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Journal articles on the topic 'Long-chain-acyl-CoA dehydrogenase'

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Published: 20 April 2024

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1

Masterson, C., A. Blackburn, and C. Wood. "Acyl-CoA dehydrogenase activity in pea cotyledon tissue during germination and initial growth." Biochemical Society Transactions 28, no. 6 (December 1, 2000): 760–62. http://dx.doi.org/10.1042/bst0280760.

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Acyl-CoA dehydrogenase activity has been measured in homogenates of post-imbibition to 14-day-old hydroponically grown pea seeds at daily intervals, using C4, C12 and C16 acyl-CoA substrates. The activity peaks of the different chain-length acyl-CoA dehydrogenases did not transpose at all points and the ratios of the chain-length activities were not constant. It therefore has to be concluded that more than one dehydrogenase is present in pea mitochondria. There was a post-imbibition initial surge of activity with short- and mid-chain-length substrates. The C16- handling enzyme first peaked at 3–4 days, which coincided with the onset of plumule unfurling and greening. Further peaks were observed with all three substrates, coinciding with secondary root formation and leaf enlargement and later with cotyledon degeneration. Overall activity showed that the long-chain acyl-CoA dehydrogenase was much more active than the short-chain acyl-CoA dehydrogenase.

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2

Treem, William R., Jeffrey S. Hyams, Charles A. Stanley, Daniel E. Hale, and Harris B. Leopold. "Hypoglycemia, Hypotonia, and Cardiomyopathy: The Evolving Clinical Picture of Long-Chain Acyl-CoA Dehydrogenase Deficiency." Pediatrics 87, no. 3 (March 1, 1991): 328–33. http://dx.doi.org/10.1542/peds.87.3.328.

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Inherited defects in fatty acid oxidation, which have been described and diagnosed with increasing frequency in the last decade, are most commonly attributed to a deficiency in the activity of medium-chain acyl-CoA dehydrogenase. Few cases of the related enzyme defect of long-chain acyl-CoA dehydrogenase activity have been reported. An infant with documented long-chain acyl-CoA dehydrogenase deficiency is described with a detailed metabolic profile, long-term clinical follow-up, and response to treatment. This patient is compared with the seven previously published cases of this disorder in order to stress the unique features of the initial presentation, more subtle late manifestations of the disease, and clinical and biochemical differentiation from the more common medium-chain acyl-CoA dehydrogenase deficiency. This report stresses the enlarging spectrum of the clinical presentation and natural history of this defect in fatty acid oxidation.

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3

Cox, Keith B., Jian Liu, Liqun Tian, Stephen Barnes, Qinglin Yang, and Philip A. Wood. "Cardiac hypertrophy in mice with long-chain acyl-CoA dehydrogenase or very long-chain acyl-CoA dehydrogenase deficiency." Laboratory Investigation 89, no. 12 (September 7, 2009): 1348–54. http://dx.doi.org/10.1038/labinvest.2009.86.

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4

Yu, Wenfeng, Xiquan Liang, Regina E. Ensenauer, Jerry Vockley, Lawrence Sweetman, and Horst Schulz. "Leaky β-Oxidation of atrans-Fatty Acid." Journal of Biological Chemistry 279, no. 50 (October 4, 2004): 52160–67. http://dx.doi.org/10.1074/jbc.m409640200.

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The degradation of elaidic acid (9-trans-octadecenoic acid), oleic acid, and stearic acid by rat mitochondria was studied to determine whether the presence of atransdouble bond in place of acisdouble bond or no double bond affects β-oxidation. Rat mitochondria from liver or heart effectively degraded the coenzyme A derivatives of all three fatty acids. However, with elaidoyl-CoA as a substrate, a major metabolite accumulated in the mitochondrial matrix. This metabolite was isolated and identified as 5-trans-tetradecenoyl-CoA. In contrast, little or none of the corresponding metabolites were detected with oleoyl-CoA or stearoyl-CoA as substrates. A kinetic study of long-chain acyl-CoA dehydrogenase (LCAD) and very long-chain acyl-CoA dehydrogenase revealed that 5-trans-tetradecenoyl-CoA is a poorer substrate of LCAD than is 5-cis-tetradecenoyl-CoA, while both unsaturated acyl-CoAs are poor substrates of very long-chain acyl-CoA dehydrogenase when compared with myristoyl-CoA. Tetradecenoic acid and tetradecenoylcarnitine were detected by gas chromatography/mass spectrometry and tandem mass spectrometry, respectively, when rat liver mitochondria were incubated with elaidoyl-CoA but not when oleoyl-CoA was the substrate. These observations support the conclusion that 5-trans-tetradecenoyl-CoA accumulates in the mitochondrial matrix, because it is less efficiently dehydrogenated by LCAD than is itscisisomer and that the accumulation of this β-oxidation intermediate facilitates its hydrolysis and conversion to 5-trans-tetradecenoylcarnitine thereby permitting a partially degraded fatty acid to escape from mitochondria. Analysis of this compromised but functional process provides insight into the operation of β-oxidation in intact mitochondria.

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5

Wijayabandara, Maheshi, Champika Gamakaranage, and Dineshani Hettiarachchi. "Very-Long-Chain Acyl-Co-Enzyme A Dehydrogenase Deficiency Presenting as Rhabdomyolysis: First Case Report from Sri Lanka." Case Reports in Genetics 2020 (October 13, 2020): 1–5. http://dx.doi.org/10.1155/2020/8894518.

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Background. Rhabdomyolysis can be either inherited or acquired such as in metabolic myopathies. Very-long-chain acyl-CoA dehydrogenase deficiency is a rare fatty acid oxidation disorder which presents with different phenotypes, and the mild adult form can present as intermittent rhabdomyolysis. Here, we present the first adult case of very-long-chain acyl-CoA dehydrogenase deficiency presenting as rhabdomyolysis in a Sri Lankan patient. Case Presentation. A 36-year-old Sri Lankan man who was born to consanguineous parents presented with severe generalized muscle pain, stiffness, and dark-coloured urine for three days following prolonged low-intensity activity. Since fourteen years of age, he has had multiple similar episodes, where one episode was complicated with acute kidney injury. His eldest brother also suffered from the similar episode. Examination revealed only generalized muscle tenderness without any weakness. His creatine phosphokinase level was above 50,000 IU/L, and he had myoglobinuria. Molecular genetic tests confirmed the diagnosis of very-long-chain acyl-CoA dehydrogenase deficiency. Following a successful recovery devoid of complications, he remained asymptomatic with lifestyle adjustments. Conclusion. Very-long-chain acyl-CoA dehydrogenase deficiency is a rare inherited cause of metabolic myopathy that gives rise to intermittent rhabdomyolysis in adults. Prompt diagnosis is essential to prevent complications and prevent its recurrence.

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6

Liang, X., W. Le, D. Zhang, and H. Schulz. "Impact of the intramitochondrial enzyme organization on fatty acid oxidation." Biochemical Society Transactions 29, no. 2 (May 1, 2001): 279–82. http://dx.doi.org/10.1042/bst0290279.

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The enzymes of mitochondrial β-oxidation are thought to be organized in at least two functional complexes, a membrane-bound, long-chain-specific β-oxidation system and a matrix system consisting of soluble enzymes with preferences for medium-chain and short-chain substrates. This hypothesis is supported by the observation that the inactivation of long-chain 3-ketoacyl-CoA thiolase by 4-bromotiglic acid (4-bromo-2-methylbut-2-enoic acid) causes the complete inhibition of palmitate β-oxidation even though 3-ketoacyl-CoA thiolase, which acts on 3-ketopalmitoyl-CoA, remains partly active. The observed substrate specificities of long-chain acyl-CoA dehydrogenase (LCAD) and very-long-chain acyl-CoA dehydrogenase prompt the suggestion that LCAD is a functional component of the long-chain-specific β-oxidation system. Altogether, a view is emerging of the organization of β-oxidation enzymes in mitochondria that supports the idea of intermediate channelling and explains the apparent absence of true intermediates of β-oxidation from mitochondria.

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7

Yamaguchi, Seiji, Yasuhiro Indo, Paul M. Coates, Takashi Hashimoto, and Kay Tanaka. "Identification of Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency in Three Patients Previously Diagnosed with Long-Chain Acyl-CoA Dehydrogenase Deficiency." Pediatric Research 34, no. 1 (July 1993): 111–13. http://dx.doi.org/10.1203/00006450-199307000-00025.

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8

Costa, Catarina G., Lambertus Dorland, Ulbe Holwerda, Isabel Tavares de Almeida, Bwee-Tien Poll-The, Cornelis Jakobs, and Marinus Duran. "Simultaneous analysis of plasma free fatty acids and their 3-hydroxy analogs in fatty acid β-oxidation disorders." Clinical Chemistry 44, no. 3 (March 1, 1998): 463–71. http://dx.doi.org/10.1093/clinchem/44.3.463.

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Abstract We present a new derivatization procedure for the simultaneous gas chromatographic–mass spectrometric analysis of free fatty acids and 3-hydroxyfatty acids in plasma. Derivatization of target compounds involved trifluoroacetylation of hydroxyl groups and tert-butyldimethylsilylation of the carboxyl groups. This new derivatization procedure had the advantage of allowing the complete baseline separation of free fatty acids and 3-hydroxyfatty acids while the superior gas chromatographic and mass spectrometric properties of tert-butyldimethylsilyl derivatives remained unchanged, permitting a sensitive analysis of the target compounds. Thirty-nine plasma samples from control subjects and patients with known defects of mitochondrial fatty acid β-oxidation were analyzed. A characteristic increase of long-chain 3-hydroxyfatty acids was observed for all of the long-chain 3-hydroxyacyl-CoA dehydrogenase-deficient and mitochondrial trifunctional protein-deficient plasma samples. For medium-chain acyl-CoA dehydrogenase deficiency and very-long-chain acyl-CoA dehydrogenase deficiency, decenoic and tetradecenoic acids, respectively, were the main abnormal fatty acids, whereas the multiple acyl-CoA dehydrogenase-deficient patients showed variable increases of these unusual intermediates. The results showed that this selective and sensitive method is a powerful tool in the diagnosis and monitoring of mitochondrial fatty acid β-oxidation disorders.

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9

Nandy, Andreas, Volker Kieweg, Franz-Georg Kräutle, Petra Vock, Burkhard Küchler, Peter Bross, Jung-Ja P. Kim, Ihab Rasched, and Sandro Ghisla. "Medium-Long-Chain Chimeric Human Acyl-CoA Dehydrogenase: Medium-Chain Enzyme with the Active Center Base Arrangement of Long-Chain Acyl-CoA Dehydrogenase†." Biochemistry 35, no. 38 (January 1996): 12402–11. http://dx.doi.org/10.1021/bi960785e.

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10

Parsons, H. G., and V. C. Dias. "Intramitochondrial fatty acid metabolism: riboflavin deficiency and energy production." Biochemistry and Cell Biology 69, no. 7 (July 1, 1991): 490–97. http://dx.doi.org/10.1139/o91-073.

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Inborn errors of fatty acid β-oxidation have contributed significantly to our understanding of intracellular fatty acid metabolism. The first intramitochondrial step in β-oxidation of fatty acyl-CoA of different chain lengths is catalyzed by the three chain length specific acyl-CoA dehydrogenases. Inherited deficiency of these enzymes has been reported. Some are riboflavin responsive. The first step of fatty acid oxidation is reviewed with specific emphasis on β-oxidation in newborn infants, rendered riboflavin deficient by phototherapy. Given that medium chain fatty acids are not stored as triacylglycerols and undergo rapid β-oxidation, they have been proposed as superior substrates compared with long chain triglycerides in times of metabolic stress. This review also examines medium chain triglycerides as an alternate energy source. When medium chain triglycerides were fed as 50% of total energy, glucose sparing was present with little loss of energy as dicarboxylic acids.Key words: β-oxidation, acyl-CoA dehydrogenase, riboflavin, medium chain triglycerides, dicarboxylic acids.

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11

THORPE, Colin, Thomas L. CIARDELLI, Charles J. STEWART, and Theodor WIELAND. "Interaction of Long-Chain Acyl-CoA Analogs with Pig Kidney General Acyl-CoA Dehydrogenase." European Journal of Biochemistry 118, no. 2 (March 3, 2005): 279–82. http://dx.doi.org/10.1111/j.1432-1033.1981.tb06397.x.

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12

Indo, Yasuhiro, Paul M. Coates, Daniel E. Hale, and Kay Tanaka. "Immunochemical Characterization of Variant Long-Chain Acyl-CoA Dehydrogenase in Cultured Fibroblasts from Nine Patients with Long-Chain Acyl-CoA Dehydrogenase Deficiency." Pediatric Research 30, no. 3 (September 1991): 211–15. http://dx.doi.org/10.1203/00006450-199109000-00001.

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13

Thapa, Dharendra, Manling Zhang, Janet R. Manning, Danielle A. Guimarães, Michael W. Stoner, Robert M. O’Doherty, Sruti Shiva, and Iain Scott. "Acetylation of mitochondrial proteins by GCN5L1 promotes enhanced fatty acid oxidation in the heart." American Journal of Physiology-Heart and Circulatory Physiology 313, no. 2 (August 1, 2017): H265—H274. http://dx.doi.org/10.1152/ajpheart.00752.2016.

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Lysine acetylation is a reversible posttranslational modification and is particularly important in the regulation of mitochondrial metabolic enzymes. Acetylation uses acetyl-CoA derived from fuel metabolism as a cofactor, thereby linking nutrition to metabolic activity. In the present study, we investigated how mitochondrial acetylation status in the heart is controlled by food intake and how these changes affect mitochondrial metabolism. We found that there was a significant increase in cardiac mitochondrial protein acetylation in mice fed a long-term high-fat diet and that this change correlated with an increase in the abundance of the mitochondrial acetyltransferase-related protein GCN5L1. We showed that the acetylation status of several mitochondrial fatty acid oxidation enzymes (long-chain acyl-CoA dehydrogenase, short-chain acyl-CoA dehydrogenase, and hydroxyacyl-CoA dehydrogenase) and a pyruvate oxidation enzyme (pyruvate dehydrogenase) was significantly upregulated in high-fat diet-fed mice and that the increase in long-chain and short-chain acyl-CoA dehydrogenase acetylation correlated with increased enzymatic activity. Finally, we demonstrated that the acetylation of mitochondrial fatty acid oxidation proteins was decreased after GCN5L1 knockdown and that the reduced acetylation led to diminished fatty acid oxidation in cultured H9C2 cells. These data indicate that lysine acetylation promotes fatty acid oxidation in the heart and that this modification is regulated in part by the activity of GCN5L1. NEW & NOTEWORTHY Recent research has shown that acetylation of mitochondrial fatty acid oxidation enzymes has greatly contrasting effects on their activity in different tissues. Here, we provide new evidence that acetylation of cardiac mitochondrial fatty acid oxidation enzymes by GCN5L1 significantly upregulates their activity in diet-induced obese mice.

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14

Cox, K. B. "Gestational, pathologic and biochemical differences between very long-chain acyl-CoA dehydrogenase deficiency and long-chain acyl-CoA dehydrogenase deficiency in the mouse." Human Molecular Genetics 10, no. 19 (September 1, 2001): 2069–77. http://dx.doi.org/10.1093/hmg/10.19.2069.

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15

Rudolf, Jeffrey D., Liao-Bin Dong, Tingting Huang, and Ben Shen. "A genetically amenable platensimycin- and platencin-overproducer as a platform for biosynthetic explorations: a showcase of PtmO4, a long-chain acyl-CoA dehydrogenase." Molecular BioSystems 11, no. 10 (2015): 2717–26. http://dx.doi.org/10.1039/c5mb00303b.

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16

FOX, Simon R., Lionel M. HILL, Stephen RAWSTHORNE, and Matthew J. HILLS. "Inhibition of the glucose-6-phosphate transporter in oilseed rape (Brassica napus L.) plastids by acyl-CoA thioesters reduces fatty acid synthesis." Biochemical Journal 352, no. 2 (November 24, 2000): 525–32. http://dx.doi.org/10.1042/bj3520525.

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Addition of oleoyl-CoA (1µM), or other acyl-CoA thioesters with a chain length of C16 or greater, to oilseed rape plastids (Brassica napus L.) inhibited the rate of D-glucose 6-phosphate (Glc6P) uptake by 70% after 2min. The IC50 value for oleoyl-CoA inhibition of the transporter was approx. 0.2–0.3µM. Inhibition was alleviated by the addition of acyl-CoA binding protein (ACBP) or BSA at slightly higher concentrations. Oleic acid (5–25µM), Tween 40 (10µM), Triton-X 100 (10µM) and palmitoylcarnitine (5µM) had no effect on Glc6P uptake. The uptake of [1-14C]Glc6P occurred in exchange for Pi, 3-phosphoglycerate or Glc6P at a typical rate of 30nmol Glc6P/min per unit of glyceraldehyde-3-phosphate dehydrogenase (NADP+). The Km(app) of the Glc6P transporter for Glc6P was 100µM. Neither CoA (0.3mM) nor ATP (3mM) inhibited Glc6P uptake, but the transporter was inhibited by 72% when ATP and CoA were added together. This inhibition was attributable to the synthesis of acyl-CoA thioesters, predominantly oleoyl-CoA and palmitoyl-CoA, by long-chain fatty acid-CoA ligase (EC 6.2.1.3) from endogenous fatty acids in the plastid preparations. Acyl-CoA thioesters did not inhibit the uptake of [2-14C]pyruvate or D-[1-14C]glucose into plastids. In vivo quantities of oleoyl-CoA and other long-chain acyl-CoA thioesters were lower than those for ACBP in early cotyledonary embryos, 0.7±0.2pmol/embryo and 2.2±0.2pmol/embryo respectively, but in late cotyledonary embryos quantities of long-chain acyl-CoA thioesters were greater than ACBP, 3±0.4pmol/embryo and 1.9±0.2pmol/embryo respectively.

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17

Nandy, A., B. Küchler, and S. Ghisla. "Molecular evolution and substrate specificity of acyl-CoA dehydrogenases: Chimaeric ‘medium/long’ chain-specific enzyme from medium-chain acyl-CoA dehydrogenase." Biochemical Society Transactions 24, no. 1 (February 1, 1996): 105–10. http://dx.doi.org/10.1042/bst0240105.

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18

Tenopoulou, Margarita, Jie Chen, Jean Bastin, Michael J. Bennett, Harry Ischiropoulos, and Paschalis-Thomas Doulias. "Strategies for Correcting Very Long Chain Acyl-CoA Dehydrogenase Deficiency." Journal of Biological Chemistry 290, no. 16 (March 3, 2015): 10486–94. http://dx.doi.org/10.1074/jbc.m114.635102.

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19

Senefeld, Carly M., and Jonathon W. Senefeld. "Very long-chain acyl-CoA dehydrogenase deficiency nomenclature: compound heterozygosity." Journal of Human Genetics 65, no. 4 (January 27, 2020): 435–36. http://dx.doi.org/10.1038/s10038-020-0727-9.

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20

Fatehi, F., A. A. Okhovat, Y. Nilipour, M. Mroczek, V. Straub, A. Töpf, A. Palibrk, et al. "Adult‐onset very‐long‐chain acyl‐CoA dehydrogenase deficiency (VLCADD)." European Journal of Neurology 27, no. 11 (July 24, 2020): 2257–66. http://dx.doi.org/10.1111/ene.14402.

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21

Kakimoto, Pâmela A. H. B., Fábio K. Tamaki, Ariel R. Cardoso, Sandro R. Marana, and Alicia J. Kowaltowski. "H2O2 release from the very long chain acyl-CoA dehydrogenase." Redox Biology 4 (April 2015): 375–80. http://dx.doi.org/10.1016/j.redox.2015.02.003.

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22

Vellekoop, P., E. F. Diekman, I. van Tuijl, M. M. C. de Vries, P. M. van Hasselt, and G. Visser. "Perioperative measures in very long chain acyl-CoA dehydrogenase deficiency." Molecular Genetics and Metabolism 103, no. 1 (May 2011): 96–97. http://dx.doi.org/10.1016/j.ymgme.2011.01.010.

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23

Murata, Ken-ya, Hideo Sugie, Ichizo Nishino, Tomoyoshi Kondo, and Hidefumi Ito. "A primigravida with very-long-chain acyl-CoA dehydrogenase deficiency." Muscle & Nerve 49, no. 2 (January 16, 2014): 295–96. http://dx.doi.org/10.1002/mus.24055.

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24

Alatibi, Khaled I., Judith Hagenbuchner, Zeinab Wehbe, Daniela Karall, Michael J. Ausserlechner, Jerry Vockley, Ute Spiekerkoetter, Sarah C. Grünert, and Sara Tucci. "Different Lipid Signature in Fibroblasts of Long-Chain Fatty Acid Oxidation Disorders." Cells 10, no. 5 (May 18, 2021): 1239. http://dx.doi.org/10.3390/cells10051239.

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Long-chain fatty acid oxidation disorders (lc-FAOD) are a group of diseases affecting the degradation of long-chain fatty acids. In order to investigate the disease specific alterations of the cellular lipidome, we performed undirected lipidomics in fibroblasts from patients with carnitine palmitoyltransferase II, very long-chain acyl-CoA dehydrogenase, and long-chain 3-hydroxyacyl-CoA dehydrogenase. We demonstrate a deep remodeling of mitochondrial cardiolipins. The aberrant phosphatidylcholine/phosphatidylethanolamine ratio and the increased content of plasmalogens and of lysophospholipids support the theory of an inflammatory phenotype in lc-FAOD. Moreover, we describe increased ratios of sphingomyelin/ceramide and sphingomyelin/hexosylceramide in LCHAD deficiency which may contribute to the neuropathic phenotype of LCHADD/mitochondrial trifunctional protein deficiency.

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25

Oey, N. A., J. P. N. Ruiter, L. IJlst, T. Attie-Bitach, M. Vekemans, R. J. A. Wanders, and F. A. Wijburg. "Acyl-CoA dehydrogenase 9 (ACAD 9) is the long-chain acyl-CoA dehydrogenase in human embryonic and fetal brain." Biochemical and Biophysical Research Communications 346, no. 1 (July 2006): 33–37. http://dx.doi.org/10.1016/j.bbrc.2006.05.088.

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26

Crawford, Sarah, Elizabeth Sablon, Nadia Ali, Ami R. Rosen, Patricia L. Hall, and Juanita Neira Fresneda. "Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency: Family Impact and Perspectives." International Journal of Neonatal Screening 9, no. 4 (October 6, 2023): 53. http://dx.doi.org/10.3390/ijns9040053.

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Very-Long-Chain Acyl-CoA Dehydrogenase Deficiency (VLCADD) is a fatty acid oxidation disorder characterized by the decreased ability of the enzyme very-long-chain acyl-CoA dehydrogenase to break down fatty acids with 14 to 20-long carbon chains. The resulting clinical manifestations are variable in severity and include hypoketotic hypoglycemia, rhabdomyolysis, and cardiomyopathy. Treatment can consist of limiting the dietary intake of long-chain fatty acids, the prevention of fasting, and the supplementation of medium-chain fats. This study, conducted in the context of a 5-year long-term follow-up on VLCADD, evaluates how the diagnosis of this fatty acid disorder impacts the family, specifically as it relates to the medical diet and barriers to care. Caregivers (n = 10) of individuals with VLCADD responded to a survey about how VLCADD potentially impacts their family. The review included the clinical outcomes of the patients (n = 11), covering instances of rhabdomyolysis, cardiomyopathy, and hospitalizations related to VLCADD. Families affected by VLCADD experience barriers to care, including difficulties with finances, ability to work, and access to nutrition.

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27

Marcì, Marcello, and Patrizia Ajovalasit. "Medium-Chain Acyl-CoA Dehydrogenase Deficiency in an Infant with Dilated Cardiomyopathy." Cardiology Research and Practice 2009 (2009): 1–3. http://dx.doi.org/10.4061/2009/281389.

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We report about an infant affected by dilated cardiomyopathy (CMP) in whom metabolic investigations evidenced medium-chain-acyl-CoA dehydrogenase deficiency (MCADD), that is one of three types of inherited disorders of mitochondrial fatty-acid -oxidation. Long-chain and very long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficits are recognized as responsible of hypertrophic or, less frequently, dilated cardiomyopathy (CMP) in childhood. Otherwise, to our knowledge, no case of MCADD associated to dilated CMP has been reported in literature.

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28

Alatibi, Khaled I., Stefan Tholen, Zeinab Wehbe, Judith Hagenbuchner, Daniela Karall, Michael J. Ausserlechner, Oliver Schilling, Sarah C. Grünert, Jerry Vockley, and Sara Tucci. "Lipidomic and Proteomic Alterations Induced by Even and Odd Medium-Chain Fatty Acids on Fibroblasts of Long-Chain Fatty Acid Oxidation Disorders." International Journal of Molecular Sciences 22, no. 19 (September 29, 2021): 10556. http://dx.doi.org/10.3390/ijms221910556.

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Medium-chain fatty acids (mc-FAs) are currently applied in the treatment of long-chain fatty acid oxidation disorders (lc-FAOD) characterized by impaired β-oxidation. Here, we performed lipidomic and proteomic analysis in fibroblasts from patients with very long-chain acyl-CoA dehydrogenase (VLCADD) and long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHADD) deficiencies after incubation with heptanoate (C7) and octanoate (C8). Defects of β-oxidation induced striking proteomic alterations, whereas the effect of treatment with mc-FAs was minor. However, mc-FAs induced a remodeling of complex lipids. Especially C7 appeared to act protectively by restoring sphingolipid biosynthesis flux and improving the observed dysregulation of protein homeostasis in LCHADD under control conditions.

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29

Onkenhout, W., V. Venizelos, P. F. van der Poel, M. P. van den Heuvel, and B. J. Poorthuis. "Identification and quantification of intermediates of unsaturated fatty acid metabolism in plasma of patients with fatty acid oxidation disorders." Clinical Chemistry 41, no. 10 (October 1, 1995): 1467–74. http://dx.doi.org/10.1093/clinchem/41.10.1467.

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Abstract The free fatty acid and total fatty acid profiles in plasma of nine patients with medium-chain acyl-CoA dehydrogenase (MCAD) deficiency, two with very-long-chain acyl-CoA dehydrogenase (VLCAD) deficiency and two with mild-type multiple acyl-CoA dehydrogenase (MAD-m) deficiency, were analyzed by gas chromatography-mass spectrometry. In the plasma of patients with MCAD deficiency we found increases of octanoic acid (8:0), decanoic acid (10:0), 4-decenoic acid (10:1 omega 6), and 4,7-decadienoic acid (10:2 omega 3), all present almost exclusively in free form. The patients with VLCAD deficiency showed increases of mainly 5-tetradecenoic acid (14:1 omega 9) and to a minor extent 5-dodecenoic acid (12:1 omega 7), 5,8-tetradecadienoic acid (14:2 omega 6), and 7,10-hexadecadienoic acid (16:2 omega 6), in both the free and esterified fatty acid fraction. The MAD-m patients showed variable increases of all the unusual fatty acids present in MCAD- and VLCAD-deficient plasma. The 14:1 omega 9, 14:2 omega 6, and 16:2 omega 6 fatty acids were present mainly in the esterified form. Measurement of these fatty acids in plasma by the relatively simple method presented here provides a sensitive and specific aid in the diagnosis of acyl-CoA dehydrogenase deficiency disorders.

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30

Eaton, S., T. Bursby, B. Middleton, M. Pourfarzam, K. Mills, A. W. Johnson, and K. Bartlecc. "The mitochondrial trifunctional protein: centre of a β-oxidation metabolon?" Biochemical Society Transactions 28, no. 2 (February 1, 2000): 177–82. http://dx.doi.org/10.1042/bst0280177.

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The trifunctional enzyme comprises three consecutive steps in the mitochondrial β-oxidation of long-chain acyl-CoA esters: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-ketoacyl-CoA thiolase. Deficiencies in either 3-hydroxyacyl-CoA dehydrogenase activity, or all three activities, are important causes of human disease. The dehydrogenase and thiolase have a requirement for NAD+ and CoA respectively, whose levels are conserved within the mitochondrion and thus provide possible means for control and regulation of β-oxidation. Using analysis of the intact CoA ester intermediates produced by the complex, we have examined the sensitivity of the complex to NAD+/NADH and acetyl-CoA. We consider the evidence for channelling within the trifunctional protein and propose a model for a β-oxidation ‘metabolon’.

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31

Sauer, Sven W., Jürgen G. Okun, Marina A. Schwab, Linda R. Crnic, Georg F. Hoffmann, Stephen I. Goodman, David M. Koeller, and Stefan Kölker. "Bioenergetics in Glutaryl-Coenzyme A Dehydrogenase Deficiency." Journal of Biological Chemistry 280, no. 23 (April 19, 2005): 21830–36. http://dx.doi.org/10.1074/jbc.m502845200.

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Inherited deficiency of glutaryl-CoA dehydrogenase results in an accumulation of glutaryl-CoA, glutaric, and 3-hydroxyglutaric acids. If untreated, most patients suffer an acute encephalopathic crisis and, subsequently, acute striatal damage being precipitated by febrile infectious diseases during a vulnerable period of brain development (age 3 and 36 months). It has been suggested before that some of these organic acids may induce excitotoxic cell damage, however, the relevance of bioenergetic impairment is not yet understood. The major aim of our study was to investigate respiratory chain, tricarboxylic acid cycle, and fatty acid oxidation in this disease using purified single enzymes and tissue homogenates from Gcdh-deficient and wild-type mice. In purified enzymes, glutaryl-CoA but not glutaric or 3-hydroxyglutaric induced an uncompetitive inhibition of α-ketoglutarate dehydrogenase complex activity. Notably, reduced activity of α-ketoglutarate dehydrogenase activity has recently been demonstrated in other neurodegenerative diseases, such as Alzheimer, Parkinson, and Huntington diseases. In contrast to α-ketoglutarate dehydrogenase complex, no direct inhibition of glutaryl-CoA, glutaric acid, and 3-hydroxyglutaric acid was found in other enzymes tested. In Gcdh-deficient mice, respiratory chain and tricarboxylic acid activities remained widely unaffected, virtually excluding regulatory changes in these enzymes. However, hepatic activity of very long-chain acyl-CoA dehydrogenase was decreased and concentrations of long-chain acylcarnitines increased in the bile of these mice, which suggested disturbed oxidation of long-chain fatty acids. In conclusion, our results demonstrate that bioenergetic impairment may play an important role in the pathomechanisms underlying neurodegenerative changes in glutaryl-CoA dehydrogenase deficiency.

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32

Diekman, Eugène F., Michel van Weeghel, Mayte Suárez-Fariñas, Carmen Argmann, Pablo Ranea-Robles, Ronald J. A. Wanders, Gepke Visser, Ingeborg van der Made, Esther E. Creemers, and Sander M. Houten. "Dietary restriction in the long-chain acyl-CoA dehydrogenase knockout mouse." Molecular Genetics and Metabolism Reports 27 (June 2021): 100749. http://dx.doi.org/10.1016/j.ymgmr.2021.100749.

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33

Djordjevic, Snezana, Yu Dong, Rosemary Paschke, Frank E. Frerman, Arnold W. Strauss, and Jung-Ja P. Kim. "Identification of the Catalytic Base in Long Chain Acyl-CoA Dehydrogenase." Biochemistry 33, no. 14 (April 12, 1994): 4258–64. http://dx.doi.org/10.1021/bi00180a021.

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34

Schrijver-Wieling, I., G. H. M. B. van Rens, D. Wittebol-Post, J. A. M. Smeitink, J. P. de Jager, H. B. C. de Klerk, and G. H. M. van Lith. "Retinal dystrophy in long chain 3-hydroxy-acyl-coA dehydrogenase deficiency." British Journal of Ophthalmology 81, no. 4 (April 1, 1997): 291–94. http://dx.doi.org/10.1136/bjo.81.4.291.

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35

Andresen, B. S., C. Vianey-Saban, P. Bross, P. Divry, C. R. Roe, M. A. Nada, I. Knudsen, and N. Gregersen. "The mutational spectrum in very long-chain acyl-CoA dehydrogenase deficiency." Journal of Inherited Metabolic Disease 19, no. 2 (March 1996): 169–72. http://dx.doi.org/10.1007/bf01799421.

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36

Mason, Katherine E., Daniel A. Stofan, and Luke I. Szweda. "Inhibition of very long chain acyl-CoA dehydrogenase during cardiac ischemia." Archives of Biochemistry and Biophysics 437, no. 2 (May 2005): 138–43. http://dx.doi.org/10.1016/j.abb.2005.03.004.

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37

Winter, Susan, Neil R. M. Buist, Nicola Longo, Saro H. Armenian, Gary Lopaschuk, and Anna Wasilewska. "Round Table Discussion." Annals of Nutrition and Metabolism 68, Suppl. 3 (2016): 21–23. http://dx.doi.org/10.1159/000448323.

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The 1st International Carnitine Working Group concluded with a round table discussion addressing several areas of relevance. These included the design of future studies that could increase the amount of evidence-based data about the role of carnitine in the treatment of fatty acid oxidation defects, for which substantial controversy still exists. There was general consensus that future trials on the effect of carnitine in disorders of fatty acid oxidation should be randomized, double-blinded, multicentered and minimally include the following diagnoses: medium-chain acyl coenzyme A (CoA) dehydrogenase deficiency, very long-chain acyl-CoA dehydrogenase deficiency, long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency and mitochondrial trifunctional protein deficiency. Another area that generated interest was trials of carnitine in cardiomyopathy and, especially, the use of biomarkers to identify patients at greater risk of cardiotoxicity following treatment with anthracyclines. The possibility that carnitine treatment may lead to improvements in autistic behaviors was also discussed, although the evidence is still not sufficient to make any firm conclusions in this regard. Preliminary data on carnitine levels in children and adolescents with primary hypertension, low birth weight and nephrotic syndrome was also presented. Lastly, the panelists stressed that there remains an objective need to harmonize the terminology used to describe carnitine deficiencies (e.g., primary, secondary and systemic deficiency).

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38

Letteron, P., N. Brahimi-Bourouina, M. A. Robin, A. Moreau, G. Feldmann, and D. Pessayre. "Glucocorticoids inhibit mitochondrial matrix acyl-CoA dehydrogenases and fatty acid beta-oxidation." American Journal of Physiology-Gastrointestinal and Liver Physiology 272, no. 5 (May 1, 1997): G1141—G1150. http://dx.doi.org/10.1152/ajpgi.1997.272.5.g1141.

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Glucocorticoid administration may produce fatty liver in humans. We investigated the effects of dexamethasone on hepatic mitochondria and lipid metabolism in mice. Dexamethasone 21-phosphate (20 microM) did not inhibit the mitochondrial inner membrane-bound very-long-chain acyl-CoA dehydrogenase but inhibited the matrixlocated long-, medium-, and short-chain dehydrogenases. Dexamethasone 21-phosphate (20 microM) inhibited the first beta-oxidation cycle of [1-(14C)]butyric acid and [1-(14C)]octanoic acid but not that of [1-(14C)]palmitic acid. Administration of dexamethasone 21-phosphate (100 mg/kg) decreased the in vivo oxidation of [1-(14C)]butyric acid and [1-(14C)]octanoic acid into [14C]CO2 but not that of [1-(14C)]palmitic acid and decreased the hepatic secretion of triglycerides. After 5 days of treatment (100 mg/kg daily), hepatic triglycerides were increased and both microvesicular steatosis and ultrastructural mitochondrial lesions were present. In conclusion, glucocorticoids inhibit medium- and short-chain acyl-CoA dehydrogenation and hepatic lipid secretion in mice. These effects may account for their steatogenic effects in humans.

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39

Chen, Xiaobo, Jiayue Chen, Bing Yan, Wei Zhang, Luke W. Guddat, Xiang Liu, and Zihe Rao. "Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria." Proceedings of the National Academy of Sciences 117, no. 28 (June 29, 2020): 16324–32. http://dx.doi.org/10.1073/pnas.2002835117.

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FadE, an acyl-CoA dehydrogenase, introduces unsaturation to carbon chains in lipid metabolism pathways. Here, we report that FadE5 fromMycobacterium tuberculosis(MtbFadE5) andMycobacterium smegmatis(MsFadE5) play roles in drug resistance and exhibit broad specificity for linear acyl-CoA substrates but have a preference for those with long carbon chains. Here, the structures ofMsFadE5 andMtbFadE5, in the presence and absence of substrates, have been determined. These reveal the molecular basis for the broad substrate specificity of these enzymes. FadE5 interacts with the CoA region of the substrate through a large number of hydrogen bonds and an unusual π–π stacking interaction, allowing these enzymes to accept both short- and long-chain substrates. Residues in the substrate binding cavity reorient their side chains to accommodate substrates of various lengths. Longer carbon-chain substrates make more numerous hydrophobic interactions with the enzyme compared with the shorter-chain substrates, resulting in a preference for this type of substrate.

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40

Katagiri, Hideki, Tomoichiro Asano, Tetsuya Yamada, Toshifumi Aoyama, Yasushi Fukushima, Masatoshi Kikuchi, Tatsuhiko Kodama, and Yoshitomo Oka. "Acyl-Coenzyme A Dehydrogenases Are Localized on GLUT4-Containing Vesicles via Association with Insulin-Regulated Aminopeptidase in a Manner Dependent on Its Dileucine Motif." Molecular Endocrinology 16, no. 5 (May 1, 2002): 1049–59. http://dx.doi.org/10.1210/mend.16.5.0831.

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Abstract Insulin-regulated aminopeptidase (IRAP, also termed vp165) is known to be localized on the GLUT4-containing vesicles and to be recruited to the plasma membrane after stimulation with insulin. The cytoplasmic region of IRAP contains two dileucine motifs and acidic regions, one of which (amino acid residues 55–82) is reportedly involved in retention of GLUT4-containing vesicles. The region of IRAP fused with glutathione-S-transferase [GST-IRAP(55–82)] was incubated with lysates from 3T3-L1 adipocytes, leading to identification of long-chain, medium-chain, and short-chain acyl-coenzyme A dehydrogenases (ACDs) as the proteins associated with IRAP. The association was nearly abolished by mutation of the dileucine motif of IRAP. Immunoblotting of fractions prepared from sucrose gradient ultracentrifugation and vesicles immunopurified with anti-GLUT4 antibody revealed these ACDs to be localized on GLUT4-containing vesicles. Furthermore, 3-mercaptopropionic acid and hexanoyl-CoA, inhibitors of long-chain and medium-chain ACDs, respectively, induced dissociation of long-chain acyl-coenzyme A dehydrogenase and/or medium-chain acyl-coenzyme A dehydrogenase from IRAP in vitro as well as recruitment of GLUT4 to the plasma membrane and stimulation of glucose transport activity in permeabilized 3T3-L1 adipocytes. These findings suggest that ACDs are localized on GLUT4-containing vesicles via association with IRAP in a manner dependent on its dileucine motif and play a role in retention of GLUT4-containing vesicles to an intracellular compartment.

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41

Zytkovicz, Thomas H., Eileen F. Fitzgerald, Deborah Marsden, Cecilia A. Larson, Vivian E. Shih, Donna M. Johnson, Arnold W. Strauss, Anne Marie Comeau, Roger B. Eaton, and George F. Grady. "Tandem Mass Spectrometric Analysis for Amino, Organic, and Fatty Acid Disorders in Newborn Dried Blood Spots." Clinical Chemistry 47, no. 11 (November 1, 2001): 1945–55. http://dx.doi.org/10.1093/clinchem/47.11.1945.

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Abstract Background: Tandem mass spectrometry (MS/MS) is rapidly being adopted by newborn screening programs to screen dried blood spots for >20 markers of disease in a single assay. Limited information is available for setting the marker cutoffs and for the resulting positive predictive values. Methods: We screened >160 000 newborns by MS/MS. The markers were extracted from blood spots into a methanol solution with deuterium-labeled internal standards and then were derivatized before analysis by MS/MS. Multiple reaction monitoring of each sample for the markers of interest was accomplished in ∼1.9 min. Cutoffs for each marker were set at 6–13 SD above the population mean. Results: We identified 22 babies with amino acid disorders (7 phenylketonuria, 11 hyperphenylalaninemia, 1 maple syrup urine disease, 1 hypermethioninemia, 1 arginosuccinate lyase deficiency, and 1 argininemia) and 20 infants with fatty and organic acid disorders (10 medium-chain acyl-CoA dehydrogenase deficiencies, 5 presumptive short-chain acyl-CoA dehydrogenase deficiencies, 2 propionic acidemias, 1 carnitine palmitoyltransferase II deficiency, 1 methylcrotonyl-CoA carboxylase deficiency, and 1 presumptive very-long chain acyl-CoA dehydrogenase deficiency). Approximately 0.3% of all newborns screened were flagged for either amino acid or acylcarnitine markers; approximately one-half of all the flagged infants were from the 5% of newborns who required neonatal intensive care or had birth weights <1500 g. Conclusions: In screening for 23 metabolic disorders by MS/MS, an mean positive predictive value of 8% can be achieved when using cutoffs for individual markers determined empirically on newborns.

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42

Damore, Mary Beth, Charles R. Roe, Teresia Goldberg, Mohammed A. Nada, Christine Vlaney-Saban, and Alfred E. Slonim. "DIAGNOSIS AND TREATMENT OF VERY-LONG-CHAIN ACYL CoA DEHYDROGENASE DEFICIENCY.846." Pediatric Research 39 (April 1996): 143. http://dx.doi.org/10.1203/00006450-199604001-00868.

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43

Kabuyama, Yukihito, Toshiyuki Suzuki, Naomi Nakazawa, Junko Yamaki, Miwako K. Homma, and Yoshimi Homma. "Dysregulation of very long chain acyl-CoA dehydrogenase coupled with lipid peroxidation." American Journal of Physiology-Cell Physiology 298, no. 1 (January 2010): C107—C113. http://dx.doi.org/10.1152/ajpcell.00231.2009.

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Idiopathic pulmonary fibrosis (IPF) is a chronic progressive lung disease of unknown etiology. We previously revealed increased oxidative stress and high expression of antioxidant proteins in culture cell lines established from lesional lung tissues with IPF (Kabuyama Y, Oshima K, Kitamura T, Homma M, Yamaki J, Munakata M, Homma Y. Genes Cells 12: 1235–1244, 2007). In this study, we show that IPF cells contain high levels of free cholesterol and its peroxidized form as compared with normal TIG7 lung fibroblasts, suggesting that radical oxygen species (ROS) are generated within specific organelles. To understand the molecular basis underlying the generation of ROS in IPF cells, we performed proteomic analysis of mitochondrial proteins from TIG and IPF cells. This analysis shows that the phosphorylation of Ser586 of very long chain acyl-CoA dehydrogenase (VLCAD) is significantly reduced in IPF cells. Similar results are obtained from immunoblotting with anti-pS586 antibody. Kinase activity toward a peptide containing Ser586 from IPF cells is significantly lower than that from TIG cells. Furthermore, a phosphorylation-negative mutant (S586A) VLCAD shows reduced electron transfer activity and a strong dominant-negative effect on fatty acid β-oxidation. The ectopic expression of the S586A mutant induced human embryonic kidney (HEK) 293 cells to produce significantly high amounts of oxidized lipids and hydrogen peroxide. HEK293 cells expressing the S586A mutant exhibit a reduction in cell growth and an enhancement in apoptosis. These results suggest a novel regulatory mechanism for homeostatic VLCAD activity, whose dysregulation might be involved in the production of oxidative stress and in the pathogenesis of IPF.

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44

Andresen, B. S., S. Olpin, E. A. Kvittingen, P. Augoustides-Savvopoulou, D. Lindhout, D. J. J. Halley, C. Vianey-Saban, et al. "DNA-based prenatal diagnosis for very-long- chain acyl-CoA dehydrogenase deficiency." Journal of Inherited Metabolic Disease 22, no. 3 (May 1999): 281–85. http://dx.doi.org/10.1023/a:1005558828223.

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45

Eminoglu, Tuba F., Leyla Tumer, Ilyas Okur, Fatih S. Ezgu, Gursel Biberoglu, and Alev Hasanoglu. "Very long-chain acyl CoA dehydrogenase deficiency which was accepted as infanticide." Forensic Science International 210, no. 1-3 (July 2011): e1-e3. http://dx.doi.org/10.1016/j.forsciint.2011.04.003.

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46

Maher, Amy C., Al-Walid Mohsen, Jerry Vockley, and Mark A. Tarnopolsky. "Low expression of long-chain acyl-CoA dehydrogenase in human skeletal muscle." Molecular Genetics and Metabolism 100, no. 2 (June 2010): 163–67. http://dx.doi.org/10.1016/j.ymgme.2010.03.011.

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47

Schiff, Manuel, Al-Walid Mohsen, Anuradha Karunanidhi, Elizabeth McCracken, Renita Yeasted, and Jerry Vockley. "Molecular and cellular pathology of very-long-chain acyl-CoA dehydrogenase deficiency." Molecular Genetics and Metabolism 109, no. 1 (May 2013): 21–27. http://dx.doi.org/10.1016/j.ymgme.2013.02.002.

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48

Spiekerkoetter, Ute, Chonan Tokunaga, Udo Wendel, Ertan Mayatepek, Lodewijk Ijlst, Frederic M. Vaz, Naomi Van Vlies, et al. "Tissue Carnitine Homeostasis in Very-Long-Chain Acyl-CoA Dehydrogenase–Deficient Mice." Pediatric Research 57, no. 6 (June 2005): 760–64. http://dx.doi.org/10.1203/01.pdr.0000157915.26049.47.

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49

Orii, Koji O., Toshifumi Aoyama, Fumiko Saito-Ohara, Tatsuro Ikeuchi, Tadao Orii, Naomi Kondo, and Takashi Hashimoto. "Molecular characterization of the mouse very-long-chain acyl-CoA dehydrogenase gene." Mammalian Genome 8, no. 7 (July 1997): 516–18. http://dx.doi.org/10.1007/s003359900488.

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50

Hesse, Julia, Carina Braun, Sidney Behringer, Uta Matysiak, Ute Spiekerkoetter, and Sara Tucci. "The diagnostic challenge in very-long chain acyl-CoA dehydrogenase deficiency (VLCADD)." Journal of Inherited Metabolic Disease 41, no. 6 (September 7, 2018): 1169–78. http://dx.doi.org/10.1007/s10545-018-0245-5.

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