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Hepatic disorders in pregnancy
Published in Hung N. Winn, Frank A. Chervenak, Roberto Romero, Clinical Maternal-Fetal Medicine Online, 2021
Ghassan M. Hammoud, Jamal A. Ibdah
There is a strong association between AFLP and a deficiency of the enzyme long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) in the fetus, a disorder of mitochondrial fatty acid beta-oxidation (75). In a study by Ibdah and colleagues, 79% of women who carried LCHAD-deficient fetuses developed AFLP (76). Infants born to mothers with AFLP may exhibit immediate or delayed nonketotic hypoglycemia, hepatic encephalopathy, cardiomyopathy, slowly progressing peripheral neuropathy, skeletal myopathy, or sudden unexpected death (77,78). Other studies reported involvement of fetal hepatic carnitine palmitoyltransferase (CPT I) deficiency and maternal medium-chain acyl-CoA dehydrogenase deficiency in AFLP (79,80). It is recommended that neonates born to pregnancies complicated by AFLP be tested for the common LCHAD G1528C mutation (81) and that this testing when done early after birth can be lifesaving as it may identify LCHAD-deficient children before they manifest the disease allowing early dietary intervention by institution of a diet low in fat and high in carbohydrate, and by substitution of the long-chain fatty acids with medium-chain fatty acids. This strong association between AFLP and the common G1528C mutation in the fetus is significant (82,83), and hence screening the offspring of women who develop AFLP at birth for this mutation can be lifesaving.
Short-chain 3-hydroxyacylCoA dehydrogenase (SCHAD) deficiency
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop
The enzyme, 3-hydroxyacyl CoA dehydrogenase, is a homodimer with 302 amino acids in each subunit [3–5] with activity against 3-hydroxyacylCoA esters of C4 to C16 length, but with greatest activity against C10 and less activity as the chain length increases (Figure 43.1). The cDNA for the gene has been cloned and sequenced [6, 7] and mapped to chromosome 4q22-26 [7]. It contains eight exons and spans 49 kb. The enzyme is synthesized with a leader peptide, which is removed after import into the mitochondria. Mutations have been identified [8].
Metabolic Diseases
Published in Stephan Strobel, Lewis Spitz, Stephen D. Marks, Great Ormond Street Handbook of Paediatrics, 2019
Stephanie Grünewald, Alex Broomfield, Callum Wilson
Regular feeds, in some FAOD even overnight feeds and the avoidance of long-chain fats are recommended, particularly necessary in long-chain disorders (longchain L-3 hydroxyacyl-CoA dehydrogenase deficiency [LCHAD] and very long-chain L-3 hydroxyacyl-CoA dehydrogenase deficiency [VLCAD]).
The impact of ascidian biofouling on the farmed Mediterranean mussel Mytilus galloprovincialis physiology and welfare, revealed by stress biomarkers
Published in Biofouling, 2023
Dimitrios K. Papadopoulos, Athanasios Lattos, Ioannis A. Giantsis, John A. Theodorou, Basile Michaelidis, Konstantinos Feidantsis
Enzyme activity assay performed for metabolic enzymes l-lactate dehydrogenase (l-LDH, EC 1.1.1.27), Citrate Synthase (CS, EC 4.1.3.7) and 3-hydroxyacyl-CoA dehydrogenase (HOAD, EC1.1.1.35). Mantle and PAM homogenization for enzyme activity assessment were prepared as described by Driedzic and Almeida-Val (1996) and Speers-Roesch et al. (2016). Regarding l-LDH, and HOAD the tissues were homogenized in a buffer containing 150 mmol l−1 imidazole, 1 mmol l−1 EDTA, 5 mmol l−1 dithiothreitol (DTT) and 1% Triton X-100, pH 7.4. For CS, tissues were homogenized in a buffer containing 20 mmol l−1 HEPES, 1 mmol l−1 EDTA with 1% Triton X-100, pH 7.4. Following homogenization samples were centrifuged at 13,000g for 10 min in 4 °C and supernatants used for enzymatic assays.
An update on diagnosis and therapy of metabolic myopathies
Published in Expert Review of Neurotherapeutics, 2018
Fat metabolism disorders should be generally treated with a carbohydrate- and protein-rich diet. FAODs respond favorably to the avoidance of fasting and sustained extraneous exercise [28,43]. During illness it is important to provide these patients with high-caloric hydration to prevent lipolysis [43]. Whether low natural fat diet together with medium-chain triglyceride (MCT) oil before and after exercise is beneficial in patients with VLCAD, is controversially discussed [44,45]. Carbohydrates and MTCs are recommended for CPT-II deficiency [1]. Patients with long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) benefit from a diet with LCT, not exceeding 10%, and an increase in the amount of MCTs [46]. The daily intake of energy should be adapted to energy requirements and diet should involve frequent meals also during the night to avoid periods of fasting [46]. Patients with VLCAD are advised to avoid fasting and dehydration, and to eat a low-fat diet with supplemental MCTs prior to periods of exercise [1]. Oral galactose treatment may be beneficial for some of the manifestations in PGM1-associated GSD [47]. However, in a recent study it has been shown that standard dosages of 1–2.5 g/kgBW are not sufficient to restore impaired glycosylation in all patients [48].
Iron-deficient diet induces distinct protein profile related to energy metabolism in the striatum and hippocampus of adult rats
Published in Nutritional Neuroscience, 2022
Jessica M. V. Pino, Erika S. Nishiduka, Márcio H. M. da Luz, Vitória F. Silva, Hanna K. M. Antunes, Alexandre K. Tashima, Pedro L. R. Guedes, Altay A. L. de Souza, Kil S. Lee
Regarding energy metabolism of the striatum, IR increased glycogen phosphorylase (PYGB) and phosphofructokinase (PFKP), but reduced glucose-6-phosphate isomerase (GPI), triose-phosphate isomerase (TPI) and glyceraldehyde dehydrogenase (GAPDH), indicating alterations in the glycolytic pathway (Figure 3, left panel and Table S2). On the other hand, 3-hydroxyacyl-CoA dehydrogenase (HSD17B10) that participates in β-oxidation and enzymes of the initial steps of the tricarboxylic acid cycle (TCA) such as citrate synthase (CS) and mitochondrial isocitrate dehydrogenase (IDH3B) were increased, suggesting that an IR diet promotes the use of fatty acid in striatum (Figure 3 left panel and Table S2). Induction of other enzymes that participate in lipid catabolism such as monoglyceride lipase, mitochondrial glycerol-3-phosphate dehydrogenase and very-long-chain 3-oxoacyl-CoA reductase in the IR group corroborates increased fatty acid consumption following insufficient iron intake (Table S2). The IR diet reduced mitochondrial malate dehydrogenase (MDH2) and voltage-dependent anion channel (VDAC), which mediates the exchange of metabolites such as pyruvate, malate, succinate, NADH and ATP/ADP between mitochondria and cytosol [19] (Figure 3 left panel and Table S2). In addition, an increase in non-catalytic subunit of complex I (NDUFA5) and a decrease in ATP synthase subunit d (ATP5H) were observed in the striatum of the IR group (Figure 3 left panel and Table S2), suggesting that mitochondrial activity might have been altered by the IR diet. However, it was also noticeable that the IR diet increased antioxidant molecules such as superoxide dismutase 2 (SOD2), glutathione-s-transferase (GSTµ3) and peroxiredoxin-6 (PRDX6), and enzymes that participate in the clearance of toxic metabolites such as aldehyde dehydrogenase (ALDH1B1) (Figure 3 left panel and Table S2).