Acid α-glucosidase deficiency in cultured fibroblasts with phenotype 2 of acid α-glucosidase

Beratis, Nicholas G.; Wilbur, Lorraine; Sklower, Susan L.

doi:10.1016/0009-8981(83)90179-1

Cited by 2 publications

(1 citation statement)

References 15 publications

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“…* Hypothetical homozygosity for the 2-allele was deduced from experiments in fibroblast cultures, where this form was found to be less active in glycogen' degradation (236,237). Based on enzyme kinetics and immunological detection of acid maltase in patients with acid maltase deficiency, Beratis defined three biochemical groups (235): a first group where an inactive enzyme protein is present, a second where no immunologically cross-reactive material is found and no residual enzyme activity can be detected, and a third group showing a reduced enzyme activity and a decreased amount of cross-reacting material.…”

Section: Acid Maltase Deficiencymentioning

confidence: 99%

Review

1991

Clinical Chemistry and Laboratory Medicine

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The inherited skeletal muscle diseases form a highly heterogeneous group of disorders covering single enzyme defects, complex metabolic disorders, storage diseases, dystrophies and malignant hyperthermia. Whereas these myopathies may be caused by a large number of different biochemical and genetic defects their clinical presentation by contrast is relatively monotonous, with only a few specific fmdings pointing to a particular molecular defect. This review of the biochemical and molecular genetic basis of these diseases concentrates on 1) disorders in fuel utilization and energy production, 2) disorders in structural integrity or mechanical function, and 3) disorders in contractility and electrophysiological properties of the muscle cell.The authors address the questions of organ-specificity and of a possible relationship between clinical, biochemical, and genetic heterogeneity of metabolic defects, and also try to present the current state of chromosome mappirig for such disorders.

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Section: Acid Maltase Deficiencymentioning

confidence: 99%

Review

1991

Clinical Chemistry and Laboratory Medicine

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Km mutant of acid α‐glucosidase in a case of cardiomyopathy without signs of skeletal muscle involvement

Suzuki¹,

Tsuji²,

Omura³

et al. 1988

Clinical Genetics

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A male patient is reported with a mutation of acid alpha-glucosidase causing an altered Km toward natural substrates. Cardiac arrhythmia was found at 12 years of age, and he died of heart failure at 15 years. No skeletal muscle involvement was observed either clinically or histologically. Acid alpha-glucosidase activity in fibroblasts was moderately low (43% of the control mean) with normal Km for 4-methylumbelliferyl alpha-D-glucoside. The hydrolysis of glycogen was markedly decreased (14% of the control mean), and the Km for maltose was increased 4-fold and for glycogen 5-fold. The biosynthesis and the posttranslational processing of the mutant enzyme appeared normal, but the total amount of the enzyme was lower than normal. This mutant enzyme comigrated with normal acid alpha-glucosidase on starch gel electrophoresis, and not with the rare isozyme, acid alpha-glucosidase 2. A possible role of this mutant enzyme in the pathogenesis of this disease and the relationship to glycogenesis II are discussed.

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Acid α-glucosidase deficiency in cultured fibroblasts with phenotype 2 of acid α-glucosidase

Cited by 2 publications

References 15 publications

Review

Review

Km mutant of acid α‐glucosidase in a case of cardiomyopathy without signs of skeletal muscle involvement

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