Crystalloid bodies in skeletal muscle of hypothyroid myopathy. Ultrastructural and histochemical studies.

Crystalloid bodies in skeletal muscle fibers have been described in myopathic and non-myopathic conditions. They have been interpreted as viral, glycogen, protein-glycogen complex, artifacts and of unknown nature. This report described similar crystalloid bodies in the postmortem muscle samples of two patients with hypothyroid myopathy. The crystalloid bodies were preferentially located in the I band and Z line region and in the subsarcolemmal region closely associated with lipofuscin. Some were present within basophilic bodies. They were formed by parallel filaments of 6-10 nm beaded periodically by electron-dense particles of 10-18 nm in a lattice, hexagonal or parallel-ripple pattern. Merging of filaments of crystalloid bodies into actin filaments of the I band was noted. The electron-dense particles stained strongly with periodic acid-thiocarbohydrazide-silver proteinate method for polysaccharides and were unaffected or partially digested by diastase treatment on the ultrathin sections. The filamentous component was neither stained for polysaccharides nor digested by diastase treatment. It is suggested that crystalloid bodies of muscle fibers are composed of two distinct subunits with particles of glycogen complex attached to filaments of unknown nature.