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Muscle phosphofructokinase deficiency

Abnormal polysaccharide in a case or late-onset myopathy

Division of Neuropathology Department of Pathology and Department of Neurology, Columbia Presbyterian Medical Center (Drs. Hays, Shevchuk, and DiMauro), New York, NY, and the Departments of Neurology and Pathology Harvard Medical School and the Brigham and Women's Hospital (Drs. Hallett, Morris, Sotrel, and Delfs), Boston, MA.

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.

Address correspondence and reprint requests to Dr. Hays, Division of Neuropathology, College of Physicians and Surgeons, 630 West 168th Street, New York. NY 10032.

Presented in part at the thirty-second annual meeting of the American Academy of Neurology, New Orleans, LA, May 1980.

Supported by Center Grants from the National Institute of Neurological and Communicative Disorders and Stroke (No. NS-11766-06) and from the Muscular Dystrophy Association, and by grant No. AM-25599-02 from the National Institute of Arthritis, Metabolism and Digestive Disease.

Accepted for publication December 16, 1980.

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