Search results for "Metabolic myopathy"

showing 4 items of 4 documents

Diagnostik und Therapie des Morbus Pompe im Kindesalter

2020

Pompe disease is a rare metabolic myopathy caused by deficiency of lysosomal α-glucosidase. Reduced enzyme activity results in abnormal intra- and extralysosomal glycogen deposition as well as impaired cellular function and autophagy. Age at manifestation and severity of disease depend on residual enzyme activity. Enzyme replacement therapy (ERT) is available since 2006. In infantile onset Pompe disease, the most severe form, markedly prolonged survival has resulted in a new phenotype with symptoms and problems not encountered previously. In addition, it became apparent that antibody formation against the recombinant human enzyme may adversely affect the response to ERT. This review summari…

Pediatricsmedicine.medical_specialtybiologybusiness.industryAutophagy030232 urology & nephrologyMedizinGlycogen deposition610 Medicine & healthDiseaseMetabolic myopathyEnzyme replacement therapymedicine.diseaseEnzyme assay03 medical and health sciences0302 clinical medicine10036 Medical Clinic030225 pediatricsPediatrics Perinatology and Child HealthGlycogen storage disease type IImedicinebiology.proteinbusinessAntibody formation
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A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population.

2002

Myoadenylate deaminase deficiency is the most common metabolic disorder of skeletal muscle in the Caucasian population, affecting approximately 2% of all individuals. Although most deficient subjects are asymptomatic, some suffer from exercise-induced myalgia suggesting a causal relationship between a lack of enzyme activity and muscle function. In addition, carriers of this derangement in purine nucleotide catabolism may have an adaptive advantage related to clinical outcome in heart disease. The molecular basis of myoadenylate deaminase deficiency in Caucasians has been attributed to a single mutant allele characterized by double C to T transitions at nucleotides +34 and +143 in mRNA enco…

ThreonineDNA ComplementaryGenotypeBlotting WesternGlycineMetabolic myopathyBiologyCompound heterozygosityPolymerase Chain ReactionWhite PeopleAMP DeaminaseMetabolic DiseasesMuscular DiseasesGenotypemedicineHumansAlleleTransversionMuscle SkeletalGenetics (clinical)AllelesElectromyographyPoint mutationMetabolic disorderAMP deaminasemedicine.diseaseMolecular biologyPhenotypeNeurologyPediatrics Perinatology and Child HealthMutationNeurology (clinical)DNA ProbesNeuromuscular disorders : NMD
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Outcome of patients with classical infantile pompe disease receiving enzyme replacement therapy in Germany

2015

Enzyme replacement therapy (ERT) has been shown to improve outcome in classical infantile Pompe disease. The purpose of this study was to assess mortality, morbidity, and shortcomings of ERT in a larger cohort of patients treated outside clinical trials. To accomplish this, we retrospectively analyzed the data of all 23 subjects with classical infantile Pompe disease having started ERT in Germany between January 2003 and December 2010.Ten patients (43%) deceased and four others (17%) became ventilator dependent. Seven infants (30.5%) made no motor progress at all, while seven (30.5%) achieved free sitting, and nine (39%) gained free walking. Besides all the seven patients (100%) attaining n…

congenital hereditary and neonatal diseases and abnormalitiesPediatricsmedicine.medical_specialtybusiness.industryMEDLINEnutritional and metabolic diseases610 Medicine & healthDiseaseMetabolic myopathyEnzyme replacement therapymedicine.disease1301 Biochemistry Genetics and Molecular Biology (miscellaneous)ArticleClinical trial2712 Endocrinology Diabetes and Metabolism10036 Medical Clinic2724 Internal MedicineCohortmedicineGlycogen storage diseasebusiness
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Myoadenylate deaminase deficiency

1987

Myoadenylate deaminase (MAD) is the rate-limiting enzyme in the purine nucleotide cycle which is biochemically linked to glycolysis and the citric cycle and thereby providing energy during intense muscular activity. In muscle fibers, myoadenylate deaminase operates at considerably higher activity levels than in other organs. First detected using enzyme-histochemical methods, it now appears that deficiency of myoadenylate deaminase is one of the most frequent enzyme defects in muscle. The primary defect may occur as an isolated nosological entity or not infrequently it is also associated with a large spectrum of different neuromuscular conditions. It seems to be the primary unassociated MAD …

myalgiaWeaknessmedicine.medical_specialtyBiopsyElectromyographyMetabolic myopathyBiologyGastroenterologyAMP Deaminase03 medical and health sciences0302 clinical medicineInternal medicineDrug DiscoveryBiopsymedicineHumansGenetics (clinical)030304 developmental biology0303 health sciencesmedicine.diagnostic_testMusclesMuscle weaknessAMP deaminaseNeuromuscular DiseasesGeneral Medicinemedicine.diseaseEndocrinologyNucleotide DeaminasesMolecular MedicineSarcoidosismedicine.symptom030217 neurology & neurosurgeryKlinische Wochenschrift
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