Glycogenosis Due to Liver and Muscle Phosphorylase Kinase Deficiency

Bashan, N; Iancu, Theodore C.; Lerner, Aaron; Fraser, Drora; Potashnik, R.; Moses, Shimon

doi:10.1203/00006450-198104000-00002

Cited by 30 publications

(7 citation statements)

References 11 publications

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“…Huijing (1975) suggested that cases of a human Xqinked muscle phosphorylase kinase deficiency might have been overlooked and falsely included in the GSD V group, which shows a preponderance of males. Recently, a human family with liver as well as muscle phosphorylase kinase deficiency was described, the disorder apparently not being sexlinked (Bashan et al, 1981). In muscle tissue of infant I strain mice phosphorylase kinase activity is present but low .…”

Section: Gsd VIIImentioning

confidence: 99%

Glycogen storage diseases in animals and their potential value as models of human disease

Walvoort

1982

J of Inher Metab Disea

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Glycogen storage diseases (GSD) are inborn errors of glycogen metabolism. Of the eight human GSD types in which the enzymatic deficiency has been identified, spontaneous animal counterparts have been reported for GSD I (glucose-6-phosphatase deficiency) in the mouse, for GSD II (acid alpha-glucosidase deficiency) in the dog, in cattle and in the quail, for GSD III (debrancher enzyme deficiency) in the dog and for GSD VIII (phosphorylase kinase deficiency) in the rat and the mouse. Experimentally induced GSD-like conditions have been described in the rat (Acarbose-induced GSD II-like conditions, iodoacetate-induced symptoms of myophosphorylase (GSD V) and myophosphofructokinase (GSD VII) deficiency) and the chicken (ochratoxin A-induced symptoms of cyclic AMP-dependent protein kinase deficiency). Enzymatic defects that are typical of the human GSD types have not been clearly identified in the induced animal conditions. The homology of animal and human GSD types is discussed. It is concluded that clinical, pathogenic and therapeutic studies of GSD may benefit from the use of animal models. For genetic studies of human GSD these models may prove to be of limited value, as the picture of several human GSD types is already obscured by genetic heterogeneity.

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Section: Gsd VIIImentioning

confidence: 99%

Glycogen storage diseases in animals and their potential value as models of human disease

Walvoort

1982

J of Inher Metab Disea

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“…The enzyme is a tetramer, the asubunit being encoded on the X chromosome and the ß-subunit on chromosome 16 (39). An X-linked type of phosphorylase kinase deficiency affects only the liver and is supposedly caused by a mutation of the PHKA locus, whereas in an autosomal recessive type, the enzyme activity is found to be low in liver, muscle, erythrocytes, and leukocytes (41). The fourth subunit is calmodulin.…”

Section: Defects In Carbohydrate Metabolismmentioning

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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“…reported up to now (Hug et al, 1966;Huijing, 1967;Bashan et al, 1981;Lerner et at., 1982;Abarbanel et al, 1986), erythrocyte PK in sex-linked liver PK-deficient patients show less than 10% of normal activity (Lederer et at., 1975), whereas a considerable degree of PK activity was retained in lymphocytes (Goji et al, 1985). Goji et al reported that PK in lymphocytes from patients with liver PK deficiency shows 40% of normal activity and that PK in lymphocytes might be an intermediate form between liver and muscle PK.…”

mentioning

confidence: 91%