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At least 415 records · Page 23Linked to original sources
PubMed1971

Studies on type II glycogenosis. Effects of cortisone derivatives on acid -glucosidase.

Cortisone causes a marked increase in the activity of liver acid alpha-glucosidase 2h after injection into male Wistar rats. Studies on rat liver tissue slices, isolated lysosomes and cultured skin fibroblasts have demonstrated similar elevations of acid alpha-glucosidase activity after incubation with cortisone. Cortisone-treated human liver tissue, obtained by needle biopsy, also shows an increase in acid alpha-glucosidase activity. Neutral alpha-glucosidase activity was not stimulated by cortisone in vivo or in liver slices.

Acid Phosphatase↗
PubMed2000

Fetal-onset severe skeletal muscle glycogenosis associated with phosphorylase-b kinase deficiency.

We report on a premature newborn girl delivered after 32 weeks of gestation by cesarean section after sparse limb movements, fetal tachycardia and late heart rate decelerations had suggested fetal distress. Following 1 day of mechanical ventilation, adequate pulmonary gas exchange was achieved by spontaneous breathing. Main symptoms were virtually complete absence of spontaneous movements, increased flexor tonus of the extremities, and hypotonia of the trunk. Inability to suck or swallow required nasogastric gavage feeding. There were no hypoglycemic episodes. Echocardiography revealed normal myocardial function. Creatine kinase was 237 U/I at 2 days of life, declining to normal values thereafter. Muscle biopsy revealed increased glycogen storage with subsarcolemmal glycogen deposits and low phosphorylase-a activity while total phosphorylase was normal after in vitro activation, suggestive of phosphorylase-b kinase deficiency. No mutation was detected in exon 1 of the myophosphorylase gene. No psychomotor development was observed, and the infant died of central apnea at 3 months of age.

Adult↗
PubMed1999

[Differential diagnosis in anorexia nervosa: glycogenosis II (the Pompe type)].

HISTORY AND ADMISSION FINDINGS: A 29-year-old woman had since early childhood been smaller and thinner than her contemporaries. Her weight was now 36.5 kg, height 158 cm. Anorexia nervosa being suspected she was to be admitted to a psychosomatic clinic. A few days before the date she developed respiratory failure which required mechanical ventilation for a month. Physical examination revealed markedly reduced musculature. INVESTIGATIONS: Muscle biopsy and fibroblast culture indicated acid maltase deficiency (glycogen storage disease Type II [Pompe's disease]). Lung functions were markedly reduced, blood gas analysis revealing global respiratory insufficiency. TREATMENT AND COURSE: Intermittent patient-controlled ventilation (at night by intermittent positive pressure ventilation) clearly improved both her general condition and blood gases. CONCLUSIONS: Acid maltase deficiency should be included as a possible cause of the differential diagnosis of anorexia nervosa. This diagnosis should strictly follow the criteria listed in ICD-10 (International Classification of Diseases), but also after exclusion of other causes.

Adult↗
PubMed1998

Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI.

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.

Amino Acid Sequence↗
PubMed1991

Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele.

The lysosomal enzyme acid alpha glucosidase (GAA) or acid maltase is deficient in glycogen storage disease type II. We sought to determine the molecular basis for the disease in an adult-onset patient, unusual for very low enzyme activity similar to that seen with the infantile-onset form and with a previously reported defect in phosphorylation. We constructed cDNA and genomic DNA libraries from the patient's cell line (GM 1935) and determined the nucleotide sequence of the coding region. There were three base-pair substitutions in one allele (C1935 to A; G2446 to A and C2780 to T), all predicting amino acid changes (Asp-645 to Glu; Val-816 to Ile and Thr-927 to Ile). To determine which of the three base-pair substitutions resulted in loss of enzyme activity, we next utilized primer-directed mutagenesis and transient gene expression in an SV40-immortalized GAA-deficient fibroblast cell line. Only the construct containing the G2446 to A mutation (Val-816 to Ile) lost GAA enzyme activity, while the other two substitutions (including the Thr-927 to Ile change that predicts a loss of a potential site for N-linked glycosylation and mannose phosphorylation) each resulted in enzyme activity equal to the control. Analysis of RFLPs in genomic DNA, as well as sequence analysis for the three base-pair alterations, indicated that the patient was a genetic compound. We next digested PCR-amplified cDNA (reverse-transcribed from RNA) with Aat II to detect the base-pair 1935 substitution and found that virtually all of the mRNA was derived from the allele with the three base-pair substitutions.(ABSTRACT TRUNCATED AT 250 WORDS)

Alleles↗
PubMed1992

Preparation of monoclonal antibodies against acid alpha-D-glucosidase for study of Chinese glycogenosis type II patients.

Two monoclonal antibodies (Mabs), 8-23 and 4-6, against human acid alpha-D-glucosidase were generated to analyse the intracellular alpha-D-glucosidase from seven Chinese Pompe's disease families with the following study design: [1] Purified alpha-D-glucosidase from normal human urine was used as antigen for immunization of mice. [2] The splenic cells of immunized mice were isolated and fused with myeloma cells NS-1 for generation of hybridomas and production of anti-human alpha-D-glucosidase Mabs and detection of presence of the enzyme in skin fibroblasts obtained from the Pompe's disease families and normal controls. [3] Functional assay of acid alpha-D-glucosidase was done. Both generated Mabs were IgG1 with a kappa light chain. Mabs 8-23 and 4-6 can recognize 70 kd (kilodaltons) alpha-D-glucosidase evidenced by radioimmunoprecipitation (RIP). Our results showed that alpha-D-glucosidase did exist in the skin fibroblasts of all seven Pompe's disease patients by RIP and in the hepatic cells by immunohistological study. However, functional assay of alpha-D-glucosidase of the seven patients with Pompe's disease showed that the enzyme function of alpha-D-glucosidase was defective. This finding is at variance with the results of other workers which indicated that the amount of mature enzyme was reduced or totally absent in most of the juvenile and adult Caucasian and South African patients. The discordance may imply that the cause of alpha-D-glucosidase deficiency in Chinese patients is quite different from that in Caucasian and South African patients. This needs further study to clarify.

Animals↗
PubMed1994

Human muscle glycogenosis due to phosphorylase kinase deficiency associated with a nonsense mutation in the muscle isoform of the alpha subunit.

Heritable phosphorylase kinase (Phk) deficiency is responsible for several forms of glycogen storage disease in humans and animals that differ in mode of inheritance and tissue-specificity. Mutations affecting different subunits and isoforms of Phk are expected to contribute to this heterogeneity. In the present study, we have investigated a case of muscle-specific, adult-onset Phk deficiency. The coding sequences of three candidate genes were analyzed by RT-PCR and sequencing: the muscle isoform of the alpha subunit (alpha M), a muscle-specifically expressed exon of the beta subunit, and the muscle isoform of the gamma subunit. Whereas the latter two sequences were found to be normal, we identified a nonsense mutation in alpha M. The condition of this patient therefore is a human homolog of the X-linked muscle Phk deficiency of I-strain mice. To our knowledge, this is the first description of a human Phk deficiency mutation.

Amino Acid Sequence↗
PubMed1997

Autosomal glycogenosis of liver and muscle due to phosphorylase kinase deficiency is caused by mutations in the phosphorylase kinase beta subunit (PHKB).

Glycogen storage disease due to phosphorylase kinase deficiency occurs in several variants that differ in mode of inheritance and tissue-specificity. This heterogeneity is suspected to be largely due to mutations affecting different subunits and isoforms of phosphorylase kinase. The gene of the ubiquitously expressed beta subunit, PHKB, was a candidate for involvement in autosomally transmitted phosphorylase kinase deficiency of liver and muscle. To identify such mutations, the complete PHKB coding sequence was amplified by RT-PCR of RNA isolated from blood samples of patients and analyzed by direct sequencing of PCR products. The characterization of mutations was complemented by PCR of genomic DNA. In one female and four male patients, we identified five independent nonsense mutations (Y418ter; R428ter; Y974H+E975ter; Q656ter in two cases), one single-base insertion in codon N421, one splice-site mutation affecting exon 31, and a large deletion involving the loss of exon 8. Although these severe translation-disrupting mutations occur in constitutively expressed sequences of the only known beta subunit gene of phosphorylase kinase, PHKB, they are associated with a surprisingly mild clinical phenotype, affecting virtually only the liver, and relatively high residual enzyme activity of approximately 10%.

Adolescent↗