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Pompe disease is a lysosomal storage disorder caused by the deficiency of acid alpha-glucosidase (EC. 3.2.1.20) due to mutations in human GAA gene.
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28 novel mutations were identified in the GAA gene in patients with late-onset Pompe disease. Patients carrying the c.-32-13T>G mutation had an older mean age at onset than patients without this mutation.
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Onset of symptoms including delay in achievement of gross motor milestones, signs of proximal muscle weakness, swallow and feeding difficulties, and sleep apnea in the first two years of life is not uncommon in individuals with late-onset Pompe disease and the c.-32-13T>G variant.
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PI-rhGAA may have the potential to be a useful therapeutic option for improving the treatment of Pompe disease.
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The most common mutation was c.-32-13T, G. in Pompe disease.
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The narrow substrate-binding pocket of rhGAA is located near the C-terminal ends of beta-strands of the catalytic (beta/alpha)8 domain and shaped by a loop from the N-terminal beta-sheet domain and both inserts I and II.
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This is the first study of rhGAA to differentiate M6P glycans and identify their attachment sites, despite rhGAA already being an approved drug for Pompe disease.
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GAA mutation is associated with Pompe disease.
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Enzyme activities (acid alpha-glucosidase (GAA), galactocerebrosidase (GALC), glucocerebrosidase (GBA), alpha-galactosidase A (GLA), alpha-iduronidase (IDUA) and sphingomyeline phosphodiesterase-1 (SMPD-1)) were measured on ~43,000 de-identified dried blood spot (DBS) punches, and screen positive samples were submitted for DNA sequencing to obtain genotype confirmation of disease risk
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enzyme replacement therapy (ERT) (alglucosidase alfa) stabilizes respiratory function and improves mobility and muscle strength in late-onset Pompe disease.Lysosomal glycogen in muscle biopsies from treatment-naive LOPD patients was reduced post-ERT (alglucosidase alfa).
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In adults with Pompe disease, antibody formation does not interfere with rhGAA efficacy in the majority of patients, is associated with IARs, and may be attenuated by the IVS1/delex18 GAA genotype
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Reanalysis of the patient's DNA sample using next generation sequencing (NGS) of a panel of target genes causing glycogen storage disorders demonstrated compound heterozygosity for a point mutation and an exonic deletion in the GAA gene.
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Thirteen novel and two common GAA mutations were identified in this study. The allelic frequency of c.2662G > T (p.Glu888X) was 23.1% in northern Chinese patients and 4.2% in southern Chinese patients, whereas the allelic frequency of c.1935C >A (p.Asp645Glu) was 20.8% in southern and 3.8% in northern Chinese patients.
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This is the first report of the alpha-glucosidase inhibitory activity of compounds 20, 26, and 29, and the findings support the important role of Eremanthus species as novel sources of new drugs and/or herbal remedies for treatment of type 2 diabetes.
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Compared with controls, GAA gene expression levels in coronary artery disease (CAD) patients were significantly increased, suggesting that GAA may be involved in the CAD development.
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Study reports on the clinical, biochemical, morphological, muscle imaging, and genetic findings of six adult Pompe patients from five unrelated families with the c.-32-13T>G GAA gene mutation in homozygous state. All patients had decreased GAA activity and elevated creatine kinase levels.
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glycogen storage disease type II is caused by deficiency of GAA activity resulting from mutation of GAA gene
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RT-PCR followed by DNA sequence analysis of patients with Pompe disease revealed new variant in GAA gene resulting in aberrant splicing event.
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Findings indicate that GAA c.2238G > C (p.W746C) novel mutation is the most common mutation in mainland Chinese late-onset Pompe patients, as observed in Taiwanese patients expanding the genetic spectrum of the disease.
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this study shows several alterations distributed along the GAA gene in a sample of Brazilian families.