Database : MEDLINE
Search on : Mitochondrial and Myopathies [Words]
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[PMID]: 29338979
[Au] Autor:Schänzer A; Rupp S; Gräf S; Zengeler D; Jux C; Akintürk H; Gulatz L; Mazhari N; Acker T; Van Coster R; Garvalov BK; Hahn A
[Ad] Address:Institute of Neuropathology, Justus Liebig University Giessen, 35392 Giessen, Germany. Electronic address: anne.schaenzer@patho.med.uni-giessen.de.
[Ti] Title:Dysregulated autophagy in restrictive cardiomyopathy due to Pro209Leu mutation in BAG3.
[So] Source:Mol Genet Metab;123(3):388-399, 2018 Mar.
[Is] ISSN:1096-7206
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Myofibrillary myopathies (MFM) are hereditary myopathies histologically characterized by degeneration of myofibrils and aggregation of proteins in striated muscle. Cardiomyopathy is common in MFM but the pathophysiological mechanisms are not well understood. The BAG3-Pro209Leu mutation is associated with early onset MFM and severe restrictive cardiomyopathy (RCM), often necessitating heart transplantation during childhood. We report on a young male patient with a BAG3-Pro209Leu mutation who underwent heart transplantation at eight years of age. Detailed morphological analyses of the explanted heart tissue showed intracytoplasmic inclusions, aggregation of BAG3 and desmin, disintegration of myofibers and Z-disk alterations. The presence of undegraded autophagosomes, seen by electron microscopy, as well as increased levels of p62, LC3-I and WIPI1, detected by immunohistochemistry and western blot analyses, indicated a dysregulation of autophagy. Parkin and PINK1, proteins involved in mitophagy, were slightly increased whereas mitochondrial OXPHOS activities were not altered. These findings indicate that altered autophagy plays a role in the pathogenesis and rapid progression of RCM in MFM caused by the BAG3-Pro209Leu mutation, which could have implications for future therapeutic strategies.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180301
[Lr] Last revision date:180301
[St] Status:In-Data-Review

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[PMID]: 29174468
[Au] Autor:Scarpelli M; Carreño-Gago L; Russignan A; de Luna N; Carnicer-Cáceres C; Ariatti A; Verriello L; Devigili G; Tonin P; Garcia-Arumi E; Pinós T
[Ad] Address:Section of Neurology, Department of Neurological, Biomedical and Movement Sciences, University of Verona, Verona, Italy.
[Ti] Title:Identification and characterization of the novel m.8305C>T MTTK and m.4440G>A MTTM gene mutations causing mitochondrial myopathies.
[So] Source:Neuromuscul Disord;28(2):137-143, 2018 Feb.
[Is] ISSN:1873-2364
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:We report on two novel mtDNA mutations in patients affected with mitochondrial myopathy. The first patient, a 44-year-old woman, had bilateral eyelid ptosis and the m.8305C>T mutation in the MTTK gene. The second patient, a 56-year-old man, had four-limb muscle weakness and the MTTM gene m.4440G>A mutation. Muscle biopsies in both patients showed ragged red fibers and numerous COX-negative fibers as well as a combined defect of complex I, III and IV activities. The two mutations were heteroplasmic and detected only in muscle tissue, with a higher mutation load in COX-negative fibers. Additionally, both mutations occurred in highly conserved mt-tRNA sites, and were not found by an in silico search in 30,589 human mtDNA sequences. Our report further expands the mutational and phenotypic spectrum of diseases associated with mutations in mitochondrial tRNA genes and reinforces the notion that mutations in mitochondrial tRNAs represent hot spots for mitochondrial myopathies in adults.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1711
[Cu] Class update date: 180225
[Lr] Last revision date:180225
[St] Status:In-Data-Review

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[PMID]: 29368910
[Au] Autor:Sinyov VV; Chicheva MM; Barinova VA; Ryzhkova AI; Zilinyi RI; Karagodin VP; Postnov AY; Sobenin IA; Orekhov AN; Sazonova MA
[Ti] Title:[The heteroplasmy level of some mutations in gene MT-CYB among women with asymptomatic atherosclerosis].
[So] Source:Genetika;52(8):951-7, 2016 Aug.
[Is] ISSN:0016-6758
[Cp] Country of publication:Russia (Federation)
[La] Language:rus
[Ab] Abstract:Atherosclerosis is a polygenic socially significant disease whose risk factors include coronary heart disease, diabetes, hypertension, and myocardial infarction. According to the literature, mutations m.14846G>A (G34S), m.15762G>A (G339Q), m.15084G>A (W113Ter), and m.15059G>A (G190Ter) of cytochrome B gene (MT-CYB) are associated with mitochondrial myopathies, myoglobinuria, and exercise intolerance. Preliminary studies carried out by the authors made it possible to discover an association of certain mitochondrial genome mutations with atherosclerotic lesions of aortic intima in people who died as a result of an accident or sudden death. The most interesting seemed to be the data on the association of mutations m.14846G>A and m.15059G>A of the cytochrome B gene with lipofibrous aortic plaques, because these mutations affect the mitochondrial respiratory chain enzyme. Defects in the given chain may be the reason for the launch of pathogenic mechanisms in the human body. Owing to the fact that mutations in the mitochondrial genome are inherited by the maternal type, it was decided to analyze cytochrome B gene mutations in a sample of female volunteers from Moscow oblast. According to the findings, mutations m.14846G>A and m.15059G>A are highly significantly associated with atherosclerotic lesions of the carotid arteries: m.14846G>A is antiatherogenic and m.15059G>A is proatherogenic.
[Mh] MeSH terms primary: Atherosclerosis/genetics
Carotid Artery Diseases/genetics
Cytochromes b/genetics
Mutation
Plaque, Atherosclerotic/genetics
[Mh] MeSH terms secundary: Adult
Aged
Aged, 80 and over
Atherosclerosis/enzymology
Carotid Artery Diseases/enzymology
Female
Humans
Middle Aged
Plaque, Atherosclerotic/enzymology
[Pt] Publication type:CLINICAL TRIAL; JOURNAL ARTICLE
[Nm] Name of substance:9035-37-4 (Cytochromes b)
[Em] Entry month:1802
[Cu] Class update date: 180205
[Lr] Last revision date:180205
[Js] Journal subset:IM
[Da] Date of entry for processing:180126
[St] Status:MEDLINE

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[PMID]: 29361167
[Au] Autor:Bartsakoulia M; Pyle A; Troncosco D; Vial J; Paz-Fiblas MV; Duff J; Griffin H; Boczonadi V; Lochmüller H; Kleinle S; Chinnery PF; Grünert S; Kirschner J; Eisner V; Horvath R
[Ad] Address:Wellcome Centre for Mitochondrial Research, Institute of Genetic Medicine, Newcastle University, Central Parkway, Newcastle upon Tyne, NE1 3BZ UK.
[Ti] Title:A novel mechanism causing imbalance of mitochondrial fusion and fission in human myopathies.
[So] Source:Hum Mol Genet;, 2018 Jan 19.
[Is] ISSN:1460-2083
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Mitochondrial dynamics play an important role in cellular homeostasis and a variety of human diseases are linked to its dysregulated function. Here we describe a 15-year-old boy with a novel disease caused by altered mitochondrial dynamics. The patient was the second child of consanguineous Jewish parents. He developed progressive muscle weakness and exercise intolerance at 6 years of age. His muscle biopsy revealed mitochondrial myopathy with numerous ragged red and cytochrome c oxidase (COX) negative fibers and combined respiratory chain complex I and IV deficiency. MtDNA copy number was elevated and no deletions of the mtDNA were detected in muscle DNA. Whole exome sequencing identified a homozygous nonsense mutation (p.Q92*) in the MIEF2 gene encoding the mitochondrial dynamics protein of 49 kDa (MID49). Immunoblotting revealed increased levels of proteins promoting mitochondrial fusion (MFN2, OPA1) and decreased levels of the fission protein DRP1. Fibroblasts of the patient showed elongated mitochondria, and significantly higher frequency of fusion events, mtDNA abundance and aberrant mitochondrial cristae ultrastructure, compared to controls. Thus, our data suggest that mutations in MIEF2 result in imbalanced mitochondrial dynamics and a combined respiratory chain enzyme defect in skeletal muscle, leading to mitochondrial myopathy.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180123
[Lr] Last revision date:180123
[St] Status:Publisher
[do] DOI:10.1093/hmg/ddy033

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[PMID]: 29074296
[Au] Autor:Mancuso M; McFarland R; Klopstock T; Hirano M; consortium on Trial Readiness in Mitochondrial Myopathies
[Ad] Address:Department of Experimental and Clinical Medicine, Neurological Institute, University of Pisa, Italy. Electronic address: mancusomichelangelo@gmail.com.
[Ti] Title:International Workshop:: Outcome measures and clinical trial readiness in primary mitochondrial myopathies in children and adults. Consensus recommendations. Rome, Italy, 16-18 November 2016.
[So] Source:Neuromuscul Disord;, 2017 Sep 08.
[Is] ISSN:1873-2364
[Cp] Country of publication:England
[La] Language:eng
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1710
[Cu] Class update date: 171027
[Lr] Last revision date:171027
[St] Status:Publisher

  6 / 3939 MEDLINE  
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[PMID]: 29054413
[Au] Autor:Mordel P; Schaeffer S; Dupas Q; Laville MA; Gérard M; Chapon F; Allouche S
[Ad] Address:Normandie Univ, UNICAEN, CHU Caen, Signalisation, électrophysiologie et imagerie des lésions d'ischémie-reperfusion myocardique, Caen, F-14032, France.
[Ti] Title:A 2 bp deletion in the mitochondrial ATP 6 gene responsible for the NARP (neuropathy, ataxia, and retinitis pigmentosa) syndrome.
[So] Source:Biochem Biophys Res Commun;494(1-2):133-137, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Mitochondrial (mt) DNA-associated NARP (neurogenic muscle weakness, ataxia, and retinitis pigmentosa) syndrome is due to mutation in the MT-ATP6 gene. We report the case of a 18-year-old man who presented with deafness, a myoclonic epilepsy, muscle weakness since the age of 10 and further developed a retinitis pigmentosa and ataxia. The whole mtDNA analysis by next-generation sequencing revealed the presence of the 2 bp microdeletion m.9127-9128 del AT in the ATP6 gene at 82% heteroplasmy in muscle and to a lower load in blood (10-20%) and fibroblasts (50%). Using the patient's fibroblasts, we demonstrated a 60% reduction of the oligomycin-sensitive ATPase hydrolytic activity, a 40% decrease in the ATP synthesis and determination of the mitochondrial membrane potential using the fluorescent probe tetramethylrhodamine, ethyl ester indicated a significant reduction in oligomycin sensitivity. In conclusion, we demonstrated that this novel AT deletion in the ATP6 gene is pathogenic and responsible for the NARP syndrome.
[Mh] MeSH terms primary: Mitochondrial Myopathies/enzymology
Mitochondrial Myopathies/genetics
Mitochondrial Proton-Translocating ATPases/genetics
Retinitis Pigmentosa/enzymology
Retinitis Pigmentosa/genetics
Sequence Deletion
[Mh] MeSH terms secundary: Adenosine Triphosphatases/genetics
Adenosine Triphosphatases/metabolism
Adenosine Triphosphate/metabolism
Base Sequence
Carrier Proteins/genetics
Carrier Proteins/metabolism
Cells, Cultured
DNA Mutational Analysis
DNA, Mitochondrial/genetics
High-Throughput Nucleotide Sequencing
Humans
Male
Membrane Potential, Mitochondrial/drug effects
Membrane Proteins/genetics
Membrane Proteins/metabolism
Mitochondrial Proton-Translocating ATPases/metabolism
Oligomycins/pharmacology
Syndrome
Young Adult
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE
[Nm] Name of substance:0 (Carrier Proteins); 0 (DNA, Mitochondrial); 0 (Membrane Proteins); 0 (Oligomycins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases); EC 3.6.3.14 (MT-ATP6 protein, human); EC 3.6.3.14 (oligomycin sensitivity-conferring protein)
[Em] Entry month:1711
[Cu] Class update date: 171113
[Lr] Last revision date:171113
[Js] Journal subset:IM
[Da] Date of entry for processing:171022
[St] Status:MEDLINE

  7 / 3939 MEDLINE  
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[PMID]: 29049993
[Au] Autor:Uenaka T; Kowa H; Ohtsuka Y; Seki T; Sekiguchi K; Kanda F; Toda T
[Ti] Title:Less Limb Muscle Involvement in Myositis Patients with Anti-Mitochondrial Antibodies.
[So] Source:Eur Neurol;78(5-6):290-295, 2017 Oct 19.
[Is] ISSN:1421-9913
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Recent studies have revealed the clinical, histological, and pathophysiological characteristics in a group of inflammatory myopathies with selected autoantibodies. We retrospectively compared the clinical manifestations and histological features between 8 anti-mitochondrial (anti-M2) antibody-positive and 33 antibody-negative patients. Patients with anti-M2 antibodies have been previously reported to have delayed diagnostic confirmation and frequent cardiopulmonary complications in comparison to those without the antibodies. In our study, clinical characteristics in patients with the antibodies were as follows: lesser degree of limb muscle weakness and atrophy as well as lymphocytic infiltration in muscle biopsy specimens, and frequent paravertebral muscle atrophy. Anti-M2 antibody appeared to be a biomarker related to not only cardiopulmonary complications, but also characteristic -distributions of affected muscles.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1710
[Cu] Class update date: 171019
[Lr] Last revision date:171019
[St] Status:Publisher
[do] DOI:10.1159/000481503

  8 / 3939 MEDLINE  
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[PMID]: 29016649
[Au] Autor:Ohn JH; Hwang JY; Moon MK; Ahn HY; Kim HH; Koo YD; Kim KI; Chang HJ; Lee HS; Jang HC; Park YJ
[Ad] Address:Department of Internal Medicine, Seoul National University Bundang Hospital, Seongnam, Republic of Korea.
[Ti] Title:Small heterodimer partner (SHP) deficiency protects myocardia from lipid accumulation in high fat diet-fed mice.
[So] Source:PLoS One;12(10):e0186021, 2017.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The small heterodimer partner (SHP) regulates fatty acid oxidation and lipogenesis in the liver by regulating peroxisome proliferator-activated receptor (PPAR) γ expression. SHP is also abundantly expressed in the myocardium. We investigated the effect of SHP expression on myocardia assessing not only heart structure and function but also lipid metabolism and related gene expression in a SHP deletion animal model. Transcriptional profiling with a microarray revealed that genes participating in cell growth, cytokine signalling, phospholipid metabolism, and extracellular matrix are up-regulated in the myocardia of SHP knockout (KO) mice compared to those of wild-type (WT) mice (nominal p value < 0.05). Consistent with these gene expression changes, the left ventricular masses of SHP KO mice were significantly higher than WT mice (76.8 ± 20.5 mg vs. 52.8 ± 6.8 mg, P = 0.0093). After 12 weeks of high fat diet (HFD), SHP KO mice gained less weight and exhibited less elevation in serum-free fatty acid and less ectopic lipid accumulation in the myocardium than WT mice. According to microarray analysis, genes regulated by PPARγ1 and PPARα were down-regulated in myocardia of SHP KO mice compared to their expression in WT mice after HFD, suggesting that the reduction in lipid accumulation in the myocardium resulted from a decrease in lipogenesis regulated by PPARγ. We confirmed the reduced expression of PPARγ1 and PPARα target genes such as CD36, medium-chain acyl-CoA dehydrogenase, long-chain acyl-CoA dehydrogenase, and very long-chain acyl-CoA dehydrogenase by SHP KO after HFD.
[Mh] MeSH terms primary: Lipogenesis/genetics
Myocardium/metabolism
Obesity/genetics
Receptors, Cytoplasmic and Nuclear/genetics
Transcriptome
[Mh] MeSH terms secundary: Acyl-CoA Dehydrogenase/genetics
Acyl-CoA Dehydrogenase/metabolism
Acyl-CoA Dehydrogenase, Long-Chain/deficiency
Acyl-CoA Dehydrogenase, Long-Chain/genetics
Acyl-CoA Dehydrogenase, Long-Chain/metabolism
Animals
CD36 Antigens/genetics
CD36 Antigens/metabolism
Cytokines/genetics
Cytokines/metabolism
Diet, High-Fat
Fatty Acids/metabolism
Gene Expression Profiling
Lipid Metabolism, Inborn Errors/genetics
Lipid Metabolism, Inborn Errors/metabolism
Liver/metabolism
Liver/pathology
Male
Mice
Mice, Knockout
Mitochondrial Diseases/genetics
Mitochondrial Diseases/metabolism
Muscular Diseases/genetics
Muscular Diseases/metabolism
Myocardium/pathology
Obesity/etiology
Obesity/metabolism
Obesity/pathology
Oligonucleotide Array Sequence Analysis
PPAR alpha/genetics
PPAR alpha/metabolism
PPAR gamma/genetics
PPAR gamma/metabolism
Protective Factors
Receptors, Cytoplasmic and Nuclear/deficiency
Signal Transduction
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (CD36 Antigens); 0 (Cytokines); 0 (Fatty Acids); 0 (PPAR alpha); 0 (PPAR gamma); 0 (Receptors, Cytoplasmic and Nuclear); 0 (nuclear receptor subfamily 0, group B, member 2); EC 1.3.8.7 (Acyl-CoA Dehydrogenase); EC 1.3.8.8 (Acyl-CoA Dehydrogenase, Long-Chain)
[Em] Entry month:1710
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186021

  9 / 3939 MEDLINE  
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[PMID]: 28969510
[Au] Autor:Zhou Y; Yi J; Liu L; Wang X; Dong L; Du A
[Ad] Address:a Department of Cardiology , Second Affiliated Hospital, Zhejiang University School of Medicine , Hangzhou , China.
[Ti] Title:Acute mitochondrial myopathy with respiratory insufficiency and motor axonal polyneuropathy.
[So] Source:Int J Neurosci;:1-6, 2017 Oct 16.
[Is] ISSN:1563-5279
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Mitochondrial myopathies (MMs) are mainly presented with chronic muscle weakness and accompanied with other syndromes. MM with acute respiratory insufficiency is rare. AIMS: To reveal the clinical, pathological and molecular characteristics of a life-threatening MM. METHODS: Muscle biopsy and enzyme staining were performed in skeletal muscles. Mitochondrial DNA (mtDNA) sequencing was analyzed and heteroplasmy were quantified by pyrosequencing. RESULTS: All three patients had tachycardia, acute lactic acidosis, dyspnea and sudden severe muscle weakness. Two patients had calf edema and abdominal pain, and one had a heart attack. Electromyography in two patients showed dramatically decreased axonal amplitudes of motor nerves. Muscle biopsies showed ragged red fibers and dramatic mitochondrial abnormality. A mtDNA m.3243A>G mutation was identified in Patient 1 (mutation load: 29% in blood and 73% in muscle) and Patient 3 (79% in blood and 89% in muscle). A mtDNA m.8344A>G mutation was found in Patient 2 (mutation load 80.4% in blood). CONCLUSION: MM characterized by lactic acidosis, respiratory failure and acute motor axonal neuropathy is life threatening.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1710
[Cu] Class update date: 171017
[Lr] Last revision date:171017
[St] Status:Publisher
[do] DOI:10.1080/00207454.2017.1387113

  10 / 3939 MEDLINE  
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[PMID]: 28947214
[Au] Autor:Dallabona C; Baruffini E; Goffrini P; Lodi T
[Ad] Address:Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
[Ti] Title:Dominance of yeast aac2 and aac2 mutations, equivalent to pathological mutations in ant1, is due to gain of function.
[So] Source:Biochem Biophys Res Commun;493(2):909-913, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The mitochondrial ADP/ATP carrier is a nuclear encoded protein, which catalyzes the exchange of ATP generated in mitochondria with ADP produced in the cytosol. In humans, mutations in the major ADP/ATP carrier gene, ANT1, are involved in several degenerative mitochondrial pathologies, leading to instability of mitochondrial DNA. Recessive mutations have been associated with mitochondrial myopathy and cardiomyopathy whereas dominant mutations have been associated with autosomal dominant Progressive External Ophtalmoplegia (adPEO). Recently, two de novo dominant mutations, R80H and R235G, leading to extremely severe symptoms, have been identified. In order to evaluate if the dominance is due to haploinsufficiency or to a gain of function, the two mutations have been introduced in the equivalent positions of the AAC2 gene, the yeast orthologue of human ANT1, and their dominant effect has been studied in heteroallelic strains, containing both one copy of wild type AAC2 and one copy of mutant aac2 allele. Through phenotypic characterization of these yeast models we showed that the OXPHOS phenotypes in the heteroallelic strains were more affected than in the hemiallelic strain indicating that the dominant trait of the two mutations is due to gain of function.
[Mh] MeSH terms primary: Adenine Nucleotide Translocator 1/genetics
DNA, Mitochondrial/genetics
Mitochondrial ADP, ATP Translocases/genetics
Mitochondrial Myopathies/genetics
Point Mutation
Saccharomyces cerevisiae Proteins/genetics
Saccharomyces cerevisiae/genetics
[Mh] MeSH terms secundary: Alleles
Humans
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Adenine Nucleotide Translocator 1); 0 (DNA, Mitochondrial); 0 (PET9 protein, S cerevisiae); 0 (SLC25A4 protein, human); 0 (Saccharomyces cerevisiae Proteins); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Entry month:1710
[Cu] Class update date: 171020
[Lr] Last revision date:171020
[Js] Journal subset:IM
[Da] Date of entry for processing:170927
[St] Status:MEDLINE


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