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a link between ACADS susceptibility variants and abnormal beta-oxidation consistent with known altered kinetics of these variants
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Korean patients with Short-chain acyl-CoA dehydrogenase deficiency showed heterogenous clinical features and ACADS genotype.
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Thirteen proteins had significant alteration in protein levels in patients carrying variation c.319C>T in ACADS compared to controls and they belonged to various pathways, such as the antioxidant system and amino acid metabolism.
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Results show significant upregulation of LASP1 and SCAD protein levels in acute psychotic bipolar disorder samples.
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IVD mutations in Asian populations are distinct from these in Western populations.
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physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of SCAD and prevented enzymatic activity loss
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In glucose-tolerant individuals the minor C-allele of rs2014355 of ACADS was associated with reduced measures of glucose-stimulated insulin release during an oral glucose tolerance test.
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We therefore propose that SCAD misfolding leads to production of ROS, which in turn leads to fission and a grain-like structure of the mitochondrial reticulum. This finding indicates a toxic response elicited by misfolded p.Arg83Cys SCAD proteins
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Molecular pathogenesis of a novel mutation, G108D, in ACADS identified in subjects with ACADS deficiency.
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Reduction of catalytic activity and stability in polymorphic variant of SCAD (Gly185Ser) is caused by decreased flexibility in the tertiary conformation of the mutant enzyme.
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Replacement of the catalytic glutamate in either short-chain acyl-CoA dehydrogenase (SCAD) or isovaleryl-CoA dehydrogenase (IVD)with glycine resulted in a several-fold reduction in affinity for substrate.
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One of 220 SIDs cases was homozygous for the prevalent MCAD A985G mutation.
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The c.319C>T mutation can lead to wide clinical and biochemical phenotypic variability, suggesting a complex multifactorial/polygenic condition. This should be screened for in individuals with multicore myopathy, particularly among the Ashkenazim.
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A homozygous variant allele of the SCAD gene, 625G>A, was detected in new case of short-chain acyl-CoA dehydrogenase deficiency.
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Extensive laboratory investigations indicate that the short-chain acyl-CoA dehydrogenase gene variant is likely preventing or delaying the normal expression of the Prader-Willi syndrome phenotype.
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SCAD deficiency should be considered as a disorder of protein folding that can lead to clinical disease in combination with other genetic and environmental factors.
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A deoxyribonucleic analysis revealed the presence of a 625G>A (G-to-A substitution at nucleotide 625) variant short-chain acyl-coenzyme A dehydrogenase gene polymorphism.
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SCAD deficiency cause a disorder that leads to the accumulation of butyrylcarnitine and ethylmalonic acid in blood and urine.
