Muscle in Lafora Disease

Publisher Website
Google Scholar
Abstract
Ultrastructural studies of muscle from a patient with Lafora disease showed sheets of glycogen particles and fine granular-filamentous material between myofibrils. These structures were frequently intermingled and stained intensely with silver proteinate, a specific stain for polysaccharides. Methods for isolation of glycogen yielded excessive hexose-releasing material. In chromatographic analysis of a hydrolysate of this material, glucose was the only component sugar. Compared with action on normal muscle glycogen, phosphorylase was ineffective, β-amylase 50% less effective, but α-amylase normally effective in degrading the Lafora polyglucosan. Incubation of muscle homogenate or isolated polyglucosan with a mixture of glucosidases capable of completely degrading normal glycogen (Diazyme) resulted in only 30% digestion of the Lafora polyglucosan. The metabolic error causing the accumulation of anomalous polysaccharide in this generalized storage disease remainsobscure.

This publication has 12 references indexed in Scilit: