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Due to enoyl coenzyme A hydratase, short chain, 1, mitochondria (ECHS1) deficiency.
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exceeding nutrients suppress Enoyl-CoA hydratase-1 (ECHS1) activity by inducing its acetylation resulting in accumulation of fatty acids and branched-chain amino acids and oncogenic mTOR activation
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ECHS1 mutations phenotype might be milder than reported earlier, compatible with prolonged survival, and also includes isolated paroxysmal exercise-induced dystonia.
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Whole exome sequencing identified heterozygous ECHS1 mutations c.836T>C (novel) and c.8C>A for short-chain enoyl-CoA hydratase (SCEH) deficiency of which 1/2 of the cases are associated with secondary lymphocyte pyruvate dehydrogenase complex deficiency.[review]
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This is the first report of homozygosity for a truncating mutation in ECHS1, which may explain the severe phenotype. Our report highlights the need to consider SCEH deficiency in patients with lethal neonatal lactic acidosis
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Human ECHS1 catalyses the hydration of five substrates via different metabolic pathways, with the highest specificity for crotonyl-CoA and the lowest specificity for tiglyl-CoA
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These results suggested that ECHS1 may promote cell proliferation in hepatocellular carcinoma in an EGFR-dependent manner.
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In conclusion, the results of the present study suggested that ECHS1 may have an important role in colorectal cancer cell proliferation and migration
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identification of four additional patients with mutations in ECHS1 highlights the importance of the valine degradation pathway in Leigh syndrome
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ECHS1 mutations cause combined respiratory chain deficiency resulting in Leigh syndrome.
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ECHS1 may play important roles in gastric cancer cell proliferation and migration through PKB- and GSK3b-related signaling pathways.
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The study demonstrated that ECHS1 mutations result in ECHS1 deficiency and are another cause of Leigh disease in two siblings.
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ECHS1 knockdown reduced cell viability and enhanced cisplatin-induced apoptosis in hepatocellular carcinoma cells.
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The results confirmed that small hepatitis B surface antigen (SHBs) interacted with ECHS1.
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The coexistence of HBs and ECHS1 enhances HepG2 cell apoptosis, affects ECHS1 localization in the mitochondria and induces apoptosis by decreasing the mitochondrial membrane potential (MMP).
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ECHS1 specifically represses STAT3 activity and negatively regulates the expression of several target genes of STAT3 through inhibiting STAT3 phosphorylation.
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Expression of mitochondrial short chain enoyl-CoA hydratase (ECHS)was significantly down-modulated in virus infected glioblastoma cells and ECHS knockdown (siRNA) impaired virus replication and cytopathic effects.
