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[PMID]: 28790927
[Au] Autor:Quinzii CM; Luna-Sanchez M; Ziosi M; Hidalgo-Gutierrez A; Kleiner G; Lopez LC
[Ad] Address:Department of Neurology, Columbia University Medical CenterNew York, NY, United States.
[Ti] Title:The Role of Sulfide Oxidation Impairment in the Pathogenesis of Primary CoQ Deficiency.
[So] Source:Front Physiol;8:525, 2017.
[Is] ISSN:1664-042X
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Coenzyme Q (CoQ) is a lipid present in all cell membranes. One of the multiple metabolic functions of CoQ is to transport electrons in the reaction catalyzed by sulfide:quinone oxidoreductase (SQOR), the first enzyme of the oxidation pathway of sulfides (hydrogen sulfide, H S). Early evidence of a defect in the metabolism of H S in primary CoQ deficiency came from yeast studies in strains defective for and (homologs of and , respectively), which have H S accumulation. Our recent studies in human skin fibroblasts and in murine models of primary CoQ deficiency show that, also in mammals, decreased CoQ levels cause impairment of H S oxidation. Patient fibroblasts carrying different mutations in genes encoding proteins involved in CoQ biosynthesis show reduced SQOR activity and protein levels proportional to the levels of CoQ. In mice, kidney, the only organ clinically affected, shows reduced SQOR levels and downstream enzymes, accumulation of H S, and glutathione depletion. mice have also low levels of thiosulfate in plasma and urine, and increased C4-C6 acylcarnitines in blood, due to inhibition of short-chain acyl-CoA dehydrogenase. Also in mice, the symptomatic organ, cerebrum, shows accumulation of H S, reduced SQOR, increase in thiosulfate sulfurtransferase and sulfite oxidase, and reduction in the levels of glutathione and glutathione enzymes, leading to alteration of the biosynthetic pathways of glutamate, serotonin, and catecholamines. mice have also reduced blood pressure, possible consequence of H S-induced vasorelaxation. Since liver is not clinically affected in and mutant mice, the effects of the impairment of H S oxidation in this organ were not investigated, despite its critical role in metabolism. In conclusion, and studies of CoQ deficient models provide evidence of tissue-specific H S oxidation impairment, an additional pathomechanism that should be considered in the understanding and treatment of primary CoQ deficiency.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1708
[Cu] Class update date: 170812
[Lr] Last revision date:170812
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.3389/fphys.2017.00525

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[PMID]: 28685490
[Au] Autor:Creanza A; Cotugno M; Mazzaccara C; Frisso G; Parenti G; Capaldo B
[Ad] Address:Department of Clinical Medicine and Surgery, University of Naples Federico II, Naples, Italy.
[Ti] Title:Successful Pregnancy in a Young Woman with Multiple Acyl-CoA Dehydrogenase Deficiency.
[So] Source:JIMD Rep;, 2017 Jul 07.
[Is] ISSN:2192-8304
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Multiple acyl-CoA dehydrogenation deficiency (MADD) is an inborn disorder of fatty acid oxidation due to a defect in electron transfer to the respiratory chain. We describe the medical/nutritional management of a successful pregnancy in a 19-year-old woman with a known diagnosis of MADD. A high-carbohydrate, low-fat, six-meal diet supplemented with protein was prescribed to meet the nutritional needs during pregnancy. L-Carnitine supplementation was also progressively increased over the weeks. Serum acyl-carnitine profile revealed raised levels of chain-length C6-C14, which remained substantially unchanged during pregnancy. Serum amino acid profile was in the normal range indicating an adequate nutritional support. Pregnancy progressed uneventful and the patient gave birth to a healthy boy without any complication.A careful clinical monitoring associated with an adequate medical/nutritional management may improve pregnancy outcome in women with MADD.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1707
[Cu] Class update date: 170707
[Lr] Last revision date:170707
[St] Status:Publisher
[do] DOI:10.1007/8904_2017_38

  3 / 217 MEDLINE  
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[PMID]: 27935074
[Au] Autor:Liang WC; Lin YF; Liu TY; Chang SC; Chen BH; Nishino I; Jong YJ
[Ad] Address:Department of Pediatrics, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung, Taiwan.
[Ti] Title:Neurite growth could be impaired by ETFDH mutation but restored by mitochondrial cofactors.
[So] Source:Muscle Nerve;56(3):479-485, 2017 Sep.
[Is] ISSN:1097-4598
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:INTRODUCTION: c.250G>A (p.Ala84Thr) in ETFDH is the most common mutation that causes later-onset multiple acyl-coenzyme A dehydrogenase deficiency (MADD) in the southern Chinese population. No functional study has targeted this mutation. METHODS: Using cells expressing ETFDH-wild-type (WT) or ETFDH-mutant (p.Ala84Thr), reactive oxygen species (ROS) production and neurite length were analyzed, followed by pathomechanism exploration and drug screening. RESULTS: Increased ROS production and marked neurite shortening were observed in the cells expressing the ETFDH-mutant, compared with WT. Further studies demonstrated that suberic acid, an accumulated intermediate metabolite in MADD, could significantly impair neurite outgrowth of NSC34 cells, but neurite shortening could be restored by supplementation with carnitine, riboflavin, or Coenzyme Q10. CONCLUSIONS: Neurite shortening caused by the c.250G>A mutation in ETFDH suggests that neural defects could be underdiagnosed in human patients with MADD. This impairment might be treatable with mitochondrial cofactor supplementation. Muscle Nerve 56: 479-485, 2017.
[Mh] MeSH terms primary: Electron-Transferring Flavoproteins/biosynthesis
Electron-Transferring Flavoproteins/genetics
Iron-Sulfur Proteins/biosynthesis
Iron-Sulfur Proteins/genetics
Mitochondria/genetics
Mitochondria/metabolism
Mutation/physiology
Neuronal Outgrowth/physiology
Oxidoreductases Acting on CH-NH Group Donors/biosynthesis
Oxidoreductases Acting on CH-NH Group Donors/genetics
[Mh] MeSH terms secundary: Cell Line
Humans
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/genetics
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/metabolism
Neurites/metabolism
Neuronal Outgrowth/drug effects
Reactive Oxygen Species/metabolism
Ubiquinone/analogs & derivatives
Ubiquinone/pharmacology
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Electron-Transferring Flavoproteins); 0 (Iron-Sulfur Proteins); 0 (Reactive Oxygen Species); 1339-63-5 (Ubiquinone); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.5.1 (electron-transferring-flavoprotein dehydrogenase); EJ27X76M46 (coenzyme Q10)
[Em] Entry month:1709
[Cu] Class update date: 170911
[Lr] Last revision date:170911
[Js] Journal subset:IM
[Da] Date of entry for processing:161210
[St] Status:MEDLINE
[do] DOI:10.1002/mus.25501

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[PMID]: 27591119
[Au] Autor:Yamada K; Kobayashi H; Bo R; Purevsuren J; Mushimoto Y; Takahashi T; Hasegawa Y; Taketani T; Fukuda S; Yamaguchi S
[Ad] Address:Department of Pediatrics, Shimane University, Faculty of Medicine, Izumo, Shimane, Japan. Electronic address: k-yamada@med.shimane-u.ac.jp.
[Ti] Title:Efficacy of bezafibrate on fibroblasts of glutaric acidemia type II patients evaluated using an in vitro probe acylcarnitine assay.
[So] Source:Brain Dev;39(1):48-57, 2017 Jan.
[Is] ISSN:1872-7131
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:INTRODUCTION: We evaluated the effects of bezafibrate (BEZ) on ß-oxidation in fibroblasts obtained from patients with glutaric acidemia type II (GA2) of various clinical severities using an in vitro probe (IVP) assay. METHODS: Cultured fibroblasts from 12 patients with GA2, including cases of the neonatal-onset type both with and without congenital anomalies (the prenatal- and neonatal-onset forms, respectively), the infantile-onset, and the myopathic forms, were studied. The IVP assay was performed by measuring acylcarnitines (ACs) in the cell culture medium of fibroblasts incubated with palmitic acid for 96h in the presence of 0-800µM BEZ using tandem mass spectrometry. RESULTS: The IVP assay showed that 100µM BEZ markedly reduced the level of palmitoylcarnitine (C16) in the neonatal-onset, infantile-onset, and myopathic forms of GA2, either increasing or maintaining a high level of acetylcarnitine (C2), which serves as an index of energy production via ß-oxidation. In the prenatal-onset form, although a small reduction of C16 was also observed in the presence of 100µM BEZ, the level of C2 remained low. At concentrations higher than 100µM, BEZ further decreased the level of ACs including C16, but a concentration over 400µM decreased the level of C2 in most cases. DISCUSSION: BEZ at 100µM was effective for all GA2 phenotypes except for the prenatal-onset form, as a reduction of C16 without deterioration of C2 is considered to indicate improvement of ß-oxidation. The effects of higher doses BEZ could not be estimated by the IVP assay but might be small or nonexistent.
[Mh] MeSH terms primary: Bezafibrate/pharmacology
Carnitine/analogs & derivatives
Fibroblasts/drug effects
Lipid Regulating Agents/pharmacology
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/drug therapy
[Mh] MeSH terms secundary: Adolescent
Adult
Age of Onset
Carnitine/metabolism
Cell Survival/drug effects
Cells, Cultured
Dose-Response Relationship, Drug
Drug Evaluation, Preclinical
Enzyme Activators/pharmacology
Female
Fibroblasts/metabolism
Humans
Infant
Infant, Newborn
Male
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/metabolism
Palmitoylcarnitine/metabolism
Peroxisome Proliferator-Activated Receptors/agonists
Skin/cytology
Skin/drug effects
Skin/metabolism
[Pt] Publication type:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Name of substance:0 (Enzyme Activators); 0 (Lipid Regulating Agents); 0 (Peroxisome Proliferator-Activated Receptors); 0 (acylcarnitine); 1935-18-8 (Palmitoylcarnitine); S7UI8SM58A (Carnitine); Y9449Q51XH (Bezafibrate)
[Em] Entry month:1702
[Cu] Class update date: 170214
[Lr] Last revision date:170214
[Js] Journal subset:IM
[Da] Date of entry for processing:160904
[St] Status:MEDLINE

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[PMID]: 27941971
[Au] Autor:Scarpellini B; Zanoni M; Sucupira MC; Truong HM; Janini LM; Segurado ID; Diaz RS
[Ad] Address:Federal University of Sao Paulo, Department of Medicine, Sao Paulo-SP, Brazil.
[Ti] Title:Plasma Metabolomics Biosignature According to HIV Stage of Infection, Pace of Disease Progression, Viremia Level and Immunological Response to Treatment.
[So] Source:PLoS One;11(12):e0161920, 2016.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: We evaluated plasma samples HIV-infected individuals with different phenotypic profile among five HIV-infected elite controllers and five rapid progressors after recent HIV infection and one year later and from 10 individuals subjected to antiretroviral therapy, five of whom were immunological non-responders (INR), before and after one year of antiretroviral treatment compared to 175 samples from HIV-negative patients. A targeted quantitative tandem mass spectrometry metabolomics approach was used in order to determine plasma metabolomics biosignature that may relate to HIV infection, pace of HIV disease progression, and immunological response to treatment. RESULTS: Twenty-five unique metabolites were identified, including five metabolites that could distinguish rapid progressors and INRs at baseline. Severe deregulation in acylcarnitine and sphingomyelin metabolism compatible with mitochondrial deficiencies was observed. ß-oxidation and sphingosine-1-phosphate-phosphatase-1 activity were down-regulated, whereas acyl-alkyl-containing phosphatidylcholines and alkylglyceronephosphate synthase levels were elevated in INRs. Evidence that elite controllers harbor an inborn error of metabolism (late-onset multiple acyl-coenzyme A dehydrogenase deficiency [MADD]) was detected. CONCLUSIONS: Blood-based markers from metabolomics show a very high accuracy of discriminating HIV infection between varieties of controls and have the ability to predict rapid disease progression or poor antiretroviral immunological response. These metabolites can be used as biomarkers of HIV natural evolution or treatment response and provide insight into the mechanisms of the disease.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1706
[Cu] Class update date: 170727
[Lr] Last revision date:170727
[Da] Date of entry for processing:161213
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.1371/journal.pone.0161920

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[PMID]: 27927213
[Au] Autor:van Eunen K; Volker-Touw CM; Gerding A; Bleeker A; Wolters JC; van Rijt WJ; Martines AM; Niezen-Koning KE; Heiner RM; Permentier H; Groen AK; Reijngoud DJ; Derks TG; Bakker BM
[Ad] Address:Department of Pediatrics, University of Groningen, University Medical Center Groningen, Hanzeplein 1, 9713 GZ, Groningen, The Netherlands.
[Ti] Title:Living on the edge: substrate competition explains loss of robustness in mitochondrial fatty-acid oxidation disorders.
[So] Source:BMC Biol;14(1):107, 2016 Dec 07.
[Is] ISSN:1741-7007
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Defects in genes involved in mitochondrial fatty-acid oxidation (mFAO) reduce the ability of patients to cope with metabolic challenges. mFAO enzymes accept multiple substrates of different chain length, leading to molecular competition among the substrates. Here, we combined computational modeling with quantitative mouse and patient data to investigate whether substrate competition affects pathway robustness in mFAO disorders. RESULTS: First, we used comprehensive biochemical analyses of wild-type mice and mice deficient for medium-chain acyl-CoA dehydrogenase (MCAD) to parameterize a detailed computational model of mFAO. Model simulations predicted that MCAD deficiency would have no effect on the pathway flux at low concentrations of the mFAO substrate palmitoyl-CoA. However, high concentrations of palmitoyl-CoA would induce a decline in flux and an accumulation of intermediate metabolites. We proved computationally that the predicted overload behavior was due to substrate competition in the pathway. Second, to study the clinical relevance of this mechanism, we used patients' metabolite profiles and generated a humanized version of the computational model. While molecular competition did not affect the plasma metabolite profiles during MCAD deficiency, it was a key factor in explaining the characteristic acylcarnitine profiles of multiple acyl-CoA dehydrogenase deficient patients. The patient-specific computational models allowed us to predict the severity of the disease phenotype, providing a proof of principle for the systems medicine approach. CONCLUSION: We conclude that substrate competition is at the basis of the physiology seen in patients with mFAO disorders, a finding that may explain why these patients run a risk of a life-threatening metabolic catastrophe.
[Mh] MeSH terms primary: Acyl-CoA Dehydrogenase/deficiency
Lipid Metabolism, Inborn Errors/genetics
Lipid Metabolism/genetics
Mitochondria/metabolism
[Mh] MeSH terms secundary: Acyl-CoA Dehydrogenase/genetics
Acyl-CoA Dehydrogenase/metabolism
Animals
Carnitine/analogs & derivatives
Carnitine/metabolism
Computational Biology
Computer Simulation
Disease Models, Animal
Fatty Acids/metabolism
Humans
Lipid Metabolism, Inborn Errors/metabolism
Male
Metabolic Networks and Pathways
Mice
Mice, Inbred C57BL
Mice, Knockout
Oxidation-Reduction
Proteomics
Substrate Specificity
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Fatty Acids); 0 (acylcarnitine); EC 1.3.8.7 (Acyl-CoA Dehydrogenase); S7UI8SM58A (Carnitine)
[Em] Entry month:1710
[Cu] Class update date: 171026
[Lr] Last revision date:171026
[Js] Journal subset:IM
[Da] Date of entry for processing:161209
[St] Status:MEDLINE

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[PMID]: 27751224
[Au] Autor:Tan JQ; Chen DY; Li ZT; Huang JW; Yan TZ; Cai R
[Ad] Address:Department of Medical Genetics, Liuzhou Maternal and Child Health Hospital, Liuzhou, Guangxi 545001, China. lzcairen@126.com.
[Ti] Title:[An analysis of clinical characteristics and gene mutation in two patients with medium- and short-chain acyl-CoA dehydrogenase deficiency].
[So] Source:Zhongguo Dang Dai Er Ke Za Zhi;18(10):1019-1025, 2016 Oct.
[Is] ISSN:1008-8830
[Cp] Country of publication:China
[La] Language:chi
[Ab] Abstract:Medium- and short-chain acyl-CoA dehydrogenase deficiency is a disorder of fatty acid ß-oxidation. Gene mutation prevents medium- and short-chain fatty acids from entry into mitochondria for oxidation, which leads to multiple organ dysfunction. In this study, serum acylcarnitines and the organic acid profile in urea were analyzed in two children whose clinical symptoms were hypoglycemia and metabolic acidosis. Moreover, gene mutations in the two children and their parents were evaluated. One of the patients was a 3-day-old male who was admitted to the hospital due to neonatal asphyxia, sucking weakness, and sleepiness. The serum acylcarnitine profile showed increases in medium-chain acylcarnitines (C6-C10), particularly in C8, which showed a concentration of 3.52 µmol/L (reference value: 0.02-0.2 µmol/L). The analysis of organic acids in urea gave a normal result. Sanger sequencing revealed a reported c.580A>G (p.Asn194Asp) homozygous mutation at exon 7 of the ACADM gene. The other patient was a 3-month-old female who was admitted to the hospital due to cough and recurrent fever for around 10 days. The serum acylcarnitine profile showed an increase in serum C4 level, which was 1.66 µmol/L (reference value: 0.06-0.6 µmol/L). The analysis of organic acids in urea showed an increase in the level of ethyl malonic acid, which was 55.9 (reference value: 0-6.2). Sanger sequencing revealed a reported c.625G>A (p.Gly209Ser) homozygous mutation in the ACADS gene. This study indicates that screening tests for genetic metabolic diseases are recommended for children who have unexplained metabolic acidosis and hypoglycemia. Genetic analyses of the ACADM and ACADS genes are helpful for the diagnosis of medium- and short-chain acyl-CoA dehydrogenase deficiency.
[Mh] MeSH terms primary: Acyl-CoA Dehydrogenase/deficiency
Lipid Metabolism, Inborn Errors/genetics
Mutation
[Mh] MeSH terms secundary: Acyl-CoA Dehydrogenase/genetics
Carnitine/analogs & derivatives
Carnitine/blood
Female
Humans
Infant
Infant, Newborn
Male
Urea/analysis
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (acylcarnitine); 8W8T17847W (Urea); EC 1.3.8.7 (Acyl-CoA Dehydrogenase); S7UI8SM58A (Carnitine)
[Em] Entry month:1703
[Cu] Class update date: 170308
[Lr] Last revision date:170308
[Js] Journal subset:IM
[Da] Date of entry for processing:161019
[St] Status:MEDLINE

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[PMID]: 27644403
[Au] Autor:Yang Y; Feng Y; Zhang X; Nakajima T; Tanaka N; Sugiyama E; Kamijo Y; Aoyama T
[Ad] Address:Department of Metabolic Regulation, Shinshu University Graduate School of Medicine.
[Ti] Title:Activation of PPARα by Fatty Acid Accumulation Enhances Fatty Acid Degradation and Sulfatide Synthesis.
[So] Source:Tohoku J Exp Med;240(2):113-22, 2016 10.
[Is] ISSN:1349-3329
[Cp] Country of publication:Japan
[La] Language:eng
[Ab] Abstract:Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the first reaction in the mitochondrial fatty acid ß-oxidation pathway. VLCAD deficiency is associated with the accumulation of fat in multiple organs and tissues, which results in specific clinical features including cardiomyopathy, cardiomegaly, muscle weakness, and hepatic dysfunction in infants. We speculated that the abnormal fatty acid metabolism in VLCAD-deficient individuals might cause cell necrosis by fatty acid toxicity. The accumulation of fatty acids may activate peroxisome proliferator-activated receptor (PPAR), a master regulator of fatty acid metabolism and a potent nuclear receptor for free fatty acids. We examined six skin fibroblast lines, derived from VLCAD-deficient patients and identified fatty acid accumulation and PPARα activation in these cell lines. We then found that the expression levels of three enzymes involved in fatty acid degradation, including long-chain acyl-CoA synthetase (LACS), were increased in a PPARα-dependent manner. This increased expression of LACS might enhance the fatty acyl-CoA supply to fatty acid degradation and sulfatide synthesis pathways. In fact, the first and last reactions in the sulfatide synthesis pathway are regulated by PPARα. Therefore, we also measured the expression levels of enzymes involved in sulfatide metabolism and the regulation of cellular sulfatide content. The levels of these enzymes and cellular sulfatide content both increased in a PPARα-dependent manner. These results indicate that PPARα activation plays defensive and compensative roles by reducing cellular toxicity associated with fatty acids and sulfuric acid.
[Mh] MeSH terms primary: Fatty Acids/metabolism
PPAR alpha/metabolism
Sulfoglycosphingolipids/metabolism
[Mh] MeSH terms secundary: Acyl-CoA Dehydrogenase, Long-Chain/genetics
Acyl-CoA Dehydrogenase, Long-Chain/metabolism
DNA/metabolism
Fenofibrate/pharmacology
Gene Expression Regulation/drug effects
Humans
Indoles/pharmacology
Metabolic Networks and Pathways/drug effects
Metabolic Networks and Pathways/genetics
Protein Binding/drug effects
RNA, Messenger/genetics
RNA, Messenger/metabolism
Real-Time Polymerase Chain Reaction
Sulfoglycosphingolipids/chemistry
Triglycerides/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Fatty Acids); 0 (Indoles); 0 (PPAR alpha); 0 (RNA, Messenger); 0 (Sulfoglycosphingolipids); 0 (Triglycerides); 080626SQ8C (MK-886); 9007-49-2 (DNA); EC 1.3.8.8 (Acyl-CoA Dehydrogenase, Long-Chain); U202363UOS (Fenofibrate)
[Em] Entry month:1703
[Cu] Class update date: 170908
[Lr] Last revision date:170908
[Js] Journal subset:IM
[Da] Date of entry for processing:160921
[St] Status:MEDLINE
[do] DOI:10.1620/tjem.240.113

  9 / 217 MEDLINE  
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[PMID]: 27433981
[Au] Autor:Sander J; Terhardt M; Sander S; Janzen N
[Ad] Address:Screening-Labor Hannover, Postbox 91 10 09, 30430 Hannover, Germany. Electronic address: j.sander@metabscreen.de.
[Ti] Title:Quantification of hypoglycin A as butyl ester.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1029-1030:169-173, 2016 Sep 01.
[Is] ISSN:1873-376X
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:L-α-amino-methylenecyclopropyl propionic acid (Hypoglycin A, HGA) has been found to be the toxic compound in fruits of the Sapindaceae family causing acute intoxication when ingested as food or feed. Clinical symptoms are consistent with acquired multiple acyl-CoA dehydrogenase deficiency (MADD). Ultra performance liquid chromatography-tandem mass spectrometry was used to measure HGA after butylation. Sample volumes were 10µL for serum and 20µL for urine. Internal standard for HGA was d3-leucine, samples were plotted on a 7-point linear calibration curve. Coefficients of variation were <15% at 0.01µmol HGA/L and ≤4.1% at 10µmol/L. R(2) values for linearity were ≥0.995. In order to quantify non-metabolized HGA together with some of its metabolites plus a spectrum of acyl glycines and acyl carnitines typical for acquired MADD in one single analysis HGA measurement was integrated into a method which we previously developed for metabolites of HGA and acyl conjugates. The new method is suitable for biochemical diagnosis of Ackee fruit poisoning or atypical myopathy in horses and for forensic purposes in cases of suspected HGA poisoning.
[Mh] MeSH terms primary: Chromatography, High Pressure Liquid/methods
Hypoglycins/analysis
Tandem Mass Spectrometry/methods
[Mh] MeSH terms secundary: Animal Feed/adverse effects
Animal Feed/analysis
Animals
Esterification
Horse Diseases/diagnosis
Horse Diseases/etiology
Horses
Hypoglycins/toxicity
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/diagnosis
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/etiology
Multiple Acyl Coenzyme A Dehydrogenase Deficiency/veterinary
Muscular Diseases/diagnosis
Muscular Diseases/etiology
Muscular Diseases/veterinary
Plant Poisoning/etiology
Plant Poisoning/veterinary
Sapindaceae/chemistry
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Hypoglycins); 156-56-9 (hypoglycin)
[Em] Entry month:1702
[Cu] Class update date: 170823
[Lr] Last revision date:170823
[Js] Journal subset:IM
[Da] Date of entry for processing:160720
[St] Status:MEDLINE

  10 / 217 MEDLINE  
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[PMID]: 27428459
[Au] Autor:Aguennouz M; Beccaria M; Purcaro G; Oteri M; Micalizzi G; Musumesci O; Ciranni A; Di Giorgio RM; Toscano A; Dugo P; Mondello L
[Ad] Address:"Dipartimento di Medicina Clinica e Sperimentale", University of Messina, Padiglione B, I piano - AOU Policlinico G. Martino - Viale Gazzi, Messina, Italy.
[Ti] Title:Analysis of lipid profile in lipid storage myopathy.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1029-1030:157-168, 2016 Sep 01.
[Is] ISSN:1873-376X
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Lipid dysmetabolism disease is a condition in which lipids are stored abnormally in organs and tissues throughout the body, causing muscle weakness (myopathy). Usually, the diagnosis of this disease and its characterization goes through dosage of Acyl CoA in plasma accompanied with evidence of droplets of intra-fibrils lipids in the patient muscle biopsy. However, to understand the pathophysiological mechanisms of lipid storage diseases, it is useful to identify the nature of lipids deposited in muscle fiber. In this work fatty acids and triglycerides profile of lipid accumulated in the muscle of people suffering from myopathies syndromes was characterized. In particular, the analyses were carried out on the muscle biopsy of people afflicted by lipid storage myopathy, such as multiple acyl-coenzyme A dehydrogenase deficiency, and neutral lipid storage disease with myopathy, and by the intramitochondrial lipid storage dysfunctions, such as deficiencies of carnitine palmitoyltransferase II enzyme. A single step extraction and derivatization procedure was applied to analyze fatty acids from muscle tissues by gas chromatography with a flame ionization detector and with an electronic impact mass spectrometer. Triglycerides, extracted by using n-hexane, were analyzed by high performance liquid chromatography coupled to mass spectrometer equipped with an atmospheric pressure chemical ionization interface. The most representative fatty acids in all samples were: C16:0 in the 13-24% range, C18:1n9 in the 20-52% range, and C18:2n6 in the 10-25% range. These fatty acids were part of the most representative triglycerides in all samples. The data obtained was statistically elaborated performing a principal component analysis. A satisfactory discrimination was obtained among the different diseases. Using component 1 vs component 3 a 43.3% of total variance was explained. Such results suggest the important role that lipid profile characterization can have in supporting a correct diagnosis.
[Mh] MeSH terms primary: Fatty Acids/analysis
Lipid Metabolism, Inborn Errors/pathology
Muscle, Skeletal/pathology
Muscular Dystrophies/pathology
Triglycerides/analysis
[Mh] MeSH terms secundary: Adolescent
Adult
Child
Chromatography, High Pressure Liquid/methods
Chromatography, Reverse-Phase/methods
Fatty Acids/metabolism
Female
Gas Chromatography-Mass Spectrometry/methods
Humans
Lipid Metabolism, Inborn Errors/metabolism
Male
Mass Spectrometry/methods
Middle Aged
Muscle, Skeletal/metabolism
Muscular Dystrophies/metabolism
Triglycerides/metabolism
Young Adult
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Fatty Acids); 0 (Triglycerides)
[Em] Entry month:1702
[Cu] Class update date: 170823
[Lr] Last revision date:170823
[Js] Journal subset:IM
[Da] Date of entry for processing:160719
[St] Status:MEDLINE


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