Chronic Progressive Myopathy With Myoglobinuria: Demonstration of a Glycogenolytic Defect in the Muscle*

Schmid, Rudi; Mahler, Robert

doi:10.1172/jci103983

Cited by 296 publications

(80 citation statements)

References 30 publications

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“…and D.M.R.) are heterozygotes, there is a striking similarity between their clinical presentation and those symptoms frequently reported for the early stages of classical McArdle's disease (1)(2)(3)(4)(5). Both, and in particular D.M.R., have begun to show some evidence ofexercise intolerance, while S.D.R.…”

Section: Resultssupporting

confidence: 51%

“…McArdle's disease is primarily an autosomal recessive disorder causing decreased exercise tolerance due to total absence ofskeletal muscle phosphorylase (1)(2)(3)(4)(5). The etiology of the disease is clearly complex, as evidenced by variation in age of onset (1)(2)(3)(4)(5)(6)(7), levels of skeletal muscle glycogen (4,8), differences in inheritance patterns (3,9) and severity of symptoms (1)(2)(3)(4)(5)8), as well as the presence or absence of immunoreactive catalytically inactive protein (10).…”

Section: Introductionmentioning

confidence: 99%

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McArdle's disease heterozygotes. Metabolic adaptation assessed using 31P-nuclear magnetic resonance.

Bogusky¹,

Taylor²,

Anderson³

et al. 1986

J. Clin. Invest.

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Two daughters of a propositus with documented McArdle's disease were shown by enzyme assay, gel electrophoresis, and immunoblotting to be partially deficient in skeletal muscle phosphorylase and, presumably, heterozygous for the trait. Both exhibited only the adult form of the skeletal muscle isozyme. By 31P-nuclear magnetic resonance, both heterozygotes showed a greater production of acid during fully aerobic exercise than when blood flow was occluded in ischemic exercise. This pattern is in contrast to that of control subjects, where there is significantly greater acid production in ischemic versus aerobic exercise, and distinct from that of phosphorylase-negative patients in which no acid is produced in either circumstance. We suggest that these heterozygotes may have adapted to their diminished phosphorylase by enhancing utilization of plasma glucose. If so, this mechanism could account for the observation that most of the symptoms of McArdle's disease are often manifest only in adulthood. These studies also show that although there are very high concentrations of phosphorylase in skeletal muscle (-2% of the soluble protein), such a high level is essential for normal muscle glycogenolysis.

show abstract

Section: Resultssupporting

confidence: 51%

Section: Introductionmentioning

confidence: 99%

McArdle's disease heterozygotes. Metabolic adaptation assessed using 31P-nuclear magnetic resonance.

Bogusky¹,

Taylor²,

Anderson³

et al. 1986

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…To test this hypothesis we performed microelectrode recordings of muscle sympathetic nerve activity (MSNA) during static exercise in patients with myophosphorylase deficiency (McArdle's disease), a condition in which contraction is not accompanied by glycogen degradation in exercising skeletal muscle (14)(15)(16).…”

Section: Introductionmentioning

confidence: 99%

Impairment of sympathetic activation during static exercise in patients with muscle phosphorylase deficiency (McArdle's disease).

Pryor¹,

Lewis²,

Haller³

et al. 1990

J. Clin. Invest.

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“…4). In five patients (2,5,6,9, and 10) no specific phosphorylase mRNA could be seen, whereas aldolase A mRNA was present.…”

Section: Resultsmentioning

confidence: 89%

Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis.

Gautron¹,

Daegelen²,

Mennecier³

et al. 1987

J. Clin. Invest.

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Lack of muscle glycogen phosphorylase activity leads to McArdle's disease, a rare metabolic myopathy. To investigate its molecular basis at the nucleic acid level, we isolated muscle phosphorylase cDNA clones from a human cDNA library in Escherichia coli plasmid pBR 322. Subcloning of one insertion of M13 bacteriophage permitted its definite identification by sequencing. Northern blot experiments revealed one specific messenger RNA of 3.4 kilobases found uniquely in tissues expressing muscle phosphorylase.We show that McArdle's disease exhibits a molecular heterogeneity at the messenger RNA level. In eight unrelated cases of McArdle's disease in which no inactive proteins had been detected, we assayed muscle biopsies for phosphorylase mRNA by Northern blotting. In five cases, no muscle phosphorylase mRNA could be detected, while in three other cases, normal length mRNA was present in lower amounts.Moreover, Southern blot analysis of DNA isolated from white blood cells in four McArdle patients revealed no major deletion or rearrangements of the phosphorylase gene as compared with controls.

show abstract

Chronic Progressive Myopathy With Myoglobinuria: Demonstration of a Glycogenolytic Defect in the Muscle*

Cited by 296 publications

References 30 publications

McArdle's disease heterozygotes. Metabolic adaptation assessed using 31P-nuclear magnetic resonance.

McArdle's disease heterozygotes. Metabolic adaptation assessed using 31P-nuclear magnetic resonance.

Impairment of sympathetic activation during static exercise in patients with muscle phosphorylase deficiency (McArdle's disease).

Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis.

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