopathy, Hypertrophic / Q000235:genetics* / Q000378:metabolism / Q000503:physiopathology; D002648:Child; D005260:Female; D005455:Fluorescent Antibody Technique; D005796:Genes; D006801:Humans; D015151:Immunoblotting; D008297:Male; D008859:Microscopy, Polarization; D008875:Middle Aged; D009154:Mutation; D009200:Myocardial Contraction; D009206:Myocardium / Q000648:ultrastructure; D009210:Myofibrils / Q000502:physiology*; D009218:Myosins / Q000235:genetics* / Q000378:metabolism*
D009218:Myosins