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[PMID]:29231630
[Au] Autor:Bliksrud YT
[Ti] Título:Tenuous link between chronic fatigue syndrome and pyruvate dehydrogenase deficiency.
[Ti] Título:Svak kobling mellom kronisk utmattelsessyndrom og pyruvat dehydrogenasemangel..
[So] Source:Tidsskr Nor Laegeforen;137(23-24), 2017 12 12.
[Is] ISSN:0807-7096
[Cp] País de publicação:Norway
[La] Idioma:eng; nor
[Mh] Termos MeSH primário: Síndrome de Fadiga Crônica
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Síndrome de Fadiga Crônica/etiologia
Síndrome de Fadiga Crônica/metabolismo
Seres Humanos
Doença da Deficiência do Complexo de Piruvato Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.4045/tidsskr.17.0948


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[PMID]:28202214
[Au] Autor:Bedoyan JK; Yang SP; Ferdinandusse S; Jack RM; Miron A; Grahame G; DeBrosse SD; Hoppel CL; Kerr DS; Wanders RJ
[Ad] Endereço:Center for Human Genetics, University Hospitals Cleveland Medical Center, Cleveland, OH, USA; Department of Genetics and Genome Sciences, Case Western Reserve University, Cleveland, OH, USA; Center for Inherited Disorders of Energy Metabolism (CIDEM), University Hospitals Cleveland Medical Center, C
[Ti] Título:Lethal neonatal case and review of primary short-chain enoyl-CoA hydratase (SCEH) deficiency associated with secondary lymphocyte pyruvate dehydrogenase complex (PDC) deficiency.
[So] Source:Mol Genet Metab;120(4):342-349, 2017 Apr.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in ECHS1 result in short-chain enoyl-CoA hydratase (SCEH) deficiency which mainly affects the catabolism of various amino acids, particularly valine. We describe a case compound heterozygous for ECHS1 mutations c.836T>C (novel) and c.8C>A identified by whole exome sequencing of proband and parents. SCEH deficiency was confirmed with very low SCEH activity in fibroblasts and nearly absent immunoreactivity of SCEH. The patient had a severe neonatal course with elevated blood and cerebrospinal fluid lactate and pyruvate concentrations, high plasma alanine and slightly low plasma cystine. 2-Methyl-2,3-dihydroxybutyric acid was markedly elevated as were metabolites of the three branched-chain α-ketoacids on urine organic acids analysis. These urine metabolites notably decreased when lactic acidosis decreased in blood. Lymphocyte pyruvate dehydrogenase complex (PDC) activity was deficient, but PDC and α-ketoglutarate dehydrogenase complex activities in cultured fibroblasts were normal. Oxidative phosphorylation analysis on intact digitonin-permeabilized fibroblasts was suggestive of slightly reduced PDC activity relative to control range in mitochondria. We reviewed 16 other cases with mutations in ECHS1 where PDC activity was also assayed in order to determine how common and generalized secondary PDC deficiency is associated with primary SCEH deficiency. For reasons that remain unexplained, we find that about half of cases with primary SCEH deficiency also exhibit secondary PDC deficiency. The patient died on day-of-life 39, prior to establishing his diagnosis, highlighting the importance of early and rapid neonatal diagnosis because of possible adverse effects of certain therapeutic interventions, such as administration of ketogenic diet, in this disorder. There is a need for better understanding of the pathogenic mechanisms and phenotypic variability in this relatively recently discovered disorder.
[Mh] Termos MeSH primário: Enoil-CoA Hidratase/deficiência
Doença da Deficiência do Complexo de Piruvato Desidrogenase/mortalidade
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Enoil-CoA Hidratase/genética
Exoma
Seres Humanos
Recém-Nascido
Masculino
Polimorfismo de Nucleotídeo Único
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 4.2.1.17 (Enoyl-CoA Hydratase); EC 4.2.1.17 (enoyl CoA hydratase, short chain, 1, mitochondrial, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE


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[PMID]:27586246
[Au] Autor:Pasca L; De Giorgis V; Macasaet JA; Trentani C; Tagliabue A; Veggiotti P
[Ad] Endereço:Department of Child Neurology and Psychiatry, IRCCS "C. Mondino" National Neurological Institute, Pavia, Italy.
[Ti] Título:The changing face of dietary therapy for epilepsy.
[So] Source:Eur J Pediatr;175(10):1267-76, 2016 Oct.
[Is] ISSN:1432-1076
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Ketogenic diet is an established and effective non-pharmacologic treatment for drug-resistant epilepsy. Ketogenic diet represents the treatment of choice for GLUT-1 deficiency syndrome and pyruvate dehydrogenase complex deficiency. Infantile spasms, Dravet syndrome and myoclonic-astatic epilepsy are epilepsy syndromes for which ketogenic diet should be considered early in the therapeutic pathway. Recently, clinical indications for ketogenic diet have been increasing, as there is emerging evidence regarding safety and effectiveness. Specifically, ketogenic diet response has been investigated in refractory status epilepticus and encephalopathy with status epilepticus during sleep. New targets in neuropharmacology, such as mitochondrial permeability transition, are being studied and might lead to using it effectively in other neurological diseases. But, inefficient connectivity and impaired ketogenic diet proposal limit ideal availability of this therapeutic option. Ketogenic diet in Italy is not yet considered as standard of care, not even as a therapeutic option for many child neurologists and epileptologists. CONCLUSIONS: The aim of this review is to revisit ketogenic diet effectiveness and safety in order to highlight its importance in drug-resistant epilepsy and other neurological disorders. WHAT IS KNOWN: • Ketogenic diet efficacy is now described in large case series, with adequate diet compliance and side effects control. • Ketogenic diet is far from being attempted as a first line therapy. Its availability varies worldwide. What is New: • New pharmacological targets such as mitochondrial permeability transition and new epileptic syndromes and etiologies responding to the diet such as refractory status epilepticus are being pointed out. • Ketogenic diet can function at its best when used as a tailor-made therapy. Fine tuning is crucial.
[Mh] Termos MeSH primário: Dieta Cetogênica/métodos
Epilepsia Resistente a Medicamentos/dietoterapia
[Mh] Termos MeSH secundário: Erros Inatos do Metabolismo dos Carboidratos/dietoterapia
Criança
Dieta Cetogênica/efeitos adversos
Dieta Cetogênica/economia
Seres Humanos
Proteínas de Transporte de Monossacarídeos/deficiência
Neoplasias/dietoterapia
Doença da Deficiência do Complexo de Piruvato Desidrogenase/dietoterapia
Convulsões/dietoterapia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Monosaccharide Transport Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160903
[St] Status:MEDLINE
[do] DOI:10.1007/s00431-016-2765-z


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[PMID]:27343776
[Au] Autor:Pinheiro A; Silva MJ; Pavlu-Pereira H; Florindo C; Barroso M; Marques B; Correia H; Oliveira A; Gaspar A; Tavares de Almeida I; Rivera I
[Ad] Endereço:Metabolism & Genetics Group, Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, Portugal.
[Ti] Título:Complex genetic findings in a female patient with pyruvate dehydrogenase complex deficiency: Null mutations in the PDHX gene associated with unusual expression of the testis-specific PDHA2 gene in her somatic cells.
[So] Source:Gene;591(2):417-24, 2016 Oct 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Human pyruvate dehydrogenase complex (PDC) catalyzes a key step in the generation of cellular energy and is composed by three catalytic elements (E1, E2, E3), one structural subunit (E3-binding protein), and specific regulatory elements, phosphatases and kinases (PDKs, PDPs). The E1α subunit exists as two isoforms encoded by different genes: PDHA1 located on Xp22.1 and expressed in somatic tissues, and the intronless PDHA2 located on chromosome 4 and only detected in human spermatocytes and spermatids. We report on a young adult female patient who has PDC deficiency associated with a compound heterozygosity in PDHX encoding the E3-binding protein. Additionally, in the patient and in all members of her immediate family, a full-length testis-specific PDHA2 mRNA and a 5'UTR-truncated PDHA1 mRNA were detected in circulating lymphocytes and cultured fibroblasts, being both mRNAs translated into full-length PDHA2 and PDHA1 proteins, resulting in the co-existence of both PDHA isoforms in somatic cells. Moreover, we observed that DNA hypomethylation of a CpG island in the coding region of PDHA2 gene is associated with the somatic activation of this gene transcription in these individuals. This study represents the first natural model of the de-repression of the testis-specific PDHA2 gene in human somatic cells, and raises some questions related to the somatic activation of this gene as a potential therapeutic approach for most forms of PDC deficiency.
[Mh] Termos MeSH primário: Mutação
Piruvato Desidrogenase (Lipoamida)/genética
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
Complexo Piruvato Desidrogenase/genética
[Mh] Termos MeSH secundário: Adulto
Células Cultivadas
Feminino
Fibroblastos/metabolismo
Dosagem de Genes
Expressão Gênica
Heterozigoto
Seres Humanos
Masculino
Complexo Piruvato Desidrogenase/metabolismo
RNA Mensageiro
Testículo/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PDHX protein, human); 0 (Pyruvate Dehydrogenase Complex); 0 (RNA, Messenger); EC 1.2.4.1 (PDHA2 protein, human); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170127
[Lr] Data última revisão:
170127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160626
[St] Status:MEDLINE


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[PMID]:27026023
[Au] Autor:Natarajan N; Tully HM; Chapman T
[Ad] Endereço:Department of Pediatrics, Seattle Children's Hospital, University of Washington School of Medicine, Seattle, WA, USA.
[Ti] Título:Prenatal presentation of pyruvate dehydrogenase complex deficiency.
[So] Source:Pediatr Radiol;46(9):1354-7, 2016 Aug.
[Is] ISSN:1432-1998
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We present the case of a female infant referred for prenatal MR evaluation of ventriculomegaly, which had been attributed by the referring obstetrician to aqueductal stenosis. Fetal MR confirmed ventriculomegaly but also demonstrated cerebral volume loss and white matter abnormalities. After birth, the infant developed persistent lactic acidosis. A diagnosis of pyruvate dehydrogenase complex deficiency was made on the basis of metabolic and molecular genetic studies. Ventriculomegaly is a common referral reason for fetal MR, yet there are few published reports of the radiographic findings that accompany inborn errors of metabolism, one potentially under-recognized cause of enlarged ventricles. This case contributes to this small body of literature on the imaging features of pyruvate dehydrogenase complex deficiency by describing pre- and postnatal MR findings and key clinical details. Our report emphasizes the necessity of considering pyruvate dehydrogenase complex deficiency and other metabolic disorders as potential etiologies for fetal ventriculomegaly since prompt diagnosis may allow for early initiation of treatment and improve outcome.
[Mh] Termos MeSH primário: Imagem por Ressonância Magnética/métodos
Doença da Deficiência do Complexo de Piruvato Desidrogenase/diagnóstico por imagem
Ultrassonografia Pré-Natal/métodos
[Mh] Termos MeSH secundário: Adulto
Diagnóstico Diferencial
Feminino
Seres Humanos
Recém-Nascido
Gravidez
Diagnóstico Pré-Natal
Doença da Deficiência do Complexo de Piruvato Desidrogenase/terapia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160331
[St] Status:MEDLINE
[do] DOI:10.1007/s00247-016-3585-z


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[PMID]:26865159
[Au] Autor:Pirot N; Crahes M; Adle-Biassette H; Soares A; Bucourt M; Boutron A; Carbillon L; Mignot C; Trestard L; Bekri S; Laquerrière A
[Ad] Endereço:From the Department of Radiology (NP), Pathology Laboratory (MC, AL), and Department of Metabolic Biochemistry (AS, SB), Rouen University Hospital, Rouen, France; Pathology Department (HAB), Lariboisière University Hospital, Rouen, France; Pathology Laboratory (MB), Jean Verdier University Hospital,
[Ti] Título:Phenotypic and Neuropathological Characterization of Fetal Pyruvate Dehydrogenase Deficiency.
[So] Source:J Neuropathol Exp Neurol;75(3):227-38, 2016 Mar.
[Is] ISSN:1554-6578
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To distinguish pyruvate dehydrogenase deficiency (PDH) from other antenatal neurometabolic disorders thereby improving prenatal diagnosis, we describe imaging findings, clinical phenotype, and brain lesions in fetuses from 3 families with molecular characterization of this condition. Neuropathological analysis was performed in 4 autopsy cases from 3 unrelated families with subsequent biochemical and molecular confirmation of PDH complex deficiency. In 2 families there were mutations in the PDHA1 gene; in the third family there was a mutation in the PDHB gene. All fetuses displayed characteristic craniofacial dysmorphism of varying severity, absence of visceral lesions, and associated encephaloclastic and developmental supra- and infratentorial lesions. Neurodevelopmental abnormalities included microcephaly, migration abnormalities (pachygyria, polymicrogyria, periventricular nodular heterotopias), and cerebellar and brainstem hypoplasia with hypoplastic dentate nuclei and pyramidal tracts. Associated clastic lesions included asymmetric leukomalacia, reactive gliosis, large pseudocysts of germinolysis, and basal ganglia calcifications. The diagnosis of PDH deficiency should be suspected antenatally with the presence of clastic and neurodevelopmental lesions and a relatively characteristic craniofacial dysmorphism. Postmortem examination is essential for excluding other closely related entities, thereby allowing for biochemical and molecular confirmation.
[Mh] Termos MeSH primário: Doenças Fetais/patologia
Feto/patologia
Doença da Deficiência do Complexo de Piruvato Desidrogenase/patologia
Doença da Deficiência do Complexo de Piruvato Desidrogenase/fisiopatologia
[Mh] Termos MeSH secundário: Adulto
Feminino
Doenças Fetais/genética
Doenças Fetais/fisiopatologia
Seres Humanos
Imagem por Ressonância Magnética
Mutação
Fenótipo
Gravidez
Piruvato Desidrogenase (Lipoamida)/genética
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
Ultrassonografia Pré-Natal
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160517
[Lr] Data última revisão:
160517
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160212
[St] Status:MEDLINE
[do] DOI:10.1093/jnen/nlv022


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[PMID]:26354166
[Au] Autor:Bhandary S; Aguan K
[Ad] Endereço:Department of Biotechnology & Bioinformatics, North-Eastern Hill University, Shillong 793 022, India; Division of Molecular Medicine, Bose Institute, Kolkata 700 054, India.
[Ti] Título:Pyruvate dehydrogenase complex deficiency and its relationship with epilepsy frequency--An overview.
[So] Source:Epilepsy Res;116:40-52, 2015 Oct.
[Is] ISSN:1872-6844
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The pyruvate dehydrogenase complex (PDHc) is a member of a family of multienzyme complexes that provides the link between glycolysis and the tricarboxylic acid (TCA) cycle by catalyzing the physiologically irreversible decarboxylation of various 2-oxoacid substrates to their corresponding acyl-CoA derivatives, NADH and CO2. PDHc deficiency is a metabolic disorder commonly associated with lactic acidosis, progressive neurological and neuromuscular degeneration that vary with age and gender. In this review, we aim to discuss the relationship between occurrence of epilepsy and PDHc deficiency associated with the pyruvate dehydrogenase complex (E1α subunit (PDHA1) and E1ß subunit (PDHB)) and PDH phosphatase (PDP) deficiency. PDHc plays a crucial role in the aerobic carbohydrate metabolism and regulates the use of carbohydrate as the source of oxidative energy. In severe PDHc deficiency, the energy deficit impairs brain development in utero resulting in physiological and structural changes in the brain that contributes to the subsequent onset of epileptogenesis. Epileptogenesis in PDHc deficiency is linked to energy failure and abnormal neurotransmitter metabolism that progressively alters neuronal excitability. This metabolic blockage might be restricted via inclusion of ketogenic diet that is broken up by ß-oxidation and directly converting it to acetyl-CoA, and thereby improving the patient's health condition. Genetic counseling is essential as PDHA1 deficiency is X-linked. The demonstration of the X-chromosome localization of PDHA1 resolved a number of questions concerning the variable phenotype displayed by patients with E1 deficiency. Most patients show a broad range of neurological abnormalities, with the severity showing some dependence on the nature of the mutation in the Elα gene, while PDHB and PDH phosphatase (PDP) deficiencies are of autosomal recessive inheritance. However, in females, the disorder is further complicated by the pattern of X-chromosome inactivation, i.e., unfavorable lyonization. Furthermore research should focus on epileptogenic animal models; this might pave a new way toward identification of the pathophysiology of this challenging disorder.
[Mh] Termos MeSH primário: Epilepsia/etiologia
Doença da Deficiência do Complexo de Piruvato Desidrogenase/complicações
[Mh] Termos MeSH secundário: Animais
Epilepsia/genética
Seres Humanos
Piruvato Desidrogenase (Lipoamida)/genética
Piruvato Desidrogenase (Lipoamida)/metabolismo
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150910
[Lr] Data última revisão:
150910
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150911
[St] Status:MEDLINE


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[PMID]:26287337
[Au] Autor:Wu ML; Liu L; Mao XJ; Peng MZ; Liu HS; Sheng HY; Cai YN; Mei HF; Fan C; Huang YL; Li XZ; Cheng J
[Ad] Endereço:Department of Genetics and Endocrinology, Guangzhou Children and Women's Medical Center, Guangzhou 510623, China. liliuxia@hotmail.com.
[Ti] Título:[Identification of a novel pathogenic mutation in PDHA1 gene for pyruvate dehydrogenase complex deficiency].
[So] Source:Zhongguo Dang Dai Er Ke Za Zhi;17(8):775-9, 2015 Aug.
[Is] ISSN:1008-8830
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To study the molecular genetic mechanism and genetic diagnosis of pyruvate dehydrogenase complex deficiency (PHD), and to provide a basis for genetic counseling and prenatal genetic diagnosis of PHD. METHODS: Polymerase chain reaction (PCR) was performed to amplify the 11 exons and exon junction of the PDHA1 gene from a child who was diagnosed with PHD based on clinical characteristics and laboratory examination results. The PCR products were sequenced to determine the mutation. An analysis of amino acid conservation and prediction of protein secondary and tertiary structure were performed using bioinformatic approaches to identify the pathogenicity of the novel mutation. RESULTS: One novel duplication mutation, c.1111_1158dup48bp, was found in the exon 11 of the PDHA1 gene of the patient. No c.1111_1158dup48bp mutation was detected in the sequencing results from 50 normal controls. The results of protein secondary and tertiary structure prediction showed that the novel mutation c.1111 _1158dup48bp led to the duplication of 16 amino acids residues, serine371 to phenylalanine386, which induced a substantial change in protein secondary and tertiary structure. The conformational change was not detected in the normal controls. CONCLUSIONS: The novel duplication mutation c.1111_1158dup48bp in the PDHA1 gene is not due to gene polymorphisms but a possible novel pathogenic mutation for PHD.
[Mh] Termos MeSH primário: Mutação
Piruvato Desidrogenase (Lipoamida)/genética
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Seres Humanos
Lactente
Masculino
Dados de Sequência Molecular
Conformação Proteica
Piruvato Desidrogenase (Lipoamida)/química
[Pt] Tipo de publicação:CASE REPORTS; ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150820
[Lr] Data última revisão:
150820
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150820
[St] Status:MEDLINE


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[PMID]:26008863
[Au] Autor:Castiglioni C; Verrigni D; Okuma C; Diaz A; Alvarez K; Rizza T; Carrozzo R; Bertini E; Miranda M
[Ad] Endereço:Unit of Neurology, Dept. of Pediatrics and Dept. of Neurology, Clínica las Condes, Santiago, Chile. Electronic address: ccastiglioni@clc.cl.
[Ti] Título:Pyruvate dehydrogenase deficiency presenting as isolated paroxysmal exercise induced dystonia successfully reversed with thiamine supplementation. Case report and mini-review.
[So] Source:Eur J Paediatr Neurol;19(5):497-503, 2015 Sep.
[Is] ISSN:1532-2130
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pyruvate dehydrogenase (PDH) deficiency is a disorder of energy metabolism with variable clinical presentations, ranging from severe infantile lactic acidosis to milder chronic neurological disorders. The spectrum of clinical manifestations is continuously expanding. METHODS AND RESULTS: We report on a 19-year-old intelligent female with PDH deficiency caused by a Leu216Ser mutation in PDHA1. She presented with recurrent hemidystonic attacks, triggered by prolonged walking or running, as the unique clinical manifestation that manifested since childhood. Laboratory workup and neuroimages were initially normal but bilateral globus pallidum involvement appeared later on brain MRI. Dystonia completely remitted after high doses of thiamine, remaining free of symptoms after 3 years of follow up. We reviewed the literature for similar observations. CONCLUSIONS: Dystonia precipitated by exercise may be the only symptom of a PDH deficiency, and the hallmark of the disease as high serum lactate or bilateral striatal necrosis at neuroimaging may be absent. A high index of suspicion and follow up is necessary for diagnosis. The clinical presentation of this patient meets the criteria for a Paroxysmal Exercise induced Dystonia, leading us to add this entity as another potential etiology for this type of paroxysmal dyskinesia, which is besides a treatable condition that responds to thiamine supplementation.
[Mh] Termos MeSH primário: Suplementos Nutricionais
Distúrbios Distônicos/etiologia
Doença da Deficiência do Complexo de Piruvato Desidrogenase/complicações
Doença da Deficiência do Complexo de Piruvato Desidrogenase/tratamento farmacológico
Tiamina/uso terapêutico
[Mh] Termos MeSH secundário: Encéfalo/patologia
Feminino
Seres Humanos
Imagem por Ressonância Magnética
Doença da Deficiência do Complexo de Piruvato Desidrogenase/diagnóstico
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
X66NSO3N35 (Thiamine)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150804
[Lr] Data última revisão:
150804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE


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[PMID]:25601413
[Au] Autor:Ferriero R; Iannuzzi C; Manco G; Brunetti-Pierri N
[Ad] Endereço:Telethon Institute of Genetics and Medicine, Via Campi Felgrei, 34, 80078, Pozzuoli, Naples, Italy.
[Ti] Título:Differential inhibition of PDKs by phenylbutyrate and enhancement of pyruvate dehydrogenase complex activity by combination with dichloroacetate.
[So] Source:J Inherit Metab Dis;38(5):895-904, 2015 Sep.
[Is] ISSN:1573-2665
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pyruvate dehydrogenase complex (PDHC) is a key enzyme in metabolism linking glycolysis to tricarboxylic acid cycle and its activity is tightly regulated by phosphorylation catalyzed by four pyruvate dehydrogenase kinase (PDK) isoforms. PDKs are pharmacological targets for several human diseases including cancer, diabetes, obesity, heart failure, and inherited PDHC deficiency. We investigated the inhibitory activity of phenylbutyrate toward PDKs and found that PDK isoforms 1-to-3 are inhibited whereas PDK4 is unaffected. Moreover, docking studies revealed putative binding sites of phenylbutyrate on PDK2 and 3 that are located on different sites compared to dichloroacetate (DCA), a previously known PDK inhibitor. Based on these findings, we showed both in cells and in mice that phenylbutyrate combined to DCA results in greater increase of PDHC activity compared to each drug alone. These results suggest that therapeutic efficacy can be enhanced by combination of drugs increasing PDHC enzyme activity.
[Mh] Termos MeSH primário: Ácido Dicloroacético/farmacologia
Fenilbutiratos/farmacologia
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Células Cultivadas
Ácido Dicloroacético/química
Ácido Dicloroacético/metabolismo
Ativação Enzimática/efeitos dos fármacos
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Fenilbutiratos/química
Fenilbutiratos/metabolismo
Proteínas Serina-Treonina Quinases/química
Proteínas Serina-Treonina Quinases/metabolismo
Complexo Piruvato Desidrogenase/antagonistas & inibidores
Complexo Piruvato Desidrogenase/química
Doença da Deficiência do Complexo de Piruvato Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Phenylbutyrates); 0 (Pyruvate Dehydrogenase Complex); 7WY7YBI87E (4-phenylbutyric acid); 9LSH52S3LQ (Dichloroacetic Acid); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150121
[St] Status:MEDLINE
[do] DOI:10.1007/s10545-014-9808-2



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