Use of platelets, mononuclear and polymorphonuclear cells in the diagnosis of glycogen storage disease type VI

Dahan, Nicole; Baussan, Christiane; Moatti, N.; Lemonnier, A

doi:10.1007/bf01800366

Cited by 11 publications

(1 citation statement)

References 14 publications

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“…Moreover, phosphorylase kinase deficiency is typically accompanied also by decreased total phosphorylase activity (Lederer et al 1975;Maire et al 1991). Determination of phosphorylase activity can be performed in leukocytes and other peripheral blood cells, but the L, B, and M isoforms seem to be expressed in different proportions in different blood cell types (Koster et al 1976;Dahan et al 1988), and details of blood-cell fractionation may influence the possibility of detecting a deficiency of the L isoenzyme (see data on patients 2 and 3, in the Subjects, Material, and Methods section above). Some laboratories therefore consider it necessary to perform a liver biopsy to establish the diagnosis, and the possibility of being able to identify PYGL mutations from blood RNA or DNA may help to avoid such biopsies.…”

Section: Discussionmentioning

confidence: 99%

Mutations in the Liver Glycogen Phosphorylase Gene (PYGL) Underlying Glycogenosis Type VI (Hers Disease)

Burwinkel

Bakker

Herschkovitz

et al. 1998

The American Journal of Human Genetics

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Deficiency of glycogen phosphorylase in the liver gives rise to glycogen-storage disease type VI (Hers disease; MIM 232700). We report the identification of the first mutations in PYGL, the gene encoding the liver isoform of glycogen phosphorylase, in three patients with Hers disease. These are two splice-site mutations and two missense mutations. A mutation of the 5' splice-site consensus of intron 14 causes the retention of intron 14 and the utilization of two illegitimate 5' splice sites, whereas a mutation of the 3' splice-site consensus of intron 4 causes the skipping of exon 5. Two missense mutations, N338S and N376K, both cause nonconservative replacements of amino acids that are absolutely conserved even in yeast and bacterial phosphorylases. We also report corrections of the PYGL coding sequence, sequence polymorphisms, and a partial PYGL gene structure with introns in the same positions as in PYGM, the gene of the muscle isoform of phosphorylase. Our findings demonstrate that PYGL mutations cause Hers disease, and they may improve laboratory diagnosis of deficiencies of the liver phosphorylase system.

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Section: Discussionmentioning

confidence: 99%

Mutations in the Liver Glycogen Phosphorylase Gene (PYGL) Underlying Glycogenosis Type VI (Hers Disease)

Burwinkel

Bakker

Herschkovitz

et al. 1998

The American Journal of Human Genetics

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Adult phosphorylase b kinase deficiency

Clemens

Yamamoto

Engel

1990

Annals of Neurology

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Phosphorylase b kinase deficiency affecting muscle has been observed infrequently in children with weakness and hepatomegaly, and in 2 adults with cramps on exertion. We observed 2 additional adults with phosphorylase b kinase deficiency: Patient 1, aged 58, had progressive, predominantly distal weakness since age 46 but no cramps on exertion; Patient 2, aged 26, had cramps on exertion since age 6 but no weakness. Lactate production on ischemic exercise was impaired only in Patient 1. The serum creatine kinase level was elevated in both. Muscle specimens showed focal glycogen excess in both, and a necrotizing myopathy and mild denervation atrophy in Patient 1. Muscle phosphorylase b kinase activity was 0.5% and 8.9% of the lowest control value in Patients 1 and 2, respectively; erythrocyte phosphorylase b kinase activity was normal in both; liver phosphorylase b kinase activity, measured in Patient 1, was also normal. Other glycolytic enzymes in muscle were preserved in both.

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