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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Muscle phosphofructokinase deficiency: abnormal polysaccharide in a case of late-onset myopathy.

A 61-year-old woman with muscle phosphofructokinase ( PFK) deficiency had mild limb weakness all her life but no cramps or myoglobinuria. For 5 years the limb weakness progressed. In muscle, PFK activity was 1% of normal and glycogen concentration was elevated (2.13%). By light microscopy, a minor component of the accumulated glycogen appeared as PAS-positive, diastase-resistant inclusions in 10% of muscle fibers. The inclusions had a filamentous fine structure that resembled the abnormal long-chain glycogen of brancher enzyme deficiency. Iodine absorption spectra of both the inclusions and a diastase-resistant fraction of isolated glycogen resembled amylopectin. The abnormal polysaccharide in PFK deficiency may be related to greatly elevated concentration of muscle glucose-6-phosphate, an activator of the chain-elongating enzyme glycogen synthase.[1]

References

  1. Muscle phosphofructokinase deficiency: abnormal polysaccharide in a case of late-onset myopathy. Hays, A.P., Hallett, M., Delfs, J., Morris, J., Sotrel, A., Shevchuk, M.M., DiMauro, S. Neurology (1981) [Pubmed]
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