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  1 / 10 MEDLINE  
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[PMID]:27940755
[Au] Autor:Tort F; Ugarteburu O; Torres MA; García-Villoria J; Girós M; Ruiz A; Ribes A
[Ad] Endereço:Secció d'Errors Congènits del Metabolisme-IBC, Servei de Bioquímica i Genètica Molecular, Hospital Clínic, IDIBAPS, CIBERER, Barcelona, Spain; and.
[Ti] Título:Lysine Restriction and Pyridoxal Phosphate Administration in a NADK2 Patient.
[So] Source:Pediatrics;138(5), 2016 Nov.
[Is] ISSN:1098-4275
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We report the case of a 10-year-old Spanish girl with mutations in NADK2 Prenatal central nervous system abnormalities showed ventriculomegaly, colpocephaly, and hypoplasia of the corpus callosum. At birth, axial hypotonia, uncoordinated movements, microcephaly, and generalized cerebellar atrophy were detected. Metabolic investigations revealed high lysine, lactate, and pipecolic acid levels in blood and cerebrospinal fluid. Pyruvate carboxylase and pyruvate dehydrogenase activity in fibroblasts were normal. Beginning at birth she received biotin, thiamine, and carnitine supplementation. A lysine-restricted diet was started when she was 1 month old. Because pipecolic acid was high, pyridoxine was added to treatment. At 3 years old, astatic myoclonic epilepsy appeared, with no response to levetiracetam. We switched pyridoxine to pyridoxal phosphate, with electroclinical improvement. Because the activity of mitochondrial respiratory chain complexes III and IV was slightly low in muscle, other cofactors such as ubidecarenone, idebenone, vitamin E, and creatine were added to the treatment. At 8 years old, plasma acylcarnitine testing was performed, and high levels of 2-trans, 4-cis-decadienoylcarnitine were found. Whole exome sequencing identified a homozygous splice site mutation in NADK2 (c.956+6T>C; p.Trp319Cysfs*21). This substitution generates exon skipping, leading to a truncated protein. In fact, NADK2 messenger RNA and the corresponding protein were almost absent. Now, at 10 years of age she presents with ataxia and incoordination. She has oromotor dysphasia but is able to understand fluid language and is a very friendly girl. We hypothesize that the patient's clinical improvement could be due to her lysine-restricted diet together with cofactors and pyridoxal phosphate administration.
[Mh] Termos MeSH primário: Dieta
Hiperlisinemias/genética
Lisina/administração & dosagem
Proteínas Mitocondriais/genética
Mutação
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfato de Piridoxal/uso terapêutico
Complexo Vitamínico B/uso terapêutico
[Mh] Termos MeSH secundário: Criança
Epilepsias Mioclônicas/genética
Epilepsias Mioclônicas/terapia
Feminino
Homozigoto
Seres Humanos
Ácido Láctico/sangue
Ácido Láctico/líquido cefalorraquidiano
Lisina/sangue
Lisina/líquido cefalorraquidiano
Doenças Mitocondriais/genética
Malformações do Sistema Nervoso/genética
Ácidos Pipecólicos/sangue
Ácidos Pipecólicos/líquido cefalorraquidiano
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Pipecolic Acids); 0 (RNA, Messenger); 12001-76-2 (Vitamin B Complex); 33X04XA5AT (Lactic Acid); 5V5IOJ8338 (Pyridoxal Phosphate); EC 2.7.1.- (NADK2 protein, human); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); H254GW7PVV (pipecolic acid); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170622
[Lr] Data última revisão:
170622
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


  2 / 10 MEDLINE  
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[PMID]:26980171
[Au] Autor:Leganés-Ramos A; Álvaro-Alonso EA; Martín de Rosales-Cabrera AM; Pérez-Encinas M
[Ad] Endereço:Servicio de Farmacia. Hospital Universitario Fundación Alcorcón (Madrid). alexlegaram@hotmail.com.
[Ti] Título:Oral formulation of pyridoxine for the treatment of pyridoxinedependent epilepsy in a paediatric patient.
[So] Source:Farm Hosp;40(2):131-3, 2016 Mar 01.
[Is] ISSN:0214-753X
[Cp] País de publicação:Spain
[La] Idioma:eng
[Mh] Termos MeSH primário: Epilepsia/tratamento farmacológico
Hiperlisinemias/tratamento farmacológico
Piridoxina/uso terapêutico
Complexo Vitamínico B/uso terapêutico
[Mh] Termos MeSH secundário: Composição de Medicamentos
Epilepsia/genética
Feminino
Seres Humanos
Hiperlisinemias/genética
Recém-Nascido
Ácidos Pipecólicos/sangue
Ácidos Pipecólicos/urina
Piridoxina/administração & dosagem
Piridoxina/química
Complexo Vitamínico B/administração & dosagem
Complexo Vitamínico B/química
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pipecolic Acids); 12001-76-2 (Vitamin B Complex); H254GW7PVV (pipecolic acid); KV2JZ1BI6Z (Pyridoxine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170214
[Lr] Data última revisão:
170214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160317
[St] Status:MEDLINE
[do] DOI:10.7399/fh.2016.40.2.9233


  3 / 10 MEDLINE  
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[PMID]:24847004
[Au] Autor:Houten SM; Denis S; Te Brinke H; Jongejan A; van Kampen AH; Bradley EJ; Baas F; Hennekam RC; Millington DS; Young SP; Frazier DM; Gucsavas-Calikoglu M; Wanders RJ
[Ad] Endereço:Department of Clinical Chemistry, Laboratory Genetic Metabolic Diseases, Department of Pediatrics, Emma Children's Hospital, Department of Genetics and Genomic Sciences and Icahn Institute for Genomics and Multiscale Biology, Icahn School of Medicine at Mount Sinai, 1425 Madison Avenue, Box 1498, Ne
[Ti] Título:Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes dienoyl-CoA reductase deficiency with hyperlysinemia.
[So] Source:Hum Mol Genet;23(18):5009-16, 2014 Sep 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dienoyl-CoA reductase (DECR) deficiency with hyperlysinemia is a rare disorder affecting the metabolism of polyunsaturated fatty acids and lysine. The molecular basis of this condition is currently unknown. We describe a new case with failure to thrive, developmental delay, lactic acidosis and severe encephalopathy suggestive of a mitochondrial disorder. Exome sequencing revealed a causal mutation in NADK2. NADK2 encodes the mitochondrial NAD kinase, which is crucial for NADP biosynthesis evidenced by decreased mitochondrial NADP(H) levels in patient fibroblasts. DECR and also the first step in lysine degradation are performed by NADP-dependent oxidoreductases explaining their in vivo deficiency. DECR activity was also deficient in lysates of patient fibroblasts and could only be rescued by transfecting patient cells with functional NADK2. Thus NADPH is not only crucial as a cosubstrate, but can also act as a molecular chaperone that activates and stabilizes enzymes. In addition to polyunsaturated fatty acid oxidation and lysine degradation, NADPH also plays a role in various other mitochondrial processes. We found decreased oxygen consumption and increased extracellular acidification in patient fibroblasts, which may explain why the disease course is consistent with clinical criteria for a mitochondrial disorder. We conclude that DECR deficiency with hyperlysinemia is caused by mitochondrial NADP(H) deficiency due to a mutation in NADK2.
[Mh] Termos MeSH primário: Hiperlisinemias/genética
Proteínas Mitocondriais/genética
NADP/deficiência
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/deficiência
Fosfotransferases (Aceptor do Grupo Álcool)/genética
[Mh] Termos MeSH secundário: Fibroblastos/metabolismo
Seres Humanos
Hiperlisinemias/fisiopatologia
Mutação
Análise de Sequência de DNA
Estresse Fisiológico
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 53-59-8 (NADP); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.1.34 (2,4-dienoyl-CoA reductase); EC 2.7.1.- (NADK2 protein, human); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
[Em] Mês de entrada:1504
[Cu] Atualização por classe:140822
[Lr] Data última revisão:
140822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140522
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddu218


  4 / 10 MEDLINE  
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[PMID]:23890588
[Au] Autor:Tondo M; Calpena E; Arriola G; Sanz P; Martorell L; Ormazabal A; Castejon E; Palacin M; Ugarte M; Espinos C; Perez B; Perez-Dueñas B; Pérez-Cerda C; Artuch R
[Ad] Endereço:Inborn Errors of Metabolism Unit, Hospital Sant Joan de Déu, Barcelona, Spain. Electronic address: mtondo@hsjdbcn.org.
[Ti] Título:Clinical, biochemical, molecular and therapeutic aspects of 2 new cases of 2-aminoadipic semialdehyde synthase deficiency.
[So] Source:Mol Genet Metab;110(3):231-6, 2013 Nov.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Our aim was to report two new cases of hyperlysinemia type I describing the clinical, biochemical and molecular features of the disease and the outcome of lysine restriction. Two children presented with febrile seizures followed by developmental delay, clumsiness and epilepsy. At age 2 and 8 years a biochemical and genetic diagnosis of hyperlysinemia type I was confirmed and lysine-restricted diet was started in both cases. Three years after initiation of lysine restriction, case 1 had not suffered further seizures. In case 2, tremor and dysmetria improved, but fine motor clumsiness persisted. Mild cognitive impairment was present in both patients despite dietary treatment. Laboratory studies: Plasma, urine and cerebrospinal fluid amino acid concentrations were measured by ion exchange chromatography. Mutation analysis of the AASS gene was performed by directly sequencing the PCR products. The plasma lysine values were higher than 1200 µmol/L in both cases. Additionally, an increase in dibasic aminoaciduria was observed. Lysine restriction decreased plasma lysine values and nearly normalised dibasic aminoaciduria. Mutational screening of the AASS gene revealed that case 1 was a compound heterozygote for c.2662 + 1_2662 + 5delGTAAGinsTT and c.874A>G and that case 2 was a compound heterozygote for c.976_977delCA and c.1925C>G. In conclusion, we present two children with hyperlysinemia type I and neurological impairment in which implementation of lysine-restricted diet achieved a mild improvement of symptoms but did not reverse cognitive impairment. The partial decrease of lysine concentrations and the normalisation of urine excretion of dibasic amino acids after lysine restriction further reinforce the possibility of this therapeutic intervention, although further investigations seem necessary.
[Mh] Termos MeSH primário: Hiperlisinemias/dietoterapia
Hiperlisinemias/diagnóstico
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Aminoácidos/sangue
Aminoácidos/urina
Criança
Pré-Escolar
Éxons
Feminino
Ordem dos Genes
Genótipo
Seres Humanos
Hiperlisinemias/genética
Hiperlisinemias/metabolismo
Mutação
Sacaropina Desidrogenases/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); EC 1.5.1.- (AASS protein, human); EC 1.5.1.- (Saccharopine Dehydrogenases)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:131016
[Lr] Data última revisão:
131016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130730
[St] Status:MEDLINE


  5 / 10 MEDLINE  
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[PMID]:23570448
[Au] Autor:Houten SM; Te Brinke H; Denis S; Ruiter JP; Knegt AC; de Klerk JB; Augoustides-Savvopoulou P; Häberle J; Baumgartner MR; Coskun T; Zschocke J; Sass JO; Poll-The BT; Wanders RJ; Duran M
[Ad] Endereço:Department of Clinical Chemistry, Laboratory Genetic Metabolic Diseases, Academic Medical Center, University of Amsterdam, Meibergdreef 9, Amsterdam, AZ 1105, The Netherlands. s.m.houten@amc.uva.nl
[Ti] Título:Genetic basis of hyperlysinemia.
[So] Source:Orphanet J Rare Dis;8:57, 2013 Apr 09.
[Is] ISSN:1750-1172
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hyperlysinemia is an autosomal recessive inborn error of L-lysine degradation. To date only one causal mutation in the AASS gene encoding α-aminoadipic semialdehyde synthase has been reported. We aimed to better define the genetic basis of hyperlysinemia. METHODS: We collected the clinical, biochemical and molecular data in a cohort of 8 hyperlysinemia patients with distinct neurological features. RESULTS: We found novel causal mutations in AASS in all affected individuals, including 4 missense mutations, 2 deletions and 1 duplication. In two patients originating from one family, the hyperlysinemia was caused by a contiguous gene deletion syndrome affecting AASS and PTPRZ1. CONCLUSIONS: Hyperlysinemia is caused by mutations in AASS. As hyperlysinemia is generally considered a benign metabolic variant, the more severe neurological disease course in two patients with a contiguous deletion syndrome may be explained by the additional loss of PTPRZ1. Our findings illustrate the importance of detailed biochemical and genetic studies in any hyperlysinemia patient.
[Mh] Termos MeSH primário: Hiperlisinemias/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Western Blotting
Linhagem Celular
Estudos de Coortes
Hibridização Genômica Comparativa
Primers do DNA
DNA Complementar/genética
Seres Humanos
Hiperlisinemias/sangue
Hiperlisinemias/fisiopatologia
Mutação
Sacaropina Desidrogenases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (DNA, Complementary); EC 1.5.1.- (AASS protein, human); EC 1.5.1.- (Saccharopine Dehydrogenases)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:150427
[Lr] Data última revisão:
150427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130411
[St] Status:MEDLINE
[do] DOI:10.1186/1750-1172-8-57


  6 / 10 MEDLINE  
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[PMID]:23350806
[Au] Autor:Pérez B; Gutiérrez-Solana LG; Verdú A; Merinero B; Yuste-Checa P; Ruiz-Sala P; Calvo R; Jalan A; Marín LL; Campos O; Ruiz MÁ; San Miguel M; Vázquez M; Castro M; Ferrer I; Navarrete R; Desviat LR; Lapunzina P; Ugarte M; Pérez-Cerdá C
[Ad] Endereço:Center of Diagnosis of Molecular Diseases, Center of Molecular Biology UAM-CSIC, Center for Biomedical Network Research on Rare Diseases, Institute for Health Research, IDIPAZ, Autonomous University of Madrid, Madrid, Spain. bperez@cbm.uam.es
[Ti] Título:Clinical, biochemical, and molecular studies in pyridoxine-dependent epilepsy. Antisense therapy as possible new therapeutic option.
[So] Source:Epilepsia;54(2):239-48, 2013 Feb.
[Is] ISSN:1528-1167
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Pyridoxine-dependent epilepsy seizure (PDE; OMIM 266100) is a disorder associated with severe seizures that can be controlled pharmacologically with pyridoxine. In the majority of patients with PDE, the disorder is caused by the deficient activity of the enzyme α-aminoadipic semialdehyde dehydrogenase (antiquitin protein), which is encoded by the ALDH7A1 gene. The aim of this work was the clinical, biochemical, and genetic analysis of 12 unrelated patients, mostly from Spain, in an attempt to provide further valuable data regarding the wide clinical, biochemical, and genetic spectrum of the disease. METHODS: The disease was confirmed based on the presence of α-aminoadipic semialdehyde (α-AASA) in urine measured by liquid chromatography tandem mass spectrometry (LC-MS/MS) and pipecolic acid (PA) in plasma and/or cerebrospinal fluid (CSF) measured by high performance liquid chromatography (HPLC)/MS/MS and by sequencing analysis of messenger RNA (mRNA) and genomic DNA of ALDH7A1. KEY FINDINGS: Most of the patients had seizures in the neonatal period, but they responded to vitamin B6 administration. Three patients developed late-onset seizures, and most patients showed mild-to-moderate postnatal developmental delay. All patients had elevated PA and α-AASA levels, even those who had undergone pyridoxine treatment for several years. The clinical spectrum of our patients is not limited to seizures but many of them show associated neurologic dysfunctions such as muscle tone alterations, irritability, and psychomotor retardation. The mutational spectrum of the present patients included 12 mutations, five already reported (c.500A>G, c.919C>T, c.1429G>C c.1217_1218delAT, and c.1482-1G>T) and seven novel sequence changes (c.75C>T, c.319G>T, c.554_555delAA, c.757C>T, c.787 + 1G>T, c.1474T>C, c.1093-?_1620+?). Only one mutation, p.G477R (c.1429G>C), was recurrent; this was detected in four different alleles. Transcriptional profile analysis of one patient's lymphoblasts and ex vivo splicing analysis showed the silent nucleotide change c.75C>T to be a novel splicing mutation creating a new donor splice site inside exon 1. Antisense therapy of the aberrant mRNA splicing in a lymphoblast cell line harboring mutation c.75C>T was successful. SIGNIFICANCE: The present results broaden our knowledge of PDE, provide information regarding the genetic background of PDE in Spain, afford data of use when making molecular-based prenatal diagnosis, and provide a cellular proof-of concept for antisense therapy application.
[Mh] Termos MeSH primário: Epilepsia/tratamento farmacológico
Epilepsia/genética
Terapia Genética/métodos
Oligonucleotídeos Antissenso/uso terapêutico
Deficiência de Vitamina B 6/complicações
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/genética
Linhagem Celular
Análise Mutacional de DNA
Epilepsia/etiologia
Éxons/genética
Feminino
Seres Humanos
Hiperlisinemias/urina
Lactente
Recém-Nascido
Linfócitos/efeitos dos fármacos
Masculino
Mutação/genética
Polimorfismo de Nucleotídeo Único
Processamento de RNA
Sacaropina Desidrogenases/deficiência
Sacaropina Desidrogenases/urina
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oligonucleotides, Antisense); EC 1.2.1.3 (ALDH7A1 protein, human); EC 1.2.1.3 (Aldehyde Dehydrogenase); EC 1.5.1.- (Saccharopine Dehydrogenases)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:130206
[Lr] Data última revisão:
130206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130129
[St] Status:MEDLINE
[do] DOI:10.1111/epi.12083


  7 / 10 MEDLINE  
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Wajner, Moacir
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[PMID]:19370404
[Au] Autor:Tonin AM; Ferreira GC; Schuck PF; Viegas CM; Zanatta A; Leipnitz G; Seminotti B; Duvall Wannmacher CM; Wajner M
[Ad] Endereço:Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, UFRGS, Rua Ramiro Barcelos, RS, Brasil.
[Ti] Título:Inhibition of creatine kinase activity by lysine in rat cerebral cortex.
[So] Source:Metab Brain Dis;24(2):349-60, 2009 Jun.
[Is] ISSN:1573-7365
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulation of lysine (Lys) in tissues and biochemical fluids is the biochemical hallmark of patients affected by familial hyperlysinemia (FH) and also by other inherited neurometabolic disorders. In the present study, we investigated the in vitro effect of Lys on various parameters of energy metabolism in cerebral cortex of 30-day-old Wistar rats. We verified that total (tCK) and cytosolic creatine kinase activities were significantly inhibited by Lys, in contrast to the mitochondrial isoform which was not affected by this amino acid. Furthermore, the inhibitory effect of Lys on tCK activity was totally prevented by reduced glutathione, suggesting a possible role of reactive species oxidizing critical thiol groups of the enzyme. In contrast, Lys did not affect (14)CO(2) production from [U-(14)C] glucose (aerobic glycolytic pathway) and [1-(14)C] acetic acid (citric acid cycle activity) neither the various activities of the electron transfer chain and synaptic Na(+)K(+)-ATPase at concentrations as high as 5.0 mM. Considering the importance of creatine kinase (CK) activity for brain energy metabolism homeostasis and especially ATP transfer and buffering, our results suggest that inhibition of this enzyme by Lys may contribute to the neurological signs presented by symptomatic patients affected by FH and other neurodegenerative disorders in which Lys accumulates.
[Mh] Termos MeSH primário: Córtex Cerebral/enzimologia
Creatina Quinase/metabolismo
Metabolismo Energético/fisiologia
Hiperlisinemias/enzimologia
Lisina/metabolismo
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Modelos Animais de Doenças
Transporte de Elétrons/fisiologia
Glutationa/fisiologia
Isoenzimas
Ratos
Ratos Wistar
ATPase Trocadora de Sódio-Potássio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); EC 2.7.3.2 (Creatine Kinase); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase); GAN16C9B8O (Glutathione); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:0909
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090417
[St] Status:MEDLINE
[do] DOI:10.1007/s11011-009-9131-z


  8 / 10 MEDLINE  
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[PMID]:17088338
[Au] Autor:Bok LA; Struys E; Willemsen MA; Been JV; Jakobs C
[Ad] Endereço:Department of Paediatrics, Máxima Medical Center, Veldhoven, The Netherlands. L.Bok@mmc.nl
[Ti] Título:Pyridoxine-dependent seizures in Dutch patients: diagnosis by elevated urinary alpha-aminoadipic semialdehyde levels.
[So] Source:Arch Dis Child;92(8):687-9, 2007 Aug.
[Is] ISSN:1468-2044
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pyridoxine-dependent seizures (PDS) is a rare, autosomal recessively inherited disorder. Recently alpha-aminoadipic semialdehyde (alpha-AASA) dehydrogenase deficiency was identified as a major cause of PDS, which causes accumulation of both alpha-AASA and pipecolic acid (PA) in body fluids. METHODS: We studied urinary and plasma alpha-AASA and PA levels in 12 Dutch clinically diagnosed patients with PDS. RESULTS: Alpha-AASA was elevated in both urine and plasma in 10 patients. In these patients plasma PA levels were also elevated but urinary PA levels were normal. DISCUSSION: In all patients with clinically definite PDS, and in most patients with probable or possible PDS, the clinical diagnosis of PDS could be confirmed at the metabolite level. Non-invasive urinary screening for alpha-AASA accumulation provides a reliable tool to diagnose PDS and can save these patients from the classical and potentially dangerous pyridoxine withdrawal test to prove PDS.
[Mh] Termos MeSH primário: Hiperlisinemias/diagnóstico
Ácidos Pipecólicos
Convulsões/diagnóstico
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/sangue
Aldeído Desidrogenase/urina
Biomarcadores/sangue
Biomarcadores/urina
Feminino
Seres Humanos
Países Baixos
Ácidos Pipecólicos/sangue
Ácidos Pipecólicos/urina
Piridoxina/uso terapêutico
Convulsões/sangue
Convulsões/urina
Complexo Vitamínico B/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Pipecolic Acids); 12001-76-2 (Vitamin B Complex); EC 1.2.1.3 (ALDH7A1 protein, human); EC 1.2.1.3 (Aldehyde Dehydrogenase); KV2JZ1BI6Z (Pyridoxine)
[Em] Mês de entrada:0708
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:061108
[St] Status:MEDLINE


  9 / 10 MEDLINE  
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[PMID]:15759964
[Au] Autor:Tofil NM; Benner KW; Winkler MK
[Ad] Endereço:Division of Pediatric Critical Care Medicine, Department of Pediatrics, the University of Alabama at Birmingham, Birmingham, AL, USA. ntofil@peds.uab.edu
[Ti] Título:Fatal hypermagnesemia caused by an Epsom salt enema: a case illustration.
[So] Source:South Med J;98(2):253-6, 2005 Feb.
[Is] ISSN:0038-4348
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The authors describe a case of fatal hypermagnesemia caused by an Epsom salt enema. A 7-year-old male presented with cardiac arrest and was found to have a serum magnesium level of 41.2 mg/dL (33.9 mEq/L) after having received an Epsom salt enema earlier that day. The medical history of Epsom salt, the common causes and symptoms of hypermagnesemia, and the treatment of hypermagnesemia are reviewed. The easy availability of magnesium, the subtle initial symptoms of hypermagnesemia, and the need for education about the toxicity of magnesium should be of interest to physicians.
[Mh] Termos MeSH primário: Hiperlisinemias/etiologia
Sulfato de Magnésio/efeitos adversos
[Mh] Termos MeSH secundário: Dor Abdominal/terapia
Criança
Enema/efeitos adversos
Evolução Fatal
Parada Cardíaca/terapia
Seres Humanos
Magnésio/sangue
Sulfato de Magnésio/uso terapêutico
Masculino
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
7487-88-9 (Magnesium Sulfate); I38ZP9992A (Magnesium)
[Em] Mês de entrada:0505
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:050312
[St] Status:MEDLINE


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[PMID]:10775527
[Au] Autor:Sacksteder KA; Biery BJ; Morrell JC; Goodman BK; Geisbrecht BV; Cox RP; Gould SJ; Geraghty MT
[Ad] Endereço:Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.
[Ti] Título:Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia.
[So] Source:Am J Hum Genet;66(6):1736-43, 2000 Jun.
[Is] ISSN:0002-9297
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The first two steps in the mammalian lysine-degradation pathway are catalyzed by lysine-ketoglutarate reductase and saccharopine dehydrogenase, respectively, resulting in the conversion of lysine to alpha-aminoadipic semialdehyde. Defects in one or both of these activities result in familial hyperlysinemia, an autosomal recessive condition characterized by hyperlysinemia, lysinuria, and variable saccharopinuria. In yeast, lysine-ketoglutarate reductase and saccharopine dehydrogenase are encoded by the LYS1 and LYS9 genes, respectively, and we searched the available sequence databases for their human homologues. We identified a single cDNA that encoded an apparently bifunctional protein, with the N-terminal half similar to that of yeast LYS1 and with the C-terminal half similar to that of yeast LYS9. This bifunctional protein has previously been referred to as "alpha-aminoadipic semialdehyde synthase," and we have tentatively designated this gene "AASS." The AASS cDNA contains an open reading frame of 2,781 bp predicted to encode a 927-amino-acid-long protein. The gene has been sequenced and contains 24 exons scattered over 68 kb and maps to chromosome 7q31.3. Northern blot analysis revealed the presence of several transcripts in all tissues examined, with the highest expression occurring in the liver. We sequenced the genomic DNA from a single patient with hyperlysinemia (JJa). The patient is the product of a consanguineous mating and is homozygous for an out-of-frame 9-bp deletion in exon 15, which results in a premature stop codon at position 534 of the protein. On the basis of these and other results, we propose that AASS catalyzes the first two steps of the major lysine-degradation pathway in human cells and that inactivating mutations in the AASS gene are a cause of hyperlysinemia.
[Mh] Termos MeSH primário: Hiperlisinemias/enzimologia
Hiperlisinemias/genética
Complexos Multienzimáticos/genética
Mutação/genética
Sacaropina Desidrogenases/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Cromossomos Humanos Par 7/genética
Clonagem Molecular
Consanguinidade
Análise Mutacional de DNA
Éxons/genética
Feminino
Perfilação da Expressão Gênica
Genes Recessivos/genética
Homozigoto
Seres Humanos
Hibridização in Situ Fluorescente
Lisina/metabolismo
Masculino
Dados de Sequência Molecular
Complexos Multienzimáticos/química
Complexos Multienzimáticos/metabolismo
Mapeamento Físico do Cromossomo
Sítios de Splice de RNA/genética
RNA Mensageiro/análise
RNA Mensageiro/genética
Sacaropina Desidrogenases/química
Sacaropina Desidrogenases/metabolismo
Alinhamento de Sequência
Deleção de Sequência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (RNA Splice Sites); 0 (RNA, Messenger); EC 1.5.1.- (AASS protein, human); EC 1.5.1.- (Saccharopine Dehydrogenases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:0106
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:000425
[St] Status:MEDLINE



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