Готові списки джерел за темами / Glycogen storage disease type III

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Добірка наукової літератури з теми "Glycogen storage disease type III"

Автор: Grafiati

Опубліковано: 14 грудня 2024

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Статті в журналах з теми "Glycogen storage disease type III"

Carvalho, Julene S., Eurem E. Matthews, James V. Leonard, and John Deanfield. "Cardiomyopathy of glycogen storage disease type III." Heart and Vessels 8, no. 3 (September 1993): 155–59. http://dx.doi.org/10.1007/bf01744800.

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Labrune, Philippe, Pascale Trioche, Isabelle Duvaltier, Paquita Chevalier, and Michel Odièvre. "Hepatocellular Adenomas in Glycogen Storage Disease Type I and III: A Series of 43 Patients and Review of the Literature." Journal of Pediatric Gastroenterology and Nutrition 24, no. 3 (March 1997): 276–79. http://dx.doi.org/10.1002/j.1536-4801.1997.tb00424.x.

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Background:Hepatocellular adenomas may develop in patients with glycogen storage disease types I and III, and the malignant degeneration of adenomas in hepatocellular carcinoma has been reported in ten cases. The aim of this work was to study the characteristics of hepatic adenomas in a large series of 43 patients with glycogen storage disease types I and III and to determine the optimal means of follow‐up.Methods:The charts of 43 patients with glycogen storage disease type I and III were studied. In all these patients, abdominal ultrasonography and the determination of serum α‐fetoprotein had been performed yearly and serum concentrations of several proteins were determined once.Results:51.8% of patients with type I and 25% of patients with type III glycogen storage disease had hepatic adenomas at the time of the study. The male to female ratio was 2 to 1 in type I, and no female had adenomas in type III. No evidence of malignant transformation was observed during the follow‐up period. Serum concentrations of several proteins were significantly higher in patients with hepatic adenomas than in patients without such lesions.Conclusions:In patients with glycogen storage disease type I and III, the determination of α‐fetoprotein serum concentration has to be combined with yearly hepatic ultrasound examinations. Other investigations such as CT scan should be considered when the size of any adenoma increases. The malignant transformation of hepatocellular adenoma into hepatocellular carcinoma remains a rare event.

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Shen, J., and Y. Chen. "Molecular Characterization of Glycogen Storage Disease Type III." Current Molecular Medicine 2, no. 2 (March 1, 2002): 167–75. http://dx.doi.org/10.2174/1566524024605752.

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Minen, Federico, Gabriele Cont, Angela De Cunto, Stefano Martelossi, Alessandro Ventura, Giuseppe Maggiore, Flavio Faletra, Paolo Gasparini, and Denise Cassandrini. "Delayed Diagnosis of Glycogen Storage Disease Type III." Journal of Pediatric Gastroenterology and Nutrition 54, no. 1 (January 2012): 122–24. http://dx.doi.org/10.1097/mpg.0b013e318228d806.

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Cleary, M. A., J. H. Walter, B. A. Kerr, and J. E. Wraith. "Facial appearance in glycogen storage disease type III." Clinical Dysmorphology 11, no. 2 (April 2002): 117–20. http://dx.doi.org/10.1097/00019605-200204000-00008.

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MOSES, S. W., N. GADOTH, N. BASHAN, E. BEN-DAVID, A. SLONIM, and K. L. WANDERMAN. "Neuromuscular Involvement in Glycogen Storage Disease Type III." Acta Paediatrica 75, no. 2 (March 1986): 289–96. http://dx.doi.org/10.1111/j.1651-2227.1986.tb10201.x.

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Korlimarla, Aditi, Stephanie Austin, Baodong Sun, and Priya Kishnani. "Hepatic Manifestations in Glycogen Storage Disease Type III." Current Pathobiology Reports 6, no. 4 (November 5, 2018): 233–40. http://dx.doi.org/10.1007/s40139-018-0182-x.

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Liu, Kai-Ming, Jer-Yuarn Wu, and Yuan-Tsong Chen. "Mouse model of glycogen storage disease type III." Molecular Genetics and Metabolism 111, no. 4 (April 2014): 467–76. http://dx.doi.org/10.1016/j.ymgme.2014.02.005.

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Salemi, Vera Maria Cury, Léa Maria Macruz Ferreira Demarchi, Estêvan Vieira Cabeda, Jaqueline Wagenführ, and Ana Cristina Tanaka. "Type III glycogen storage disease mimicking hypertrophic cardiomyopathy." European Heart Journal - Cardiovascular Imaging 13, no. 2 (November 14, 2011): 197. http://dx.doi.org/10.1093/ejechocard/jer231.

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Zimakas, P. J. A. "Glycogen storage disease type III in Inuit children." Canadian Medical Association Journal 172, no. 3 (February 1, 2005): 355–58. http://dx.doi.org/10.1503/cmaj.1031589.

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Дисертації з теми "Glycogen storage disease type III"

Vidal, Patrice. "Développement d'un traitement de thérapie génique pour la glycogénose de type III." Electronic Thesis or Diss., Sorbonne université, 2018. http://www.theses.fr/2018SORUS571.

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La glycogénose de type III (GSDIII) est une maladie génétique récessive due à des mutations affectant l’activité de l'enzyme de débranchement du glycogène (GDE). Les symptômes sont une hépatomégalie et une hypoglycémie chez l’enfant puis une faiblesse musculaire dégénérative chez l’adulte. Aucun traitement curatif n'existe pour GSDIII. Nous avons dans un premier temps développé un modèle de souris GSDIII viable possédant phénotype proche de la maladie de l’homme. La thérapie génique permet le traitement des maladies métaboliques et neuromusculaires. En thérapie génique in vivo, les vecteurs dérivés du virus adéno-associé (AAV) ont démontré leur efficacité chez l’homme. Une limitation dans le développement d'une thérapie génique pour la GSDIII est la taille du transgène qui dépasse la taille d’encapsidation de l'AAV. Nous avons exploré une approche alternative utilisant la voie lysosomale de la dégradation du glycogène par l’enzyme GAA. Les résultats chez les souris GSDIII montrent que l’augmentation de la quantité de GAA dans les muscles ne permet pas de traiter le phénotype de la GSDIII alors qu’au contraire elle induit une normalisation de la quantité du glycogène hépatique. La seconde étape fut de faire exprimer à nouveau la GDE par les cellules. Nous avons développé deux vecteurs pouvant utiliser les mécanismes de la recombinaison homologue. Cette stratégie a permis la correction du phénotype GSDIII dans le modèle murin de la maladie. Les résultats montrent qu’il est possible de corriger la faiblesse musculaire ainsi que l’accumulation de glycogène conduisant à la vacuolisation du tissu. L’efficacité de cette stratégie ne reste néanmoins que partielle dans le foie
Glycogen storage disease type III (GSDIII) is a recessive genetic disorder caused by mutations affecting the activity of the glycogen debranching enzyme (GDE). Symptoms are hepatomegaly and hypoglycemia during childhood and degenerative muscle weakness during adulthood. At present, no curative treatment exists for GSDIII. First, we developed and characterized a mouse model that faithfully recapitulates the human disease. Gene therapy allows the treatment of previously untreatable metabolic and neuromuscular diseases. Adeno-associated virus (AAV) vectors are vectors of choice for in vivo gene therapy, with an excellent safety and efficacy profile demonstrated in human. A major limitation for GSDIII is the size of the transgene that exceeds the genome packaging capacity of AAV vectors. We explored an alternative approach using the lysosomal pathway and the acid alpha-glucosidase (GAA) able to degrade the glycogen, overloading the lysosomes with this protein. In muscles, the increase of GAA activity is not able to treat the phenotype of GSDIII whereas the overexpression of GAA in the liver induces a normalization of the concentration of glycogen. The second step of this thesis was to have GDE de novo expressed in cells. We developed strategy based on the injection of two vectors that can use the mechanisms of homologous recombination. This allowed the correction of the GSDIII phenotype in a murine model of the disease. The results show that it is possible to correct the muscle phenotype of GSDIII. Nevertheless, the effectiveness of this strategy remains only partial in the liver, again highlighting a different glycogen degradation pathway in both tissues

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Rossiaud, Lucille. "Modélisation et compréhension de la glycogénose de type III grâce à l'utilisation de cellules souches pluripotentes induites humaines." Electronic Thesis or Diss., université Paris-Saclay, 2024. https://www.biblio.univ-evry.fr/theses/2024/interne/2024UPASL091.pdf.

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La glycogénose de type III (GSDIII) est une maladie génétique rare due à un déficit en enzyme débranchante du glycogène (GDE), provoquant une accumulation de glycogène dans le foie, le cœur et les muscles squelettiques. Alors que les atteintes hépatiques dominent durant l'enfance, les atteintes musculaires progressent et deviennent prédominantes à l'âge adulte. L'absence de modèles humains freine la compréhension de cette pathologie et la mise au point de traitements.Dans ce contexte, mon premier objectif était de créer des modèles pathologiques humains in vitro à partir de cellules souches pluripotentes induites (hiPSC). J'ai généré cinq lignées hiPSC pathologiques : quatre lignées dérivées de patients par reprogrammation et une lignée génétiquement modifiée par CRISPR/Cas9. Ces cellules ont ensuite été différenciées en myocytes et en hépatocytes, les deux types cellulaires pertinents pour l'étude de la GSDIII. J'ai confirmé que ces cellules expriment respectivement les marqueurs spécifiques des muscles et du foie, et récapitulent, en condition de privation de glucose, le phénotype d'accumulation de glycogène en comparaison à des cellules saines.Le deuxième objectif visait à mieux comprendre les mécanismes physiopathologiques de la GSDIII et à identifier de nouveaux biomarqueurs de la pathologie. Je me suis d'abord focalisée sur le muscle, pour lequel j'ai identifié, par séquençage ARN des myocytes dérivés d'hiPSC, des gènes différentiellement exprimés entre cellules saines et pathologiques. Une analyse comparative avec les données d'un séquençage ARN réalisés sur des biopsies de triceps de souris saines et GSDIII a révélé la surexpression d'un gène commun codant pour la Galectine-3, un marqueur de vésicules endommagées. Sa surexpression a été validée dans les myocytes mutés dérivés d'hiPSC, ainsi que dans les triceps de souris GSDIII et dans des biopsies de patients. En parallèle, une approche similaire sur les hépatocytes dérivés d'hiPSC a permis d'identifier de potentiels biomarqueurs du foie, ouvrant la voie à une meilleure compréhension des mécanismes physiopathologiques hépatiques. Le dernier objectif était d'utiliser ces modèles pathologiques humains in vitro pour tester de nouvelles thérapies. J'ai démontré que le traitement de myocytes mutés par des vecteurs AAV exprimant la GDE humaine complète ou tronquée, préalablement validés dans des modèles in vivo de souris et de rats GSDIII, diminuait l'accumulation de glycogène à des niveaux comparables à ceux de cellules saines. Ces expériences ont confirmé l'intérêt du développement de ces nouveaux modèles in vitro. L'ensemble de ces travaux ont permis l'identification de nouveaux biomarqueurs de la GSDIII, permettant d'améliorer la compréhension des mécanismes moléculaires dans le muscle et le foie. La création de ces nouveaux modèles in vitro ouvre également de nouvelles perspectives thérapeutiques pour la GSDIII, notamment en facilitant le criblage de médicaments
Glycogen storage disease type III (GSDIII) is a rare genetic disorder caused by glycogen debranching enzyme (GDE) deficiency, leading to an accumulation of glycogen accumulation in the liver, heart and skeletal muscles. While liver damages predominate in childhood, muscle impairments progress and become predominant in adulthood. The lack of human models hinders our understanding of the disease and the development of treatments.In this context, my first objective was to create in vitro human pathological models from induced pluripotent stem cells (hiPSCs). I generated five pathological hiPSC lines: four lines derived from patients by reprogramming and one line genetically modified by CRISPR/Cas9. These cells were then differentiated into myocytes and hepatocytes, the two relevant cell types for the study of GSDIII. I confirmed that these cells express muscle and liver specific markers respectively, and recapitulate the glycogen accumulation phenotype under glucose starvation conditions compared to healthy cells.The second objective was to better understand the pathophysiological mechanisms of GSDIII and to identify new biomarkers of the disease. I first focused on muscle, for which I identified genes differentially expressed between healthy and pathological cells by RNA sequencing of hiPSC-derived myocytes. Comparative analysis with RNA sequencing data from triceps biopsies of healthy and GSDIII mice revealed overexpression of a common gene encoding galectin-3, a marker of damaged vesicles. This overexpression was validated in mutated myocytes derived from hiPSCs, as well as in the triceps of GSDIII mice and in patient biopsies. In parallel, a similar approach on hiPSC-derived hepatocytes identified potential liver biomarkers, paving the way for a better understanding of the mechanisms of liver damage.The final objective was to use these in vitro human pathological models to test new therapies. I demonstrated that treatment of mutated myocytes with AAV vectors expressing complete or truncated human GDE, previously validated on in vivo GSDIII mouse and rat models, reduced glycogen accumulation to levels comparable to those of healthy cells. These experiments confirmed the value of developing these new in vitro models.Taken together, this work has led to the identification of new biomarkers for GSDIII, providing a better understanding of the molecular mechanisms in muscle and liver. The creation of these new in vitro models also opens up new therapeutic prospects for GSDIII, particularly by facilitating drug screening

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Bhattacharya, K. "Improvement of the nutritional management of glycogen storage disease type I." Thesis, University College London (University of London), 2010. http://discovery.ucl.ac.uk/19282/.

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The nutritional management of glycogen storage disease has often been called “the intensive regimen”. The intensive regimen may not be without consequence. This thesis aims to characterise the intensive regimen and implement changes. Chapter 1 discusses concepts of glucose homeostasis in humans and introduces the glycogen storage diseases as a group of disorders. The metabolic physiology of those glycogen storage disorders associated with hypoglycaemia are reviewed and traditional methods used to ameliorate these metabolic disturbances are discussed. Methods used in the study include cornstarch loads, breath enrichment of 13CO2, hydrogen breath tests and dietary assessment as well as participant characteristics are discussed in chapter 2. Chapter 3 examines nutritional management as a cross-sectional dietary survey of children and adults with GSD, comparing the patient group to expert-panel recommendations as well as age and sex matched controls. Chapter 4 looks at the short-term effect a new carbohydrate therapy has on biochemical indices of metabolic control focusing on glucose, lactate and insulin profiles. These studies are double-blind cross-over studies, comparing the novel starch to uncooked cornstarch. Similarly Chapter 5 studies further short-term metabolic effects of the novel starch compared to cornstarch by examining hydrogen breath test data and enrichment of 13C02 in breath in an attempt to gauge the mechanism of action of the novel carbohydrate therapy. Chapter 6 examines the implementation of the new dietary starch into subjects' long-term dietary regimen in the form of a randomised cross-over trial. The primary endpoints are quantity of treatment starch use but safety, efficacy and patient acceptance of therapy are also considered. Chapter 7 brings together these various studies drawing conclusions and suggestions for further study. This chapter highlights the difficulties in performing investigations in rare disorders, when subjects are vulnerable to metabolic decompensation and recommends further study in healthy volunteers.

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Crane, Bayley. "Efficacy of Gene Therapy in Dogs with Glycogen Storage Disease Type Ia." NCSU, 2009. http://www.lib.ncsu.edu/theses/available/etd-03202009-163526/.

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Glycogen storage diseases (GSD) are inherited metabolic disorders that affect glycogen use and storage. People with GSD Ia lack the enzyme glucose-6-phosphatase (G6Pase). As a result, these people are unable to convert liver glycogen to free glucose and develop severe hypoglycemia. Patients with GSD also develop growth retardation, hepatomegaly, renomegaly, hypertriglyceridemia, hypercholesterolemia, and hyperlactacidemia. No cure for GSD Ia currently exists. Patients are treated symptomatically with repeated naso-gastric feedings and glucose infusions to maintain normal blood glucose concentrations. Despite treatment, the underlying enzymatic defect remains. Gene therapy holds the promise of correcting this metabolic defect, thus providing a true cure for GSD Ia. Gene therapy uses modified virus particles to deliver a replacement functional G6Pase gene to the patientâs liver. Our group is using two viral vectors, adeno-associated virus (AAV) and helper-dependent adenovirus (HDAd), for gene therapy in dogs with an inheritable form of GSD Ia. We have treated three GSD Ia dogs with the AAV vector and two GSD Ia dogs with the HDAd vector. Vector-treated dogs were able to maintain normal blood glucose concentrations and unlike their untreated counterparts, survived for several years. These promising results provide hope that gene therapy may emerge as an effective treatment for people with GSD Ia.

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Remiche, Gauthier. "Genotype-phenotype Correlation in Late-onset Glycogen Storage Disease Type II, Early Diagnosis and Prognostic Determinants." Doctoral thesis, Universite Libre de Bruxelles, 2016. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/227822.

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Glycogen storage disease type II (GSDII) is an autosomal recessive lysosomal storage disorder caused by acid alpha-1,4-glucosidase (GAA) deficiency. This study aimed to provide an in-depth description of a late-onset GSDII (LO-GSDII) cohort (n=36) and assess potential genotype-phenotype correlation. We performed a clinical record-based study, some patients (n= 19) were also followed prospectively. Phenotypes were highly variable. We focused our clinical assessment onrespiratory failure, as it is the most frequent cause of death in LO-GSDII. In addition to standard spirometric measures, in a subgroup of patients (n = 10) we utilized a new tool, optoelectronic plethysmography (OEP), to investigate the pathophysiology of respiratory muscle impairment.The GAA gene was sequenced in every patient, and pathogenic mutations were identified inall of them. Almost all (35/36) patients carried the same mutation on one allele, IVS1-32-13T>G, which was in compound heterozygosity with a variety of other GAA mutations. To investigate genotype-phenotype correlation, we divided the patient cohort in two groups, according to the severity of the mutation on the second allele. The respiratory function study focused on diaphragmatic weakness. According to the change in forced vital capacity in supine position (ΔFVC), we defined patients with ΔFVC>25% ashaving diaphragmatic weakness (DW) and those with ΔFVC<25% as without diaphragmatic weakness (noDW). We measured pulmonary function and chest wall volumes using OEP inboth groups. We found a good correlation between the supine abdominal contribution to tidal volume (%VAB) and ΔFVC. Patients showed reduced chest wall and abdominal inspiratory capacity and low abdominal expiratory reserve volume. In terms of genotype-phenotype correlation, we counted more subjects in the group with severe second mutations (n=21) who had severe motor disability and respiratory dysfunction. However, this finding remains preliminary because differences were not significant, likely because of small sample size. Finally, in two smaller substudies, we investigated the occurrence of urinary and fecal incontinence in LO-GSDII, and reported a possibly non-fortuitous association of LO-GSDII and hydromyelia in two individuals. Overall, this work 1) provided new insight into genotype-phenotype correlation in GSDII, suggesting that it is of complex nature; 2) refined the analysis of respiratory muscle impairment and showed the utility of OEP for respiratory assessment in this neuromuscular disorder, and possibly in others as well; 3) indicated some so far little studied phenotypic features of LO-GSD-II that deserve further investigation.
Doctorat en Sciences médicales (Médecine)
info:eu-repo/semantics/nonPublished

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Hermans, Monique Maria Petra. "Structural and functional analysis of lysosomal [alpha]-glucosidase in relation to glycogen storage disease type II." [S.l.] : Rotterdam : [The Author] ; Erasmus University [Host], 1993. http://hdl.handle.net/1765/13746.

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Nascimbeni, Anna Chiara. "Glycogenosys type II and Danon Disease: molecular study and muscle pathology." Doctoral thesis, Università degli studi di Padova, 2009. http://hdl.handle.net/11577/3426098.

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The objective of this study was to examine at molecular, biochemical and muscle pathology level two groups of patients affected with Danon disease and GSDII, in order to get new insights that might help in tracing genotype-phenotype correlations and to delineate their pathological mechanisms. Glycogen storage disease type II (GSDII) is an autosomal recessive disorder (OMIM # 232300) caused by the deficiency of the lysosomal enzyme acid ?-glucosidase or acid maltase (EC 3.2.1.20/3), which catalyses the hydrolysis of ?-1,4 and ?-1,6 links of glycogen. The enzyme deficiency leads to lysosomal accumulation of glycogen that results in different clinical phenotypes, ranging from the : the severe infantile-onset form to the childhood, juvenile or adult-onset forms (late-onset forms). We investigated 23 patients with infantile-onset or late-onset glycogen storage disease type II by enzyme activity, protein expression by immunoblotting, GAA gene mutations, and muscle pathology including immunolabeling for Golgi and sarcolemmal proteins. The enzyme activity resulted absent or minimal in infantile-onset cases and variably reduced in late-onset patients. Genotype-phenotype correlation (seven novel mutations were found) showed that most late-onset patients had the heterozygous c.–32-13T>G leaky splicing mutation (one patient was homozygous), but the course of the disease was often difficult to predict on the basis of the mutations alone. One important and novel result from our study came from the Western blot analysis of the different maturative forms of acid ? –glucosidase protein in the muscle from patients with GSDII. We have demonstrated that the muscle from patients with GSDII has a predominant expression of inactive forms of acid ?-glucosidase protein and severely reduced or absent levels of the mature forms. Furthermore, the residual amount of the mature forms of the protein on blotting correlated with the level of enzyme activity in muscle. We first report a different molecular weight of the mature and the intermediate forms of the protein between patients and controls that we attribute to an excessive sialylation of mutant proteins. This is likely caused by a delayed transport and longer transit of the inactive proteins in the Golgi where the sialyltransferases are localized. Supporting this hypothesis, we observed that, in both infantile and late-onset patients, there is an enhanced proliferation of the Golgi apparatus. On the other hand, we did not find any increased expression of LAMP-1 in patients with GSDII, possibly due to the fact that only a minor proportion of mutant enzyme protein is able to reach the lysosomes. Another interesting data rises from the morphologic analysis of the different cellular organelles. Interestingly, we observed a differential degree of dysfunction of endocytic and autophagic pathways in patients with infantile and late-onset GSDII. In late-onset acid maltase deficient muscle, vacuolar membranes expressed sarcolemmal proteins, such as caveolin-3 and dystrophin (previously classified as type 2 vacuoles) and not in the infantile form of the disease (type 4 vacuoles, lakes of glycogen). These features are possibly due to reduced membrane proliferation and vesicular movement in the overcrowded muscle fibers of Pompe disease, and to the membrane remodelling occurring only in patients with late-onset GSDII, which would be a protective mechanism to prevent membrane rupture during fiber contraction. This observation is important because the pathogenesis of the autophagosomes has not yet been fully investigated. Autophagy and membrane remodelling, which is peculiar to late onset disease, might modify a clear response to enzyme replacement therapy and, also, compartmentalize the delivery of the recombinant enzyme. Danon disease, an X-linked dominant disorder, results from mutations in the lysosome-associated membrane protein-2 (LAMP2) gene and presents with hypertrophic cardiomyopathy, skeletal myopathy, and mental retardation. To investigate the effects of LAMP2 gene mutations on protein expression in different tissues, we screened LAMP2 gene mutations and LAMP-2 protein deficiency in the skeletal muscle of nine unrelated patients with hypertrophic cardiomyopathy and vacuolar myopathy. We identified three novel families (including one affected mother) with unreported LAMP2 gene null mutations and LAMP-2 protein deficiency in skeletal and myocardial muscle, leukocytes, and fibroblasts. LAMP-2 protein deficiency was detectable in various tissues, including leukocytes, explaining the multisystem clinical involvement. Skeletal muscle immunopathology showed that mutant protein was not localized in the Golgi complex, vacuolar membranes expressed sarcolemmal- specific proteins, and the degree of muscle fiber vacuolization correlated with clinical muscle involvement. In our female patient, muscle histopathology and LAMP-2 protein analysis was inconclusive, indicating that diagnosis in females requires mutation identification. The random X-chromosome inactivation found in muscle and leukocytes excluded the possibility that selective involvement of some tissues in females is due to skewed X-chromosome inactivation. Therefore, biochemical analysis of leukocytes might be used for screening in male patients, but genetic screening is required in females.
Scopo di questo studio è stato quello di analizzare a livello molecolare, biochimico e della patologia muscolare due gruppi di pazienti affetti dalla malattia di Danon e da glicogenosi di tipo II, in modo da acquisire nuove informazioni utili a tracciare possibili correlazioni genotipo-fenotipo e a chiarire i meccanismi patologici alla base di queste patologie. La Glicogenosi di tipo II (GSDII) è una malattia autosomica recessiva (OMIM # 232300) causata da un deficit dell’enzima mitocondriale ?-glucosidasi o maltasi acida (EC 3.2.1.20/3), che catalizza l’idrolisi dei legami glicogeno ? -1,4 e ? -1,6. Tale deficit enzimatico porta all’accumulo a livello lisosomale di glicogeno, che genera un’ampia eterogeneità clinica, che spazia da casi con esordio infantile e quadro clinico molto severo a forme più benigne con esordio tardivo nell’età adulta. Sono stati analizzati 23 pazienti con deficit di ?-glucosidasi acida per l’attività enzimatica mediante saggio fluorimetrico, l’espressione proteica mediante immunoblotting, la presenza di mutazioni nel gene GAA con SSCP e la patologia muscolare mediante immunocolorazione del Golgi e delle proteine sarcolemmali. L’attività enzimatica è risultata assente o minima nei casi ad esordio infantile e variabilmente ridotta nei pazienti con esordio tardivo. Le correlazioni genotipo-fenotipo indicano che la maggior parte dei pazienti ad esordio tardivo presentano la mutazione “leaky splicing” c.–32-13T>G in eterozigosi (un paziente era omozigote), ma il decorso della malattia è spesso difficile da prevedere solo sulla base delle mutazioni. Un risultato interessante deriva dall’analisi mediante western blot dell’espressione dell’?-glucosidasi nei pazienti: abbiamo infatti dimostrato che il muscolo di questi pazienti esprime prevalentemente forme inattive/immature dell’enzima ?-glucosidasi, mentre la forma matura della proteina è assente o presente a livelli molto ridotti. Inoltre, si è visto che l’eventuale quantità residua di forme proteiche mature riscontrate al western blot correla con i livelli di attività enzimatica riscontrati nel muscolo di questi pazienti. Il peso molecolare sia delle forme mature che di quelle immature/inattive è risultato essere maggiore nei pazienti rispetto ai muscoli di controllo. Attribuiamo tali differenze ad un’eccessiva sialilizzazione delle forme proteiche non funzionali, causata probabilmente da un loro trasporto ritardato o da una loro ritenzione nel complesso di Golgi, in cui agiscono le sialil-transferasi. A sostegno di tale ipotesi, abbiamo riscontrato una proliferazione del Golgi nelle fibre muscolari dei pazienti, causata possibilmente dalla ritenzione delle forme enzimatiche inattive, che non possono venire correttamente veicolate ai lisosomi. Le membrane vacuolari esprimono le proteine sarcolemmali nei pazienti con esordio tardivo ma non in quelli ad esordio infantile, suggerendo un’autofagia estesa ed un rimodellamento della membrana vacuolare nei pazienti ad esordio tardivo. La Malattia di Danon ha ereditarietà di tipo dominante legato al cromosoma X ed è causata da mutazioni nel gene LAMP2 (Lysosomal Associated Membrane Protein-2), e si presenta con cardiomiopatia ipertrofica, miopatia e ritardo mentale. Per studiare gli effetti delle mutazioni nel gene LAMP2 sull’espressione proteica in diversi tessuti, abbiamo effettuato uno screening molecolare ed un’analisi del difetto proteico sul tessuto muscolare, cardiaco, sui leucociti e fibroblasti di 9 soggetti maschi non correlati tra loro, con cardiomiopatia ipertrofica e miopatia vacuolare. Tre dei 9 soggetti analizzati hanno evidenziato un deficit proteico di LAMP2 generalizzato. Tale difetto è stato infatti riscontrato in tutti i tessuti da noi analizzati: tessuto muscolare scheletrico e cardiaco, leucociti e fibroblasti. Questo risultato indica che l’analisi biochimica può essere svolta in modo non invasivo sui leucociti, e potrebbe quindi essere impiegata nello screening dei soggetti maschi; inoltre, questo deficit multi-organo di proteina LAMP2 potrebbe spiegare il coinvolgimento clinico multisistemico. Abbiamo inoltre esteso l’analisi anche alla madre di un affetto: in questo caso il muscolo, i fibroblasti e i leucociti presentano livelli proteici comparabili al controllo normale. Sono state identificate mutazioni nel gene LAMP2 in tutti e 3 i pazienti maschi e nella femmina eterozigote. Ciascun paziente presentava una mutazione diversa e non riportata precedentemente in letteratura: sono tutte mutazioni nulle (nonsenso o frame-shifting) che ci si aspetta diano origine ad una proteina tronca, con perdita del dominio trans-membrana. ’istopatologia muscolare ha evidenziato una vacuolizzazione fibrale estesa e della degenerazione . L’analisi immunopatologica del muscolo scheletrico ha evidenziato che non vi è proliferazione del complesso del Golgi nei pazienti, che le membrane vacuolari esprimono le proteine sarcolemmali e che il grado di vacuolizzazione correla con il coinvolgimento clinico a livello muscolare. L’analisi dell’inattivazione del cromosoma X effettuata sul tessuto muscolare e sui leucociti ha escluso la possibilità che il coinvolgimento selettivo di alcuni tessuti nelle femmine sia dovuto ad una inattivazione non casuale dell’X

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Ichikawa, Shoji. "The molecular genetic analysis of three human neurological disorders." free online free to MU campus, others may purchase, 2002. http://wwwlib.umi.com/cr/mo/preview?3074409.

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Curlis, Yvette M. "Attitudes towards newborn screening for Pompe disease among affected adults, family members and parents of 'healthy' children /." Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/7065.

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Pompe disease is a rare autosomal recessive condition caused by a deficiency in lysosomal alpha glucosidase. It is a progressive and often fatal muscular disease with wide variation in clinical presentation. Two broad clinical categories of Pompe disease have been identified; infantile- and late- onset. In the past decade, enzyme replacement therapy has shown promising results in treating the underlying pathology, resulting in improved clinical outcome. Clinical trials indicating that initiation of treatment at an earlier disease stage leads to a higher chance of preventing permanent damage have led to the proposition of introducing newborn screening for Pompe disease. All forms of Pompe disease are caused by the same pathology, and thus newborn screening has the potential to identify those affected with the more severe infantile-onset form as well as those with late-onset disease who may not present with symptoms until late in life.
The aim of this study was to investigate attitudes towards newborn screening for Pompe disease among affected adults, their family members and parents of ‘healthy’ children. Affected adults were recruited through support groups in Australia, the United Kingdom and United States; family members of affected adults were recruited from Australia; and parents of ‘healthy’ children were recruited through maternal child health clinics in Victoria, Australia. Participants completed questionnaires exploring their experiences of Pompe disease and/or newborn screening and their attitudes towards newborn screening for Pompe disease.
Support for newborn screening for Pompe disease was high among adults with Pompe disease (85.4%), parents of ‘healthy’ children (93.9%) and all three family members of affected adults who participated in this study. However, when offered a theoretical screening test that would only identify infantile-onset Pompe disease, 42.1% of adults with Pompe disease and 53.1% of parents of ‘healthy’ children preferred this screen, indicating that these stakeholders have some concerns regarding detection of late-onset disease in infancy. Factors influencing attitudes were investigated and support for newborn screening in affected adults was highly correlated with age of onset of disease; a preference to have been diagnosed in infancy; a belief that an earlier diagnosis would have made symptoms easier to cope with; and a stronger confidence in the efficacy of enzyme replacement therapy.
Potential benefits of diagnosis of late-onset disease in infancy were identified as being able to avoid the diagnosis odyssey, access enzyme replacement therapy at the optimal time, and allow individuals to make appropriate life choices. Participants identified increased anxiety in parents and the potential for over-protectiveness, in addition to possible discrimination, as harms of newborn screening for Pompe disease.
Families in which an infant is identified with the potential for late-onset Pompe disease will need assistance to adapt to and manage this diagnosis, so that anxiety is minimised and unnecessary limitations are not placed on the child. Whilst potential medical and psychosocial benefits can result from newborn screening, it is important to carefully consider the potential for harm and the resources required to appropriately manage these so that ultimately benefit outweighs harm.

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Schleissing, Mary Rucker. "Biochemical and functional analysis after in utero delivery of recombinant adeno-associated virus to a mouse model of glycogen storage disease type II." [Gainesville, Fla.] : University of Florida, 2002. http://purl.fcla.edu/fcla/etd/UFE0000603.

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Книги з теми "Glycogen storage disease type III"

Filosto, Massimiliano. Advances in diagnosis and management of glycogenosis II. Hauppauge, N.Y: Nova Science Publishers, 2011.

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Crowley, John F. Chasing miracles: The Crowley family journey of strength, hope, and joy. New York: Newmarket Press, 2010.

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Anand, Geeta. The Cure. New York: HarperCollins, 2009.

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Toscano, Antonio, Massimiliano Filosto, and Alessandro Padovani. Advances in Diagnosis and Management of Glycogenosis II. Nova Science Publishers, Incorporated, 2013.

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van der Ploeg, Ans T., and Pascal Laforêt. Pompe Disease. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0055.

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Pompe disease, also named acid maltase deficiency and glycogen storage disease type II (GSDII), is a rare autosomal recessive disorder caused by the deficiency of the glycogen-degrading lysosomal enzyme acid α‎-glucosidase. The clinical spectrum of this disease is broad, varying from a lethal infantile-onset generalized myopathy including cardiomyopathy, to late-onset slowly progressive muscle weakness mimicking limb-girdle muscular dystrophy. Respiratory insufficiency is a frequent complication and the main cause of death. The prognosis of Pompe disease has changed considerably with the use of enzyme replacement therapy using recombinant acid α‎-glucosidase (alglucosidase alfa), which has been widely available since 2006. Improvements in survival and major motor achievements can be observed in patients with infantile forms, and recent studies demonstrate improvement of walking distance and stabilization of pulmonary function in late-onset forms. A longer-term study of the safety and efficacy of ERT, based on data gathering across the complete spectrum of Pompe disease via national or international patient registries, is needed in order to formulate more precise guidelines for treatment.

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Anand, Geeta. The Cure: How a Father Raised $100 Million--And Bucked the Medical Establishment--In a Quest to Save His Children. William Morrow, 2006.

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Anand, Geeta. The Cure: How a Father Raised $100 Million--And Bucked the Medical Establishment--In a Quest to Save His Children. William Morrow, 2006.

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Anand, Geeta. Cure: How a Father Raised $100 Million--and Bucked the Medical Establishment--in a Quest to Save His Children. HarperCollins Publishers, 2009.

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Anand, Geeta. Cure: How a Father Raised $100 Million--and Bucked the Medical Establishment--in a Quest to Save His Children. HarperCollins Publishers, 2009.

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Anand, Geeta. Cure: How a Father Raised $100 Million--and Bucked the Medical Establishment--in a Quest to Save His Children. HarperCollins Publishers, 2010.

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Частини книг з теми "Glycogen storage disease type III"

Timson, David J., Richard J. Reece, James B. Thoden, Hazel M. Holden, Andrea L. Utz, Beverly M. K. Biller, Eugen-Matthias Strehle, et al. "Glycogen Storage Disease Type III." In Encyclopedia of Molecular Mechanisms of Disease, 729. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8632.

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Austin, S. L., A. D. Proia, M. J. Spencer-Manzon, J. Butany, S. B. Wechsler, and P. S. Kishnani. "Cardiac Pathology in Glycogen Storage Disease Type III." In JIMD Reports, 65–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/8904_2011_118.

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Shin, Y. S., M. Rieth, J. Tausenfreund, and W. Endres. "First Trimester Diagnosis of Glycogen Storage Disease Type II and Type III." In Studies in Inherited Metabolic Disease, 289–91. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-009-1069-0_30.

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Maire, I., G. Mandon, and M. Mathieu. "First Trimester Prenatal Diagnosis of Glycogen Storage Disease Type III." In Studies in Inherited Metabolic Disease, 292–94. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-009-1069-0_31.

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Lee, Teresa M., Erika S. Berman-Rosenzweig, Alfred E. Slonim, and Wendy K. Chung. "Two Cases of Pulmonary Hypertension Associated with Type III Glycogen Storage Disease." In JIMD Reports, 79–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/8904_2011_20.

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Gatti, R., G. Lamedica, M. Di Rocco, D. Massocco, N. Marchese, and C. Borrone. "Long-term Cornstarch Therapy in Glycogen Storage Disease Types I, Ib and III." In Practical Developments in Inherited Metabolic Disease: DNA Analysis, Phenylketonuria and Screening for Congenital Adrenal Hyperplasia, 280–83. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4131-1_48.

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Brambilla, Alessandra, Savina Mannarino, Roberta Pretese, Serena Gasperini, Cinzia Galimberti, and Rossella Parini. "Improvement of Cardiomyopathy After High-Fat Diet in Two Siblings with Glycogen Storage Disease Type III." In JIMD Reports, 91–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/8904_2014_343.

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Sentner, Christiaan P., Yvonne J. Vos, Klary N. Niezen-Koning, Bart Mol, and G. Peter A. Smit. "Mutation Analysis in Glycogen Storage Disease Type III Patients in the Netherlands: Novel Genotype-Phenotype Relationships and Five Novel Mutations in the AGL Gene." In JIMD Reports, 19–26. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/8904_2012_134.

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Mansour, Eli, and Ana Flavia Bernardes Sousa. "Glycogen Storage Disease Type 1b." In Encyclopedia of Medical Immunology, 330–33. New York, NY: Springer New York, 2020. http://dx.doi.org/10.1007/978-1-4614-8678-7_136.

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Manners, D. J. "Glycogen Storage Disease, Type I." In Ciba Foundation Symposium - Control of Glycogen Metabolism, 321–35. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470719343.ch23.

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Тези доповідей конференцій з теми "Glycogen storage disease type III"

Giugliano, Giusy, Michela Schiavo, Daniele Pirone, Jaromir Behal, Vittorio Bianco, Sandro Montefusco, Pasquale Memmolo, Lisa Miccio, Pietro Ferraro, and Diego L. Medina. "Investigation on lysosomal accumulation by a quantitative analysis of 2D phase-maps in digital holography microscopy." In Digital Holography and Three-Dimensional Imaging, Th2A.6. Washington, D.C.: Optica Publishing Group, 2024. http://dx.doi.org/10.1364/dh.2024.th2a.6.

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Quantitative Phase Imaging through Digital Holography (QPI-DH) represents a quantitative and label-free method to detect lysosomal dysfunction in cells. Testing in the cellular model of Mucopolysaccharidosis type III-A, a lysosomal storage disease, demonstrate its potential.

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Ke, Li,. "Recurrence Quantification Analysis of Sustained Sub-Maximal Grip Force in Patients with Glycogen Storage Disease Type III." In Modeling and Control in Biomedical Systems, edited by Rees, Stephen, chair Andreassen, Steen and Andreassen, Steen. Elsevier, 2009. http://dx.doi.org/10.3182/20090812-3-dk-2006.00067.

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Quackenbush, David, Justin Devito, Luigi Garibaldi, and Melissa Buryk. "Late Presentation of Glycogen Storage Disease Type Ia and Iii in Children with Short Stature and Hepatomegaly*." In Selection of Abstracts From NCE 2016. American Academy of Pediatrics, 2018. http://dx.doi.org/10.1542/peds.141.1_meetingabstract.753.

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Merrigan, Christine, Orla Purcell, Eimear Forbes, Jenny Mc Nulty, Emma Lally, and Prof Ellen Crushell. "GP229 The use of the ketogenic diet in a metabolic patient with glycogen storage disease type IIIa." In Faculty of Paediatrics of the Royal College of Physicians of Ireland, 9th Europaediatrics Congress, 13–15 June, Dublin, Ireland 2019. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2019. http://dx.doi.org/10.1136/archdischild-2019-epa.288.

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Alrasheed, Khalid, Tahseen Mozaffar, and Mari Perez-Rosendahl. "Muscle Pathology in a Case of Glycogen Storage Disease III (P6-8.014)." In 2023 Annual Meeting Abstracts. Lippincott Williams & Wilkins, 2023. http://dx.doi.org/10.1212/wnl.0000000000202881.

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Kallenbach, Michael, Petra May, David Pullmann, David Schöler, Jan Philipp Köhler, Irene Esposito, Tom Lüdde, and Stephan vom Dahl. "Incidence of hepatic adenomas in adult glycogen storage disease type Ia/b." In 39. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag, 2023. http://dx.doi.org/10.1055/s-0042-1759983.

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Yahşi, Aysun, Tuğba Erat, Halil Özdemir, Tuğçe Tural Kara, Reyhan Erol, Fatma Tuba Eminoğlu, Elif Ince, et al. "P274 An unexpected disease in an infant with pancytopenia and pulmonary abscess: glycogen storage disease type 1b." In 8th Europaediatrics Congress jointly held with, The 13th National Congress of Romanian Pediatrics Society, 7–10 June 2017, Palace of Parliament, Romania, Paediatrics building bridges across Europe. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2017. http://dx.doi.org/10.1136/archdischild-2017-313273.362.

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Wang, Shutao, Balasundar I. Raju, Evgeniy Leyvi, David A. Weinstein, and Ralf Seip. "Acoustically accessible window determination for ultrasound mediated treatment of glycogen storage disease type Ia patients." In 11TH INTERNATIONAL SYMPOSIUM ON THERAPEUTIC ULTRASOUND. AIP, 2012. http://dx.doi.org/10.1063/1.4757373.

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Bell, Alexandra, and Ahmed Al-Mukhtar. "P087 Liver transplant in Glycogen Storage Disease Type 1a; a case that disputes current guidelines." In Abstracts of the British Association for the Study of the Liver Annual Meeting, 22–24 November 2021. BMJ Publishing Group Ltd and British Society of Gastroenterology, 2021. http://dx.doi.org/10.1136/gutjnl-2021-basl.95.

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Pellegrino, Francesco, Aimee Wiseman, Lucy Jackman, Leanne Goh, and Edward Gaynor. "OC81 Eosinophilic esophagitis successfully treated with elimination diet and proton pump inhibitors in a patient with glycogen storage disease type 9c." In Abstracts of the BSPGHAN 38th Annual Meeting, 20–22 March 2024, The Bristol Hotel, Bristol, UK. BMJ Publishing Group Ltd, 2024. http://dx.doi.org/10.1136/flgastro-2024-bspghan.77.

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