Relevant bibliographies by topics / Pompe disease; substrate localisation

Academic literature on the topic 'Pompe disease; substrate localisation'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Pompe disease; substrate localisation"

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Preisler, Nicolai, Pascal Laforêt, Karen Lindhardt Madsen, Edith Husu, Christoffer Rasmus Vissing, Gitte Hedermann, Henrik Galbo, Christopher Lindberg, and John Vissing. "Skeletal muscle metabolism during prolonged exercise in Pompe disease." Endocrine Connections 6, no. 6 (August 2017): 384–94. http://dx.doi.org/10.1530/ec-17-0042.

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Objective Pompe disease (glycogenosis type II) is caused by lysosomal alpha-glucosidase deficiency, which leads to a block in intra-lysosomal glycogen breakdown. In spite of enzyme replacement therapy, Pompe disease continues to be a progressive metabolic myopathy. Considering the health benefits of exercise, it is important in Pompe disease to acquire more information about muscle substrate use during exercise. Methods Seven adults with Pompe disease were matched to a healthy control group (1:1). We determined (1) peak oxidative capacity (VO2peak) and (2) carbohydrate and fatty acid metabolism during submaximal exercise (33 W) for 1 h, using cycle-ergometer exercise, indirect calorimetry and stable isotopes. Results In the patients, VO2peak was less than half of average control values; mean difference −1659 mL/min (CI: −2450 to −867, P = 0.001). However, the respiratory exchange ratio increased to >1.0 and lactate levels rose 5-fold in the patients, indicating significant glycolytic flux. In line with this, during submaximal exercise, the rates of oxidation (ROX) of carbohydrates and palmitate were similar between patients and controls (mean difference 0.226 g/min (CI: 0.611 to −0.078, P = 0.318) and mean difference 0.016 µmol/kg/min (CI: 1.287 to −1.255, P = 0.710), respectively). Conclusion Reflecting muscle weakness and wasting, Pompe disease is associated with markedly reduced maximal exercise capacity. However, glycogenolysis is not impaired in exercise. Unlike in other metabolic myopathies, skeletal muscle substrate use during exercise is normal in Pompe disease rendering exercise less complicated for e.g. medical or recreational purposes.
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Dajnoki, Angéla, Adolf Mühl, György Fekete, Joan Keutzer, Joe Orsini, Victor DeJesus, X. Kate Zhang, and Olaf A. Bodamer. "Newborn Screening for Pompe Disease by Measuring Acid α-Glucosidase Activity Using Tandem Mass Spectrometry." Clinical Chemistry 54, no. 10 (October 1, 2008): 1624–29. http://dx.doi.org/10.1373/clinchem.2008.107722.

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Abstract background: Pompe disease, caused by the deficiency of acid α-glucosidase (GAA), is a lysosomal storage disorder that manifests itself in its most severe form within the first months of life. Early detection by newborn screening is warranted, since prompt initiation of enzyme replacement therapy may improve morbidity and mortality. We evaluated a tandem mass spectrometry (MS/MS) method to measure GAA activity for newborn screening for Pompe disease. methods: We incubated 3.2-mm punches from dried blood spots (DBS) for 22 h with the substrate [7-benzoylamino-heptyl)-{2-[4-(3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-phenylcarbamoyl]- ethyl}-carbamic acid tert-butyl ester] and internal standard [7-d5-benzoylamino-heptyl)-[2-(4-hydroxy-phenylcarbamoyl)-ethyl]-carbamic acid tertbutyl ester]. We quantified the resulting product and internal standard using MS/MS. We assessed inter- and intrarun imprecision, carryover, stability, and correlation between enzyme activities and hematocrit and punch location and generated a Pompe disease–specific cutoff value using routine newborn screening samples. results: GAA activities in DBS from 29 known Pompe patients were <2 μmol/h/L. GAA activities in routine newborn screening samples were [mean (SD)] 14.7 (7.2) μmol/h/L (n = 10 279, median 13.3, 95% CI 14.46–14.74 μmol/h/L) and in normal adult samples 9.3 (3.3) μmol/h/L (n = 229, median 9, 95% CI 8.88–9.72 μmol/h/L). GAA activity was stable for 28 days between 37 °C and −80 °C. Carryover could not be observed, whereas intrarun and interrun imprecision were <10%. The limit of detection was 0.26 μmol/h/L and limit of quantification 0.35 μmol/h/L. conclusions: The measurement of GAA activities in dry blood spots using MS/MS is suitable for high-throughput analysis and newborn screening for Pompe disease.
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Sista, Ramakrishna S., Allen E. Eckhardt, Tong Wang, Carrie Graham, Jeremy L. Rouse, Scott M. Norton, Vijay Srinivasan, et al. "Digital Microfluidic Platform for Multiplexing Enzyme Assays: Implications for Lysosomal Storage Disease Screening in Newborns." Clinical Chemistry 57, no. 10 (October 1, 2011): 1444–51. http://dx.doi.org/10.1373/clinchem.2011.163139.

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BACKGROUND Newborn screening for lysosomal storage diseases (LSDs) has been gaining considerable interest owing to the availability of enzyme replacement therapies. We present a digital microfluidic platform to perform rapid, multiplexed enzymatic analysis of acid α-glucosidase (GAA) and acid α-galactosidase to screen for Pompe and Fabry disorders. The results were compared with those obtained using standard fluorometric methods. METHODS We performed bench-based, fluorometric enzymatic analysis on 60 deidentified newborn dried blood spots (DBSs), plus 10 Pompe-affected and 11 Fabry-affected samples, at Duke Biochemical Genetics Laboratory using a 3-mm punch for each assay and an incubation time of 20 h. We used a digital microfluidic platform to automate fluorometric enzymatic assays at Advanced Liquid Logic Inc. using extract from a single punch for both assays, with an incubation time of 6 h. Assays were also performed with an incubation time of 1 h. RESULTS Assay results were generally comparable, although mean enzymatic activity for GAA using microfluidics was approximately 3 times higher than that obtained using bench-based methods, which could be attributed to higher substrate concentration. Clear separation was observed between the normal and affected samples at both 6- and 1-h incubation times using digital microfluidics. CONCLUSIONS A digital microfluidic platform compared favorably with a clinical reference laboratory to perform enzymatic analysis in DBSs for Pompe and Fabry disorders. This platform presents a new technology for a newborn screening laboratory to screen LSDs by fully automating all the liquid-handling operations in an inexpensive system, providing rapid results.
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Ullman, Julie C., Kevin T. Mellem, Yannan Xi, Terrence F. Satterfield, Tarunmeet Gujral, Rebeca Choy, Julian R. Homburger, et al. "Substrate reduction therapy for Pompe disease: Small molecule inhibition of glycogen synthase 1 in preclinical models." Molecular Genetics and Metabolism 135, no. 2 (February 2022): S122. http://dx.doi.org/10.1016/j.ymgme.2021.11.324.

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van Diggelen, O. P., L. F. Oemardien, N. A. M. E. van der Beek, M. A. Kroos, H. K. Wind, Y. V. Voznyi, D. Burke, M. Jackson, B. G. Winchester, and A. J. J. Reuser. "Enzyme analysis for Pompe disease in leukocytes; superior results with natural substrate compared with artificial substrates." Journal of Inherited Metabolic Disease 32, no. 3 (April 19, 2009): 416–23. http://dx.doi.org/10.1007/s10545-009-1082-3.

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Njeim, Mario, and Frank Bogun. "Selecting the Appropriate Ablation Strategy: the Role of Endocardial and/or Epicardial Access." Arrhythmia & Electrophysiology Review 4, no. 3 (2015): 184. http://dx.doi.org/10.15420/aer.2015.4.3.184.

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Percutaneous catheter ablation has emerged as an effective treatment modality for the management of ventricular tachycardia. Despite years of progress in this field, the role of epicardial mapping and ablation needs to be further refined. In this review, we discuss the relationship between the type of underlying heart disease and the location of the arrythmogenic substrate as it pertains to a procedural approach. We describe the contribution of preprocedural and intraprocedural diagnostic tools for the localisation of the arrhythmogenic substrate, with a special emphasis on cardiac MRI and electrophysiological mapping. In our opinion, the preferred approach to target ventricular tachycardia should depend on the patient’s underlying heart disease and the location of scar tissue, which can be best visualised using cardiac MRI.
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Clayton, Nicholas P., Carol A. Nelson, Timothy Weeden, Kristin M. Taylor, Rodney J. Moreland, Ronald K. Scheule, Lucy Phillips, Andrew J. Leger, Seng H. Cheng, and Bruce M. Wentworth. "Antisense Oligonucleotide-mediated Suppression of Muscle Glycogen Synthase 1 Synthesis as an Approach for Substrate Reduction Therapy of Pompe Disease." Molecular Therapy - Nucleic Acids 3 (January 2014): e206. http://dx.doi.org/10.1038/mtna.2014.57.

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Clayton, Nicholas P., Carol A. Nelson, Timothy Weeden, Kristin M. Taylor, Rodney J. Moreland, Ronald K. Scheule, Andrew J. Leger, Lucy Phillips, Seng H. Cheng, and Bruce M. Wentworth. "Antisense oligonucleotide-mediated suppression of muscle glycogen synthase 1 synthesis as an approach for substrate reduction therapy of Pompe disease." Molecular Genetics and Metabolism 114, no. 2 (February 2015): S32. http://dx.doi.org/10.1016/j.ymgme.2014.12.055.

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Tortorelli, Silvia, Coleman T. Turgeon, Dimitar K. Gavrilov, Devin Oglesbee, Kimiyo M. Raymond, Piero Rinaldo, and Dietrich Matern. "Simultaneous Testing for 6 Lysosomal Storage Disorders and X-Adrenoleukodystrophy in Dried Blood Spots by Tandem Mass Spectrometry." Clinical Chemistry 62, no. 9 (September 1, 2016): 1248–54. http://dx.doi.org/10.1373/clinchem.2016.256255.

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Abstract BACKGROUND Newborn screening for lysosomal storage disorders (LSD) has revealed that late-onset variants of these conditions are unexpectedly frequent and therefore may evade diagnosis. We developed an efficient and cost-effective multiplex assay to diagnose six LSDs and several peroxisomal disorders in patients presenting with diverse phenotypes at any age. METHODS Three 3-mm dried blood spot (DBS) punches were placed into individual microtiter plates. One disc was treated with a cocktail containing acid sphingomyelinase-specific substrate and internal standard (IS). To the second DBS we added a cocktail containing substrate and IS for β-glucosidase, acid α-glucosidase, α-galactosidase A, galactocerebrosidase, and α-L-iduronidase. The third DBS was extracted with methanol containing d4-C26 lysophosphatidylcholine as IS and stored until the enzyme plates were combined and purified by liquid–liquid and solid-phase extraction. The extracts were evaporated, reconstituted with the extract from the lysophosphatidylcholine plate, and analyzed by flow injection tandem mass spectrometry. RESULTS Reference intervals were determined by analysis of 550 samples from healthy controls. DBS from confirmed patients with 1 of the 6 LSDs (n = 33), X-adrenoleukodystrophy (n = 9), or a peroxisomal biogenesis disorder (n = 5), as well as carriers for Fabry disease (n = 17) and X-adrenoleukodystrophy (n = 5), were analyzed for assay validation. Prospective clinical testing of 578 samples revealed 25 patients affected with 1 of the detectable conditions. CONCLUSIONS Our flow injection tandem mass spectrometry approach is amenable to high-throughput population screening for Hurler disease, Gaucher disease, Niemann–Pick A/B disease, Pompe disease, Krabbe disease, Fabry disease, X-adrenoleukodystrophy, and peroxisomal biogenesis disorder in DBS.
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Lin, Na, Jingyu Huang, Sara Violante, Joseph J. Orsini, Michele Caggana, Erin E. Hughes, Colleen Stevens, et al. "Liquid Chromatography–Tandem Mass Spectrometry Assay of Leukocyte Acid α-Glucosidase for Post-Newborn Screening Evaluation of Pompe Disease." Clinical Chemistry 63, no. 4 (April 1, 2017): 842–51. http://dx.doi.org/10.1373/clinchem.2016.259036.

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Abstract BACKGROUND Pompe disease (PD) is the first lysosomal storage disorder to be added to the Recommended Uniform Screening Panel for newborn screening. This condition has a broad phenotypic spectrum, ranging from an infantile form (IOPD), with severe morbidity and mortality in infancy, to a late-onset form (LOPD) with variable onset and progressive weakness and respiratory failure. Because the prognosis and treatment options are different for IOPD and LOPD, it is important to accurately determine an individual's phenotype. To date, no enzyme assay of acid α-glucosidase (GAA) has been described that can differentiate IOPD vs LOPD using blood samples. METHODS We incubated 10 μL leukocyte lysate and 25 μL GAA substrate and internal standard (IS) assay cocktail for 1 h. The reaction was purified by a liquid–liquid extraction. The extracts were evaporated and reconstituted in 200 μL methanol and analyzed by LC-MS/MS for GAA activity. RESULTS A 700-fold higher analytical range was observed with the LC-MS/MS assay compared to the fluorometric method. When GAA-null and GAA-containing fibroblast lysates were mixed, GAA activity could be measured accurately even in the range of 0%–1% of normal. The leukocyte GAA activity in IOPD (n = 4) and LOPD (n = 19) was 0.44–1.75 nmol · h−1 · mg−1 and 2.0–6.5 nmol · h−1 · mg−1, respectively, with no overlap. The GAA activity of pseudodeficiency patients ranged from 3.0–28.1 nmol · h−1 · mg−1, showing substantial but incomplete separation from the LOPD group. CONCLUSIONS This assay allows determination of low residual GAA activity in leukocytes. IOPD, LOPD, and pseudodeficiency patients can be partially differentiated by measuring GAA using blood samples.
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Dissertations / Theses on the topic "Pompe disease; substrate localisation"

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Turner, Christopher Travis. "Substrate localisation as a therapeutic option for Pompe disease." Thesis, 2014. http://hdl.handle.net/2440/91780.

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Pompe disease is a progressive form of muscular dystrophy caused by a deficiency in the lysosomal enzyme α-glucosidase (GAA). GAA catabolises glycogen and its deficiency leads to glycogen accumulation in the vesicular network of affected cells. Multiple therapies exist to treat Pompe disease but these are not completely effective (Winkel et al., 2003), necessitating the development of new therapeutic strategies. A number of enzymes that reside outside of the lysosome, either in the cytoplasm (Watanabe et al., 2008) or in circulation (Ugorski et al., 1983), can catabolise glycogen. It was postulated that if vesicular glycogen in Pompe cells was transferred out of these compartments it could then be alternatively degraded. The ability to remove vesicular glycogen from Pompe cells may reduce the onset/progression of the disorder, providing a therapeutic option for patients. Exocytosis is a ubiquitous cellular mechanism where intracellular vesicles fuse with the cell surface and permit vesicle content to be released from the cell. It was postulated that exocytosis may provide a mechanism to release accumulated glycogen from Pompe cells. Approximately 4% of vesicular glycogen was exocytosed from Pompe skin fibroblasts after 2 hrs in culture. Pompe cells exocytosed 2.7-fold more glycogen than unaffected cells. A cellular mechanism was therefore identified that had the capacity to release glycogen from Pompe cells. Culture conditions can alter the amount of exocytosis in fibroblasts (Martinez et al., 2000). In this study the effect of cell confluence and components of the culture media on lysosomal exocytosis was examined in Pompe skin fibroblasts. Increasing the extracellular concentration of Ca²⁺ led to a 1.4-fold increase in glycogen release compared to cells cultured in standard media conditions. Culture confluence had a key influence on glycogen exocytosis, with sub-confluent Pompe cells releasing >80% of glycogen after 2 hrs in culture, 35-fold higher than confluent cells. Exocytic mechanisms therefore exist that allow up-regulation of glycogen exocytosis in Pompe skin fibroblasts. A number of pharmacological compounds induce exocytosis in cultured cells (Amatore et al., 2006). Pompe skin fibroblasts treated with three compounds; calcimycin, lysophosphatidylcholine and α-L-iduronidase, each demonstrated a ≥ 1.5-fold increase in glycogen exocytosis, when compared to untreated Pompe controls. Calcimycin was the most effective compound for inducing glycogen exocytosis, with 12% released after 2 hrs of treatment, but confluent Pompe cells released less than that observed from sub-confluent Pompe cells. This difference in glycogen release may have resulted from the induction of different exocytic mechanisms. Complete exocytosis, where the vesicle completely fuses with the cell surface and releases all vesicle content, is induced in sub-confluent Pompe cells. In contrast, cavicapture, involving only a partial pore opening and limited vesicle content release, is induced in response to calcimycin treatment. The identification of a compound capable of inducing complete exocytosis may therefore improve glycogen release from Pompe cells. Taken together, natural glycogen exocytosis and the ability to induce glycogen exocytosis with pharmacological compounds provided proof-of-concept for exocytic induction as a strategy to re-locate accumulated glycogen from Pompe cells, potentially providing a new therapeutic option for the disorder.
Thesis (Ph.D.) -- University of Adelaide, School of Paediatrics and Reproductive Health, 2014
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