Incorporation of [14C]Glucose into α-1,4 Bonds of Glycogen by Leukocytes and Fibroblasts of Patients with Type III Glycogen Storage Disease

Gutman, Alisa; Barash, V.; Schramm, H; Deckelbaum, Richard J.; Granot, Esther; Aker, Memet; Kohn, Gertrude

doi:10.1203/00006450-198501000-00009

Cited by 9 publications

(3 citation statements)

References 8 publications

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“…Leukocytes were isolated from 20 ml of heparinized blood [21]; the final cell pellets were kept at -135°C and, at the time of analysis, were resuspended and sonicated as described previously [20]. Muscle homogenate (10%) and peripheral nerve homogenate (5%) were prepared in all-glass homogenizers in a medium containing 5 mM Tris, 1 mM ethylenediaminetetraacetic acid, and 5 mM mercaptoethanol, p H 7.2, and centrifuged at 10,000 g for 10 minutes.…”

Section: Tissue Preparation and Enzyme Assaysmentioning

confidence: 99%

Glycogen branching enzyme deficiency in adult polyglucosan body disease

Bruno

Servidei

Shanske

et al. 1993

Annals of Neurology

102

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Branching enzyme activity was assayed in muscle, peripheral nerve, and leukocytes from 2 Ashkenazi-Jewish patients with adult polyglucosan body disease and 1 African-American and 3 Caucasian patients with the same clinical and pathological features. Branching enzyme activity was normal in the muscle specimens from both Jewish and non-Jewish patients. However, the activity was markedly decreased not only in the leukocytes from the 2 Jewish patients (confirming previous findings), but also in peripheral nerve specimens, whereas it was normal in nerve tissue and leukocytes from all non-Jewish patients. These data confirm a branching enzyme deficiency in a subgroup of patients with adult polyglucosan body disease, and show that the defect is tissue-specific, suggesting that adult polyglucosan body disease has more than one biochemical basis.

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Section: Tissue Preparation and Enzyme Assaysmentioning

confidence: 99%

Glycogen branching enzyme deficiency in adult polyglucosan body disease

Bruno

Servidei

Shanske

et al. 1993

Annals of Neurology

102

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“…The reaction was carried out at 30°C and aliquots of 50 #1 were taken at 15, 30, 45 and 60min and spotted on Whatman ET-31 filter paper. The filter papers were washed with 66% ethanol as previously described (Gutman et al, 1985) and the precipitated radiactive glycogen was determined using a liquid scintillation spectrometer. Non-specific incorporation due to endogenous glycogen primer was measured in parallel with heat-inactivated tissue extract, and this activity was substracted from the total activity.…”

Section: Methodsmentioning

confidence: 99%

Apparent absence of glycogen branching enzyme activity in phosphofructokinase deficiency

Barash

Lilling

Fischer

et al. 1991

J of Inher Metab Disea

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A 30-year-old woman with clinical features and biochemical findings of muscle phosphofructokinase deficiency was found to have a very low level of alpha-1,4-glucan:alpha-1,4-glucan-6-transglucosylase (branching enzyme, EC 2.4.1.18) activity in muscle. In contrast, branching enzyme activity in the leukocytes was in the range of control values. After sedimentation of the glycogen from muscle homogenates by centrifugation at 105,000 g, branching enzyme activity in muscle of the patient was similar to that of control subjects. This patient illustrates the possibility of falsely diagnosing branching enzyme deficiency when muscle glycogen content is elevated. It is likely that such an artefact may also cause a false positive diagnosis of branching enzyme deficiency in other metabolic diseases associated with glycogen accumulation.

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“…Heterozygotes have an intermediate level of enzyme activity (Shin et al, 1984). However, in view of the numerous biochemical subtypes (van Hoof and Hers, 1967) as well as a type III glycogen storage disease case with normal enzyme activity in red cells (Gutman et al, 1985), it is recommended that other tissues should be investigated in clinically suspected cases which have normal activity in red cells. So far all our cases with this type of glycogen storage disease showed a deficient enzyme activity in red cells but their clinical features were rather variable.…”

Section: Diagnosis Of Various Glycogenosesmentioning

confidence: 99%

Diagnosis of glycogen storage disease

Shin

1990

J of Inher Metab Disea

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Glycogen storage diseases are associated with more than 15 different enzyme deficiencies and can be clinically divided mainly into two groups, those that affect primarily the liver and those that affect principally the muscle. In this report each glycogenosis has been clinically and biochemically documented and possibilities for an accurate and prompt diagnosis of the various types have been summarized. Most of the patients suffering from type II, type III, type IV and type VIa can easily be diagnosed by analysis of peripheral blood cells without the need for tissue biopsies. First trimester diagnosis using chorionic villi is feasible for severe forms of the glycogenoses, type IIa, type IIIa and type IV.

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Incorporation of [14C]Glucose into α-1,4 Bonds of Glycogen by Leukocytes and Fibroblasts of Patients with Type III Glycogen Storage Disease

Cited by 9 publications

References 8 publications

Glycogen branching enzyme deficiency in adult polyglucosan body disease

Glycogen branching enzyme deficiency in adult polyglucosan body disease

Apparent absence of glycogen branching enzyme activity in phosphofructokinase deficiency

Diagnosis of glycogen storage disease

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