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[PMID]: 29451896
[Au] Autor:Ji H; Li D; Wu Y; Zhang Q; Gu Q; Xie H; Ji T; Wang H; Zhao L; Zhao H; Yang Y; Feng H; Xiong H; Ji J; Yang Z; Kou L; Li M; Bao X; Chang X; Zhang Y; Li L; Li H; Niu Z; Wu X; Xiao J; Jiang Y; Wang J
[Ad] Address:Department of Pediatrics, Peking University First Hospital, Beijing, China.
[Ti] Title:Hypomyelinating disorders in China: The clinical and genetic heterogeneity in 119 patients.
[So] Source:PLoS One;13(2):e0188869, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:OBJECTIVE: Hypomyelinating disorders are a group of clinically and genetically heterogeneous diseases characterized by neurological deterioration with hypomyelination visible on brain MRI scans. This study was aimed to clarify the clinical and genetic features of HMDs in Chinese population. METHODS: 119 patients with hypomyelinating disorders in Chinese population were enrolled and evaluated based on their history, clinical manifestation, laboratory examinations, series of brain MRI with follow-up, genetic etiological tests including chromosomal analysis, multiplex ligation probe amplification, Sanger sequencing, targeted enrichment-based next-generation sequencing and whole exome sequencing. RESULTS: Clinical and genetic features of hypomyelinating disorders were revealed. Nine different hypomyelinating disorders were identified in 119 patients: Pelizaeus-Merzbacher disease (94, 79%), Pelizaeus-Merzbacher-like disease (10, 8%), hypomyelination with atrophy of the basal ganglia and cerebellum (3, 3%), GM1 gangliosidosis (5, 4%), GM2 gangliosidosis (3, 3%), trichothiodystrophy (1, 1%), Pol III-related leukodystrophy (1, 1%), hypomyelinating leukodystrophy type 9 (1, 1%), and chromosome 18q deletion syndrome (1, 1%). Of the sample, 94% (112/119) of the patients were genetically diagnosed, including 111 with mutations distributing across 9 genes including PLP1, GJC2, TUBB4A, GLB1, HEXA, HEXB, ERCC2, POLR3A, and RARS and 1 with mosaic chromosomal change of 46, XX,del(18)(q21.3)/46,XX,r(18)(p11.32q21.3)/45,XX,-18. Eighteen novel mutations were discovered. Mutations in POLR3A and RARS were first identified in Chinese patients with Pol III-related leukodystrophy and hypomyelinating leukodystrophy, respectively. SIGNIFICANCE: This is the first report on clinical and genetic features of hypomyelinating disorders with a large sample of patients in Chinese population, identifying 18 novel mutations especially mutations in POLR3A and RARS in Chinese patients, expanding clinical and genetic spectrums of hypomyelinating disorders.
[Mh] MeSH terms primary: Genetic Heterogeneity
Hereditary Central Nervous System Demyelinating Diseases/epidemiology
[Mh] MeSH terms secundary: China/epidemiology
Chromosome Banding
Female
Hereditary Central Nervous System Demyelinating Diseases/diagnostic imaging
Hereditary Central Nervous System Demyelinating Diseases/genetics
Hereditary Central Nervous System Demyelinating Diseases/pathology
Humans
Infant
Infant, Newborn
Karyotyping
Magnetic Resonance Imaging
Male
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:180217
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188869

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[PMID]: 28931644
[Au] Autor:Hamilton EMC; Bertini E; Kalaydjieva L; Morar B; Dojcáková D; Liu J; Vanderver A; Curiel J; Persoon CM; Diodato D; Pinelli L; van der Meij NL; Plecko B; Blaser S; Wolf NI; Waisfisz Q; Abbink TEM; van der Knaap MS; Recessive H-ABC Research Group
[Ad] Address:From the Department of Child Neurology (E.M.C.H., N.I.W., T.E.M.A., M.S.v.d.K.), Amsterdam Neuroscience (E.M.C.H., N.I.W., T.E.M.A., M.S.v.d.K.), Department of Clinical Genetics (C.M.P., Q.W.), Department of Functional Genomics, Center for Neurogenomics and Cognitive Research (M.S.v.d.K.), VU Univer
[Ti] Title: founder mutation in the Roma population causes recessive variant of H-ABC.
[So] Source:Neurology;89(17):1821-1828, 2017 Oct 24.
[Is] ISSN:1526-632X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:OBJECTIVE: To identify the gene defect in patients with hypomyelination with atrophy of the basal ganglia and cerebellum (H-ABC) who are negative for mutations. METHODS: We performed homozygosity mapping and whole exome sequencing (WES) to detect the disease-causing variant. We used a Taqman assay for population screening. We developed a luciferase reporter construct to investigate the effect of the promoter mutation on expression. RESULTS: Sixteen patients from 14 families from different countries fulfilling the MRI criteria for H-ABC exhibited a similar, severe clinical phenotype, including lack of development and a severe epileptic encephalopathy. The majority of patients had a known Roma ethnic background. Single nucleotide polymorphism array analysis in 5 patients identified one large overlapping homozygous region on chromosome 13. WES in 2 patients revealed a homozygous deletion in the promoter region of . Sanger sequencing confirmed homozygosity for this variant in all 16 patients. All patients shared a common haplotype, indicative of a founder effect. Screening of 1,000 controls from different European Roma panels demonstrated an overall carrier rate of the mutation of 3%-25%. Transfection assays showed that the deletion significantly reduced expression in specific CNS cell lines. CONCLUSIONS: encodes ubiquitin-fold modifier 1 (UFM1), a member of the ubiquitin-like family involved in posttranslational modification of proteins. Its exact biological role is unclear. This study associates a gene defect with a disease and sheds new light on possible UFM1 functional networks.
[Mh] MeSH terms primary: Amino Acid Transport Systems, Acidic/deficiency
Antiporters/deficiency
Basal Ganglia/pathology
Cerebellum/pathology
Hereditary Central Nervous System Demyelinating Diseases/genetics
Mitochondrial Diseases/genetics
Polymorphism, Single Nucleotide/genetics
Proteins/genetics
Psychomotor Disorders/genetics
[Mh] MeSH terms secundary: Adolescent
Adult
Amino Acid Transport Systems, Acidic/genetics
Antiporters/genetics
Atrophy/etiology
Basal Ganglia/diagnostic imaging
Cell Line, Tumor/pathology
Cerebellum/diagnostic imaging
Child
Child, Preschool
DNA Mutational Analysis
Family Health
Female
HeLa Cells
Hereditary Central Nervous System Demyelinating Diseases/complications
Hereditary Central Nervous System Demyelinating Diseases/diagnostic imaging
Humans
Image Processing, Computer-Assisted
Italy
Magnetic Resonance Imaging
Male
Mitochondrial Diseases/complications
Mitochondrial Diseases/diagnostic imaging
Psychomotor Disorders/complications
Psychomotor Disorders/diagnostic imaging
Transfection
Tubulin/genetics
Young Adult
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Amino Acid Transport Systems, Acidic); 0 (Antiporters); 0 (Proteins); 0 (TUBB4A protein, human); 0 (Tubulin); 0 (UFM1 protein, human)
[Em] Entry month:1711
[Cu] Class update date: 171105
[Lr] Last revision date:171105
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:170922
[St] Status:MEDLINE
[do] DOI:10.1212/WNL.0000000000004578

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[PMID]: 28575651
[Au] Autor:Chelban V; Patel N; Vandrovcova J; Zanetti MN; Lynch DS; Ryten M; Botía JA; Bello O; Tribollet E; Efthymiou S; Davagnanam I; Bashiri FA; Wood NW; Rothman JE; Alkuraya FS; Houlden H; SYNAPSE Study Group
[Ad] Address:Department of Molecular Neuroscience, University College London, London WC1N 3BG, UK; Department of Neurology and Neurosurgery, Institute of Emergency Medicine, Toma Ciorba 1, 2052 Chisinau, Republic of Moldova. Electronic address: v.chelban@ucl.ac.uk.
[Ti] Title:Mutations in NKX6-2 Cause Progressive Spastic Ataxia and Hypomyelination.
[So] Source:Am J Hum Genet;100(6):969-977, 2017 Jun 01.
[Is] ISSN:1537-6605
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Progressive limb spasticity and cerebellar ataxia are frequently found together in clinical practice and form a heterogeneous group of degenerative disorders that are classified either as pure spastic ataxia or as complex spastic ataxia with additional neurological signs. Inheritance is either autosomal dominant or autosomal recessive. Hypomyelinating features on MRI are sometimes seen with spastic ataxia, but this is usually mild in adults and severe and life limiting in children. We report seven individuals with an early-onset spastic-ataxia phenotype. The individuals come from three families of different ethnic backgrounds. Affected members of two families had childhood onset disease with very slow progression. They are still alive in their 30s and 40s and show predominant ataxia and cerebellar atrophy features on imaging. Affected members of the third family had a similar but earlier-onset presentation associated with brain hypomyelination. Using a combination of homozygozity mapping and exome sequencing, we mapped this phenotype to deleterious nonsense or homeobox domain missense mutations in NKX6-2. NKX6-2 encodes a transcriptional repressor with early high general and late focused CNS expression. Deficiency of its mouse ortholog results in widespread hypomyelination in the brain and optic nerve, as well as in poor motor coordination in a pattern consistent with the observed human phenotype. In-silico analysis of human brain expression and network data provides evidence that NKX6-2 is involved in oligodendrocyte maturation and might act within the same pathways of genes already associated with central hypomyelination. Our results support a non-redundant developmental role of NKX6-2 in humans and imply that NKX6-2 mutations should be considered in the differential diagnosis of spastic ataxia and hypomyelination.
[Mh] MeSH terms primary: Amino Acid Transport Systems, Acidic/deficiency
Antiporters/deficiency
Hereditary Central Nervous System Demyelinating Diseases/complications
Hereditary Central Nervous System Demyelinating Diseases/genetics
Homeodomain Proteins/genetics
Intellectual Disability/complications
Intellectual Disability/genetics
Mitochondrial Diseases/complications
Mitochondrial Diseases/genetics
Muscle Spasticity/complications
Muscle Spasticity/genetics
Mutation/genetics
Optic Atrophy/complications
Optic Atrophy/genetics
Psychomotor Disorders/complications
Psychomotor Disorders/genetics
Spinocerebellar Ataxias/complications
Spinocerebellar Ataxias/genetics
[Mh] MeSH terms secundary: Adult
Amino Acid Sequence
Amino Acid Transport Systems, Acidic/genetics
Antiporters/genetics
Brain/embryology
Brain/metabolism
Child
Female
Gene Regulatory Networks
Homeodomain Proteins/chemistry
Humans
Infant
Male
Pedigree
Phenotype
Young Adult
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Amino Acid Transport Systems, Acidic); 0 (Antiporters); 0 (Homeodomain Proteins); 0 (NKX6-2 protein, human)
[Em] Entry month:1707
[Cu] Class update date: 170906
[Lr] Last revision date:170906
[Js] Journal subset:IM
[Da] Date of entry for processing:170603
[St] Status:MEDLINE

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[PMID]: 28429368
[Au] Autor:Juaristi I; García-Martín ML; Rodrigues TB; Satrústegui J; Llorente-Folch I; Pardo B
[Ad] Address:Departamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid-Consejo Superior de Investigaciones Científicas, Madrid, Spain.
[Ti] Title:ARALAR/AGC1 deficiency, a neurodevelopmental disorder with severe impairment of neuronal mitochondrial respiration, does not produce a primary increase in brain lactate.
[So] Source:J Neurochem;142(1):132-139, 2017 Jul.
[Is] ISSN:1471-4159
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:ARALAR/AGC1 (aspartate-glutamate mitochondrial carrier 1) is an important component of the NADH malate-aspartate shuttle (MAS). AGC1-deficiency is a rare disease causing global cerebral hypomyelination, developmental arrest, hypotonia, and epilepsy (OMIM ID #612949); the aralar-KO mouse recapitulates the major findings in humans. This study was aimed at understanding the impact of ARALAR-deficiency in brain lactate levels as a biomarker. We report that lactate was equally abundant in wild-type and aralar-KO mouse brain in vivo at postnatal day 17. We find that lactate production upon mitochondrial blockade depends on up-regulation of lactate formation in astrocytes rather than in neurons. However, ARALAR-deficiency decreased cell respiration in neurons, not astrocytes, which maintained unchanged respiration and lactate production. As the primary site of ARALAR-deficiency is neuronal, this explains the lack of accumulation of brain lactate in ARALAR-deficiency in humans and mice. On the other hand, we find that the cytosolic and mitochondrial components of the glycerol phosphate shuttle are present in astrocytes with similar activities. This suggests that glycerol phosphate shuttle is the main NADH shuttle in astrocytes and explains the absence of effects of ARALAR-deficiency in these cells.
[Mh] MeSH terms primary: Aggrecans/genetics
Aggrecans/metabolism
Amino Acid Transport Systems, Acidic/deficiency
Antiporters/deficiency
Hereditary Central Nervous System Demyelinating Diseases/genetics
Lactic Acid/metabolism
Mitochondria/genetics
Mitochondria/metabolism
Mitochondrial Diseases/genetics
Nervous System Diseases/genetics
Nervous System Diseases/metabolism
Neurons/metabolism
Psychomotor Disorders/genetics
[Mh] MeSH terms secundary: Amino Acid Transport Systems, Acidic/genetics
Animals
Antiporters/genetics
Astrocytes/metabolism
Brain Chemistry/genetics
Glucose/metabolism
Glucosephosphate Dehydrogenase/genetics
Glucosephosphate Dehydrogenase/metabolism
Mice
Mice, Inbred C57BL
Mice, Knockout
Oxygen Consumption/genetics
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Agc1 protein, mouse); 0 (Aggrecans); 0 (Amino Acid Transport Systems, Acidic); 0 (Antiporters); 33X04XA5AT (Lactic Acid); EC 1.1.1.49 (Glucosephosphate Dehydrogenase); IY9XDZ35W2 (Glucose)
[Em] Entry month:1708
[Cu] Class update date: 170814
[Lr] Last revision date:170814
[Js] Journal subset:IM
[Da] Date of entry for processing:170422
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.14047

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[PMID]: 28407788
[Au] Autor:Choquet K; Yang S; Moir RD; Forget D; Larivière R; Bouchard A; Poitras C; Sgarioto N; Dicaire MJ; Noohi F; Kennedy TE; Rochford J; Bernard G; Teichmann M; Coulombe B; Willis IM; Kleinman CL; Brais B
[Ad] Address:Montreal Neurological Institute, McGill University, 3801 University Street, room 622, Montréal, Québec, H3A 2B4, Canada.
[Ti] Title:Absence of neurological abnormalities in mice homozygous for the Polr3a G672E hypomyelinating leukodystrophy mutation.
[So] Source:Mol Brain;10(1):13, 2017 04 13.
[Is] ISSN:1756-6606
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Recessive mutations in the ubiquitously expressed POLR3A gene cause one of the most frequent forms of childhood-onset hypomyelinating leukodystrophy (HLD): POLR3-HLD. POLR3A encodes the largest subunit of RNA Polymerase III (Pol III), which is responsible for the transcription of transfer RNAs (tRNAs) and a large array of other small non-coding RNAs. In order to study the central nervous system pathophysiology of the disease, we introduced the French Canadian founder Polr3a mutation c.2015G > A (p.G672E) in mice, generating homozygous knock-in (KI/KI) as well as compound heterozygous mice for one Polr3a KI and one null allele (KI/KO). Both KI/KI and KI/KO mice are viable and are able to reproduce. To establish if they manifest a motor phenotype, WT, KI/KI and KI/KO mice were submitted to a battery of behavioral tests over one year. The KI/KI and KI/KO mice have overall normal balance, muscle strength and general locomotion. Cerebral and cerebellar Luxol Fast Blue staining and measurement of levels of myelin proteins showed no significant differences between the three groups, suggesting that myelination is not overtly impaired in Polr3a KI/KI and KI/KO mice. Finally, expression levels of several Pol III transcripts in the brain showed no statistically significant differences. We conclude that the first transgenic mice with a leukodystrophy-causing Polr3a mutation do not recapitulate the childhood-onset HLD observed in the majority of human patients with POLR3A mutations, and provide essential information to guide selection of Polr3a mutations for developing future mouse models of the disease.
[Mh] MeSH terms primary: Hereditary Central Nervous System Demyelinating Diseases/genetics
Mutation/genetics
Myelin Sheath/metabolism
RNA Polymerase III/genetics
[Mh] MeSH terms secundary: Animals
Cerebellum/pathology
Cerebellum/physiopathology
Gene Knock-In Techniques
Hereditary Central Nervous System Demyelinating Diseases/physiopathology
Homozygote
Humans
Mice, Inbred C57BL
Mice, Knockout
Motor Activity
Purkinje Cells/metabolism
Purkinje Cells/pathology
RNA Polymerase III/metabolism
Transcription, Genetic
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:EC 2.7.7.6 (RNA Polymerase III)
[Em] Entry month:1710
[Cu] Class update date: 171106
[Lr] Last revision date:171106
[Js] Journal subset:IM
[Da] Date of entry for processing:170415
[St] Status:MEDLINE
[do] DOI:10.1186/s13041-017-0294-y

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[PMID]: 28378817
[Au] Autor:O'Brien A; Marshall CR; Blaser S; Ray PN; Yoon G
[Ad] Address:Department of Paediatrics, Division of Clinical and Metabolic Genetics, The Hospital for Sick Children, Toronto, Ontario, Canada.
[Ti] Title:Severe neurodegeneration, progressive cerebral volume loss and diffuse hypomyelination associated with a homozygous frameshift mutation in CSTB.
[So] Source:Eur J Hum Genet;25(6):775-778, 2017 Jun.
[Is] ISSN:1476-5438
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Mutations of the cystatin B gene (CSTB; OMIM 601145) are known to cause Unverricht-Lundborg disease or progressive myoclonic epilepsy-1A (EPM1A, MIM #254800). Most patients are homozygous for an expanded (>30) dodecamer repeat in the promoter region of CSTB, or are compound heterozygotes for the dodecamer repeat and a point mutation. We report two adolescent sisters born to consanguineous parents of Sri Lankan descent who presented with profound global developmental delay, microcephaly, cortical blindness and axial hypotonia with appendicular hypertonia. Neither sibling ever developed head control, independent sitting or ambulation, and never developed speech. The elder sister had a seizure disorder. Both sisters had profound microcephaly and distinct facial features. On serial brain imaging, they had progressive atrophy of the corpus callosum and supratentorial brain, and diffuse hypomyelination with progressive loss of myelin signal. Exome sequencing revealed both siblings to be homozygous for a c.218dupT (p.His75Serfs*2) mutation in exon 3 of CSTB. The neuroimaging features of our patients are consistent with those observed in Cstb-knockout mice, which supports the hypothesis that disease severity is inversely correlated with the amount of residual functional cystatin B protein.
[Mh] MeSH terms primary: Blindness, Cortical/genetics
Cystatin B/genetics
Developmental Disabilities/genetics
Frameshift Mutation
Hereditary Central Nervous System Demyelinating Diseases/genetics
Microcephaly/genetics
[Mh] MeSH terms secundary: Adolescent
Blindness, Cortical/diagnosis
Child
Corpus Callosum/diagnostic imaging
Corpus Callosum/pathology
Developmental Disabilities/diagnosis
Female
Hereditary Central Nervous System Demyelinating Diseases/diagnosis
Homozygote
Humans
Male
Microcephaly/diagnosis
Myelin Sheath/pathology
Pedigree
Syndrome
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE
[Nm] Name of substance:0 (CSTB protein, human); 88844-95-5 (Cystatin B)
[Em] Entry month:1709
[Cu] Class update date: 170912
[Lr] Last revision date:170912
[Js] Journal subset:IM
[Da] Date of entry for processing:170406
[St] Status:MEDLINE
[do] DOI:10.1038/ejhg.2017.39

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[PMID]: 28092989
[Au] Autor:Pilch KS; Spaeth PJ; Yuki N; Wakerley BR
[Ad] Address:a Department of Cell and Developmental Biology , University College London , UK.
[Ti] Title:Therapeutic complement inhibition: a promising approach for treatment of neuroimmunological diseases.
[So] Source:Expert Rev Neurother;17(6):579-591, 2017 Jun.
[Is] ISSN:1744-8360
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:INTRODUCTION: Autoimmunity is an important cause of disease both in the central and peripheral nervous systems. Aetiologies and clinical manifestations are complex and heterogeneous. Inappropriate control of complement activation at inappropriate sites has been recognized as a major determinant in several neurological conditions, including Guillain-Barré syndrome and neuromyelitis optica. In each case pathogenesis is thought to be associated with generation of autoantibodies which upon binding guide activation of the complement system to self-tissue. Areas covered: Modulation of the complement system activation at such sites may represent a novel therapeutic approach for treatment of immune-mediated inflammatory conditions. In this review we focus on the therapeutic effects of complement inhibitors in Guillain-Barré syndrome and neuromyelitis optica and highlight recent developments within the field. Expert Commentary: Conventional first line treatment strategies in GBS and NMO have the potential disadvantage of causing widespread immunosuppressive effects. A more targeted approach may therefore be more effective and less disruptive to the immune system, especially in the case of NMO, which requires long term immunosuppression. Modulation of the complement system may hold the key and has already been shown to be of clinical benefit in other non-neurological conditions, including paroxysmal nocturnal hemoglobinuria and hereditary angioedema.
[Mh] MeSH terms primary: Complement Activation/drug effects
Guillain-Barre Syndrome/immunology
Guillain-Barre Syndrome/therapy
Immunomodulation
Neuromyelitis Optica/immunology
Neuromyelitis Optica/therapy
[Mh] MeSH terms secundary: Autoantibodies
Autoimmunity
Humans
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Autoantibodies)
[Em] Entry month:1707
[Cu] Class update date: 171031
[Lr] Last revision date:171031
[Js] Journal subset:IM
[Da] Date of entry for processing:170118
[St] Status:MEDLINE
[do] DOI:10.1080/14737175.2017.1282821

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[PMID]: 28007994
[Au] Autor:Peeters K; Chamova T; Tournev I; Jordanova A
[Ad] Address:Molecular Neurogenomics Group, Department of Molecular Genetics, VIB and University of Antwerp, Antwerpen 2610, Belgium.
[Ti] Title:Axonal neuropathy with neuromyotonia: there is a HINT.
[So] Source:Brain;140(4):868-877, 2017 Apr 01.
[Is] ISSN:1460-2156
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Recessive mutations in the gene encoding the histidine triad nucleotide binding protein 1 (HINT1) were recently shown to cause a motor-predominant Charcot-Marie-Tooth neuropathy. About 80% of the patients exhibit neuromyotonia, a striking clinical and electrophysiological hallmark that can help to distinguish this disease and to guide diagnostic screening. HINT1 neuropathy has worldwide distribution and is particularly prevalent in populations inhabiting central and south-eastern Europe. With 12 different mutations identified in more than 60 families, it ranks among the most common subtypes of axonal Charcot-Marie-Tooth neuropathy. This article provides an overview of the present knowledge on HINT1 neuropathy with the aim to increase awareness and spur interest among clinicians and researchers in the field. We propose diagnostic guidelines to recognize and differentiate this entity and suggest treatment strategies to manage common symptoms. As a recent player in the field of hereditary neuropathies, the role of HINT1 in peripheral nerves is unknown and the underlying disease mechanisms are unexplored. We provide a comprehensive overview of the structural and functional characteristics of the HINT1 protein that may guide further studies into the molecular aetiology and treatment strategies of this peculiar Charcot-Marie-Tooth subtype.
[Mh] MeSH terms primary: Charcot-Marie-Tooth Disease/genetics
Hereditary Sensory and Motor Neuropathy/genetics
Isaacs Syndrome/genetics
Myotonia/genetics
Nerve Tissue Proteins/genetics
Peripheral Nervous System Diseases/genetics
[Mh] MeSH terms secundary: Charcot-Marie-Tooth Disease/epidemiology
Charcot-Marie-Tooth Disease/pathology
Hereditary Sensory and Motor Neuropathy/epidemiology
Hereditary Sensory and Motor Neuropathy/pathology
Humans
Isaacs Syndrome/epidemiology
Isaacs Syndrome/pathology
Myotonia/epidemiology
Myotonia/pathology
Peripheral Nervous System Diseases/epidemiology
Peripheral Nervous System Diseases/pathology
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (HINT1 protein, human); 0 (Nerve Tissue Proteins)
[Em] Entry month:1704
[Cu] Class update date: 170425
[Lr] Last revision date:170425
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:161224
[St] Status:MEDLINE
[do] DOI:10.1093/brain/aww301

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[PMID]: 28000699
[Au] Autor:Vasilescu C; Isohanni P; Palomäki M; Pihko H; Suomalainen A; Carroll CJ
[Ad] Address:Research Programs Unit, Molecular Neurology, Biomedicum-Helsinki, University of Helsinki, Helsinki, Finland.
[Ti] Title:Absence of Hikeshi, a nuclear transporter for heat-shock protein HSP70, causes infantile hypomyelinating leukoencephalopathy.
[So] Source:Eur J Hum Genet;25(3):366-370, 2017 Feb.
[Is] ISSN:1476-5438
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Genetic leukoencephalopathies are a heterogeneous group of central nervous system disorders with white matter involvement. In a Finnish patient, we identified a novel homozygous disease-causing variant in HIKESHI, c.11G>C, p.(Cys4Ser), leading to hypomyelinating leukoencephalopathy with periventricular cysts and vermian atrophy. A founder Ashkenazi-Jewish disease-causing variant recently linked Hikeshi and its heat-shock protective function to leukoencephalopathy. In our patient, clinical features of lower limb spasticity, optic atrophy, nystagmus, and severe developmental delay were similar to reported patients. Additional features included vermian atrophy, epileptic seizures, and an ovarian tumor. Structural modeling and protein analyses revealed that modified interactions inside Hikeshi's hydrophobic pockets induce protein instability. The patient's cells showed impaired nuclear translocation of HSP70 during heat shock, and decreased ERO1-Lα, an endoplasmic reticulum (ER) oxidoreductase. Overall, we show that: (1) the clinical spectrum associated with Hikeshi deficiency extends to leukoencephalopathy with vermian atrophy and epilepsy; (2) the cellular disease process involves both nuclear chaperone and ER functions.
[Mh] MeSH terms primary: Carrier Proteins/genetics
Hereditary Central Nervous System Demyelinating Diseases/genetics
[Mh] MeSH terms secundary: Active Transport, Cell Nucleus
Carrier Proteins/chemistry
Cell Nucleus
Cells, Cultured
HSP70 Heat-Shock Proteins/metabolism
Hereditary Central Nervous System Demyelinating Diseases/diagnosis
Humans
Infant
Membrane Glycoproteins/metabolism
Oxidoreductases/metabolism
Protein Stability
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE
[Nm] Name of substance:0 (Carrier Proteins); 0 (HSP70 Heat-Shock Proteins); 0 (Membrane Glycoproteins); 0 (hikeshi protein, human); EC 1.- (ERO1L protein, human); EC 1.- (Oxidoreductases)
[Em] Entry month:1708
[Cu] Class update date: 170807
[Lr] Last revision date:170807
[Js] Journal subset:IM
[Da] Date of entry for processing:161222
[St] Status:MEDLINE
[do] DOI:10.1038/ejhg.2016.189

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[PMID]: 27863451
[Au] Autor:Lee M; Park CH; Chung HK; Kim HJ; Choi Y; Yoo JH; Yoon YC; Hong YB; Chung KW; Choi BO; Lee HW
[Ad] Address:Department of Neurology, Ewha Womans University School of Medicine and Ewha Medical Research Institute, Seoul, South Korea.
[Ti] Title:Cerebral white matter abnormalities in patients with charcot-marie-tooth disease.
[So] Source:Ann Neurol;81(1):147-151, 2017 Jan.
[Is] ISSN:1531-8249
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Here, we report the structural evidence of cerebral white matter abnormalities in Charcot-Marie-Tooth (CMT) patients and the relationship between these abnormalities and clinical disability. Brain diffusion tensor imaging (DTI) was performed in CMT patients with demyelinating (CMT1A/CMT1E), axonal (CMT2A/CMT2E), or intermediate (CMTX1/DI-CMT) peripheral neuropathy. Although all patients had normal brain magnetic resonance imaging, all genetic subgroups except CMT1A had abnormal DTI findings indicative of significant cerebral white matter abnormalities: decreased fractional anisotropy and axial diffusivity, and increased radial diffusivity. DTI abnormalities were correlated with clinical disability, suggesting that there is comorbidity of central nervous system damage with peripheral neuropathy in CMT patients. ANN NEUROL 2017;81:147-151.
[Mh] MeSH terms primary: Charcot-Marie-Tooth Disease/pathology
Peripheral Nervous System Diseases/pathology
White Matter/pathology
[Mh] MeSH terms secundary: Anisotropy
Case-Control Studies
Charcot-Marie-Tooth Disease/genetics
Diffusion Tensor Imaging
Disability Evaluation
Female
Humans
Male
Mutation
Neuroimaging
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1706
[Cu] Class update date: 170725
[Lr] Last revision date:170725
[Js] Journal subset:IM
[Da] Date of entry for processing:161119
[St] Status:MEDLINE
[do] DOI:10.1002/ana.24824


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