Tatsushi Toda

Kobe University, Kōbe, Hyōgo, Japan

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Publications (214)1154.59 Total impact

  • International journal of cardiology 08/2015; 192. DOI:10.1016/j.ijcard.2015.05.004 · 6.18 Impact Factor
  • Clinical Neurophysiology 06/2015; 126(6). DOI:10.1016/j.clinph.2015.02.030 · 2.98 Impact Factor
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    ABSTRACT: Glucocerebrosidase gene (GBA) variants that cause Gaucher disease are associated with Parkinson disease (PD) and dementia with Lewy bodies (DLB). To investigate the role of GBA variants in multiple system atrophy (MSA), we analyzed GBA variants in a large case-control series. We sequenced coding regions and flanking splice sites of GBA in 969 MSA patients (574 Japanese, 223 European, and 172 North American) and 1509 control subjects (900 Japanese, 315 European, and 294 North American). We focused solely on Gaucher-disease-causing GBA variants. In the Japanese series, we found nine carriers among the MSA patients (1.65%) and eight carriers among the control subjects (0.89%). In the European series, we found three carriers among the MSA patients (1.35%) and two carriers among the control subjects (0.63%). In the North American series, we found five carriers among the MSA patients (2.91%) and one carrier among the control subjects (0.34%). Subjecting each series to a Mantel-Haenszel analysis yielded a pooled odds ratio (OR) of 2.44 (95% confidence interval [CI], 1.14-5.21) and a P-value of 0.029 without evidence of significant heterogeneity. Logistic regression analysis yielded similar results, with an adjusted OR of 2.43 (95% CI 1.15-5.37) and a P-value of 0.022. Subtype analysis showed that Gaucher-disease-causing GBA variants are significantly associated with MSA cerebellar subtype (MSA-C) patients (P = 7.3 × 10(-3)). The findings indicate that, as in PD and DLB, Gaucher-disease-causing GBA variants are associated with MSA.
    04/2015; 2(4):417-26. DOI:10.1002/acn3.185
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    ABSTRACT: Fukuyama congenital muscular dystrophy (FCMD) is a congenital muscular dystrophy rarely reported outside Japan. Here, we report three patients with Fukuyama congenital muscular dystrophy (FCMD) in China who shared a similar clinical phenotype and 3-kb insertion in the FKTN 3' untranslated region. Immunofluorescence staining was undertaken on muscle biopsies from three patients using alpha dystroglycan antibody (IIH6). Genomic DNA from patients and parents was extracted from peripheral blood leukocytes. Polymerase chain reaction and DNA sequencing were employed to analyze the exons and surrounding intron sequences of the fukutin (FKTN) gene to detect mutations. Haplotype analysis was also performed on each patient and their parents. All patients had delayed mental and motor development, febrile convulsions, muscle weakness, and moderate to significant raised levels of serum creatine kinase (7000-11,160U/L, 25-60×normal). Brain MRI scans showed micropolygyria and extensive dysplasia in the white matter and brainstem. Electromyography revealed myopathic changes. Muscle immunofluorescence studies demonstrated reduced IIH6 staining. Genetic testing showed compound heterozygous mutations of FKTN. Cases 1 and 2 had a c.139C>T (p.Arg47(∗)) heterozygous mutation. Case 3 had a c.346C>T (p.Gln116(∗)) heterozygous mutation. All patients had a heterozygous 3-kb insertion in the FKTN 3' untranslated region. Haplotype analyses suggested that these patients had the same haplotype as Japanese patients. Copyright © 2015 The Japanese Society of Child Neurology. Published by Elsevier B.V. All rights reserved.
    Brain & development 03/2015; DOI:10.1016/j.braindev.2015.02.010 · 1.54 Impact Factor
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    ABSTRACT: Uric acid (urate) has been suggested to play a protective role in Parkinson's disease onset through its antioxidant activity. Dysfunction of ABCG2, a high-capacity urate exporter, is a major cause for early-onset gout based on hyperuricemia. In this study, the effects of a dysfunctional ABCG2 variant (Q141K, rs2231142) were analyzed on the ages at onset of gout patients (N = 507) and Parkinson's disease patients (N = 1015). The Q141K variant hastened the gout onset (P = 0.0027), but significantly associated with later Parkinson's disease onset (P = 0.025). Our findings will be helpful for development of more effective prevention of Parkinson's disease.
    03/2015; 2(3). DOI:10.1002/acn3.167
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    ABSTRACT: α-Dystroglycanopathy (α-DGP) is a group of muscular dystrophy characterized by abnormal glycosylation of α-dystroglycan (α-DG), including Fukuyama congenital muscular dystrophy (FCMD), muscle-eye-brain disease, Walker-Warburg syndrome, and congenital muscular dystrophy type 1D (MDC1D), etc. LARGE, the causative gene for MDC1D, encodes a glycosyltransferase to form [-3Xyl-α1,3GlcAβ1-] polymer in the terminal end of the post-phosphoryl moiety, which is essential for α-DG function. It has been proposed that LARGE possesses the great potential to rescue glycosylation defects in α-DGPs regardless of causative genes. However, the in vivo therapeutic benefit of using LARGE activity is controversial. To explore the conditions needed for successful LARGE gene therapy, here we used Large-deficient and fukutin-deficient mouse models for MDC1D and FCMD, respectively. Myofibre-selective LARGE expression via systemic adeno-associated viral gene transfer ameliorated dystrophic pathology of Large-deficient mice even when intervention occurred after disease manifestation. However, the same strategy failed to ameliorate the dystrophic phenotype of fukutin-conditional knockout mice. Furthermore, forced expression of Large in fukutin-deficient embryonic stem cells also failed to recover α-DG glycosylation, however coexpression with fukutin strongly enhanced α-DG glycosylation. Together, our data demonstrated that fukutin is required for LARGE-dependent rescue of α-DG glycosylation, and thus suggesting new directions for LARGE-utilizing therapy targeted to myofibres.
    Scientific Reports 02/2015; 5:8316. DOI:10.1038/srep08316 · 5.58 Impact Factor
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    ABSTRACT: Identification of causative genes in mendelian forms of Parkinson's disease is valuable for understanding the cause of the disease. We did genetic studies in a Japanese family with autosomal dominant Parkinson's disease to identify novel causative genes. We did a genome-wide linkage analysis on eight affected and five unaffected individuals from a family with autosomal dominant Parkinson's disease (family A). Subsequently, we did exome sequencing on three patients and whole-genome sequencing on one patient in family A. Variants were validated by Sanger sequencing in samples from patients with autosomal dominant Parkinson's disease, patients with sporadic Parkinson's disease, and controls. Participants were identified from the DNA bank of the Comprehensive Genetic Study on Parkinson's Disease and Related Disorders (Juntendo University School of Medicine, Tokyo, Japan) and were classified according to clinical information obtained by neurologists. Splicing abnormalities of CHCHD2 mutants were analysed in SH-SY5Y cells. We used the Fisher's exact test to calculate the significance of allele frequencies between patients with sporadic Parkinson's disease and unaffected controls, and we calculated odds ratios and 95% CIs of minor alleles. We identified a missense mutation (CHCHD2, 182C>T, Thr61Ile) in family A by next-generation sequencing. We obtained samples from a further 340 index patients with autosomal dominant Parkinson's disease, 517 patients with sporadic Parkinson's disease, and 559 controls. Three CHCHD2 mutations in four of 341 index cases from independent families with autosomal dominant Parkinson's disease were detected by CHCHD2 mutation screening: 182C>T (Thr61Ile), 434G>A (Arg145Gln), and 300+5G>A. Two single nucleotide variants (-9T>G and 5C>T) in CHCHD2 were confirmed to have different frequencies between sporadic Parkinson's disease and controls, with odds ratios of 2·51 (95% CI 1·48-4·24; p=0·0004) and 4·69 (1·59-13·83, p=0·0025), respectively. One single nucleotide polymorphism (rs816411) was found in CHCHD2 from a previously reported genome-wide association study; however, there was no significant difference in its frequency between patients with Parkinson's disease and controls in a previously reported genome-wide association study (odds ratio 1·17, 95% CI 0·96-1·19; p=0·22). In SH-SY5Y cells, the 300+5G>A mutation but not the other two mutations caused exon 2 skipping. CHCHD2 mutations are associated with, and might be a cause of, autosomal dominant Parkinson's disease. Further genetic studies in other populations are needed to confirm the pathogenicity of CHCHD2 mutations in autosomal dominant Parkinson's disease and susceptibility for sporadic Parkinson's disease, and further functional studies are needed to understand how mutant CHCHD2 might play a part in the pathophysiology of Parkinson's disease. Japan Society for the Promotion of Science; Japanese Ministry of Education, Culture, Sports, Science and Technology; Japanese Ministry of Health, Labour and Welfare; Takeda Scientific Foundation; Cell Science Research Foundation; and Nakajima Foundation. Copyright © 2015 Elsevier Ltd. All rights reserved.
    The Lancet Neurology 02/2015; 14(3). DOI:10.1016/S1474-4422(14)70266-2 · 21.82 Impact Factor
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    ABSTRACT: accepted on Dec. 24, 2014
    The Lancet Neurology 02/2015; accepted. · 21.82 Impact Factor
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    ABSTRACT: This study was conducted to find out Spinocerebellar Ataxias (SCA) by genetic analysis from those patients presenting with Parkinsonism in the Neurology department of Mymensingh Medical College Hospital, Bangladesh. A sample of about 5ml blood was collected by venipuncture in EDTA tube after having informed consent from each patients and healthy individual, with due Institutional Ethical committee approval for genetic study of 7 healthy people and 9 patients. The neurological disorder along with a complete physical and/or psychological, as well as family history and demographic data was recorded with a prescribed questionnaire by the neurologists of Mymensingh Medical College Hospital. Extraction of genomic DNA from the venous blood using Flexi Gene DNA kit (Qiagen, Japan) was performed in Faculty of Veterinary Science, Bangladesh Agricultural University, Mymensingh, Bangladesh. The extracted DNA was stored, accumulated and then were sent to Division of Clinical Genetics, Department of Medical Genetics, Osaka University Medical School, Suita, Osaka 565 0871, Japan for PCR and further analysis. PCR amplification of the CAG repeat was performed for the SCA1, SCA2, SCA3, SCA6 loci using primers SCA1N-F1 and SCA1N-R1, SCA2-F1 and SCA2-R1, MJDF1 and MJDR1, SCA6-F1 and SCA6-R1, respectively. SCA1 PCR of both healthy individual and suspected Parkinsons Disease (PD) patients DNA was found 250 bp (no. of CAG repeats=36). SCA2 PCR products reveal the DNA products of about 150 bp (no. of CAG repeats=23) except one patient that was suspected and it was sequenced and revealed 175bp (no. of CAG repeats=30). SCA3 PCR product size of both healthy individual and patient DNA was within 250 (no. of CAG repeats=11) to 300 bp (no. of CAG repeats=28) except one patient which was about 320 bp and its CAG repeats was about 34. SCA6 PCR product size of both healthy individual and patient DNA was about 150 bp (no. of CAG repeats=16).
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    ABSTRACT: A 65-year-old woman experienced progressive intrinsic muscle wasting on the right hand over a period of 7 years. The distribution of muscular atrophy and weakness was consistent with the area innervated by the right C8 and Th1 nerve roots. Neurophysiological examination suggested a right lower trunk lesion. An elongated right transverse process of the C7 vertebra and an aberrant subclavian artery were detected on computed tomography images, and the right lower trunk of the brachial plexus appeared to be lifted upward on magnetic resonance images. The patient was diagnosed with true neurogenic thoracic outlet syndrome. A fibrous band extending from the elongated transverse process was found during surgery, and symptoms did not progress further after resection of the band. True neurogenic thoracic outlet syndrome can cause monomelic amyotrophy, and localized neuroimaging and detailed neurophysiological examination were useful for diagnosis.
    01/2015; 55(3):155-9. DOI:10.5692/clinicalneurol.55.155
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    ABSTRACT: Long QT syndrome (LQTS) is an arrhythmogenic disorder that can lead to sudden death. To date, mutations in 15 LQTS-susceptibility genes have been implicated. However, the genetic cause for approximately 20% of LQTS patients remains elusive. Here, we performed whole-exome sequencing analyses on 59 LQTS and 61 unaffected individuals in 35 families and 138 unrelated LQTS cases, after genetic screening of known LQTS genes. Our systematic analysis of familial cases and subsequent verification by Sanger sequencing identified 92 candidate mutations in 88 genes for 23 of the 35 families (65.7%): these included eleven de novo, five recessive (two homozygous and three compound heterozygous) and seventy-three dominant mutations. Although no novel commonly mutated gene was identified other than known LQTS genes, protein-protein interaction (PPI) network analyses revealed ten new pathogenic candidates that directly or indirectly interact with proteins encoded by known LQTS genes. Furthermore, candidate gene based association studies using an independent set of 138 unrelated LQTS cases and 587 controls identified an additional novel candidate. Together, mutations in these new candidates and known genes explained 37.1% of the LQTS families (13 in 35). Moreover, half of the newly identified candidates directly interact with calmodulin (5 in 11; comparison with all genes; p=0.042). Subsequent variant analysis in the independent set of 138 cases identified 16 variants in the 11 genes, of which 14 were in calmodulin-interacting genes (87.5%). These results suggest an important role of calmodulin and its interacting proteins in the pathogenesis of LQTS.
    PLoS ONE 01/2015; 10(7):e0130329. DOI:10.1371/journal.pone.0130329 · 3.53 Impact Factor
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    ABSTRACT: A 76-year-old female was referred to our department because of diplopia for two months and intermittent claudication for five months. She showed medial longitudinal fasciculus (MLF) syndrome. Brain MRI (T2WI) showed multiple infarctions in the right pontine tegmentum and left paramedian midbrain. A biopsy of superficial temporal artery showed the characteristic findings of glanulomatous inflammation indicative of giant cell arteritis. We thought the mechanism of this cerebral infarction as artery to artery embolization or intracranial arteritis. Treatment with oral prednisolone (1 mg/kg/day) improved her limb claudication and normalized serum C-reactive protein level.
    Rinsho shinkeigaku = Clinical neurology 01/2015; 55(2):107-10. DOI:10.5692/clinicalneurol.55.107
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    ABSTRACT: The patient was a 46-year-old woman having a history of multiple sclerosis (MS) for 14 years. She had been treated with interferon β-1b since 2001, but discontinued because of psychiatric problems in 2006. Thereafter relapses were observed 1-2 times a year, and EDSS became 2.5 to 6.5. In April 2012, relapse of MS was noticed and the patient received introduction of fingolimod (FTY) after methylprednisolone (mPSL) pulse therapy. Twenty days later, dysarthria and lower limb weakness were appeared. Brain MRI showed more than 20 several millimeter Gd enhanced lesions in periventricular white matter, juxta-cortical white matter, and cerebellum. Careful determination and observation are required upon the FTY administration into the MS with high frequency of relapse.
    01/2015; 55(6):417-20. DOI:10.5692/clinicalneurol.cn-000515
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    ABSTRACT: We report a patient having classical clinical feature of neurologic muscle weakness, ataxia, and retinitis pigmentosa (NARP) and a novel mutation, m.8729 G>A in mitochondria DNA. The patient was referred to our hospital because of progressive ataxia in her limbs and trunk. She had a history of incapability of running long distances from childhood. Neurological examination revealed cerebellar ataxia, distal dominant muscle weakness in the limbs, hyporeflexia, hypoesthesia, myoclonus, sensorineural deafness, and retinitis pigmentosa. Magnetic resonance imaging (MRI) showed atrophy of brain stem and cerebellum as well as calcification of basal ganglia. In both serum and cerebrospinal fluid, lactate and pyruvate levels were elevated. Histological examination of biopsied muscle revealed chronic neurogenic changes without ragged red fibers. Genetic analysis of mitochondrial DNA (mtDNA) of the muscle revealed a heteroplasmic mutation, m.8729 G>A. Chemical analysis of the respiratory chain complexes in her muscle specimen demonstrated lower activities of complexes I and V. In our case, novel mutation of m.8729 G>A in mtDNA was indicated as the cause of NARP syndrome.
    Rinsho shinkeigaku = Clinical neurology 01/2015; 55(2):91-5. DOI:10.5692/clinicalneurol.55.91
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    ABSTRACT: Limb malformations are rare disorders with high genetic heterogeneity. Although multiple genes/loci have been identified in limb malformations, underlying genetic factors still remain to be determined in most patients.
    Orphanet Journal of Rare Diseases 10/2014; 9(1):125. DOI:10.1186/s13023-014-0125-5 · 3.96 Impact Factor
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    ABSTRACT: Defects in dystroglycan glycosylation are associated with a group of muscular dystrophies, termed dystroglycanopathies, that include Fukuyama congenital muscular dystrophy (FCMD). It is widely believed that abnormal glycosylation of dystroglycan leads to disease-causing membrane fragility. We previously generated knock-in mice carrying a founder retrotransposal insertion in fukutin, the gene responsible for FCMD, but these mice did not develop muscular dystrophy, which hindered exploring therapeutic strategies. We hypothesized that dysferlin functions may contribute to muscle cell viability in the knock-in mice; however, pathological interactions between glycosylation abnormalities and dysferlin defects remain unexplored. To investigate contributions of dysferlin deficiency to the pathology of dystroglycanopathy, we have crossed dysferlin-deficient dysferlinsjl/sjl mice to the fukutin-knock-in fukutinHp/- and Large-deficient Largemyd/myd mice, which are phenotypically distinct models of dystroglycanopathy. The fukutinHp/- mice do not show a dystrophic phenotype; however, (dysferlinsjl/sjl: fukutinHp/-) mice showed a deteriorated phenotype compared with (dysferlinsjl/sjl: fukutinHp/+) mice. These data indicate that the absence of functional dysferlin in the asymptomatic fukutinHp/- mice triggers disease manifestation and aggravates the dystrophic phenotype. A series of pathological analyses using double mutant mice for Large and dysferlin indicate that the protective effects of dysferlin appear diminished when the dystrophic pathology is severe and also may depend on the amount of dysferlin proteins. Together, our results show that dysferlin exerts protective effects on the fukutinHp/- FCMD mouse model, and the (dysferlinsjl/sjl: fukutinHp/-) mice will be useful as a novel model for a recently proposed antisense oligonucleotide therapy for FCMD.
    PLoS ONE 09/2014; 9(9):e106721. DOI:10.1371/journal.pone.0106721 · 3.53 Impact Factor
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    ABSTRACT: Background: The ASCO classification can evaluate the etiology and mechanisms of ischemic stroke more comprehensively and systematically than conventional stroke classification systems such as Trial of Org 10172 in Acute Stroke Treatment (TOAST). Simultaneously, risk factors for cognitive impairment such as arterial sclerosis, leukoaraiosis, and atrial fibrillation can also be gathered and graded using the ASCO classification. Methods: Sixty patients with postischemic stroke underwent cognitive testing, including testing by the Japanese version of the Montreal cognitive assessment (MoCA-J) and the mini-mental state examination (MMSE). Ischemic strokes were categorized and graded by the ASCO classification. In this phenotype-based classification, every patient is characterized by the A-S-C-O system (A for Atherosclerosis, S for Small vessel disease, C for Cardiac source, and O for Other cause). Each of the 4 phenotypes is graded 0, 1, 2, or 3, according to severity. The conventional TOAST classification was also applied. Correlations between individual MoCA-J/MMSE scores and the ASCO scores were assessed. Results: The total score of the ASCO classification significantly correlated with the total scores of MoCA-J and MMSE. This correlation was more apparent in MoCA-J than in MMSE, because MoCA-J scores were normally distributed, whereas MMSE scores were skewed toward the higher end of the range (ceiling effect). Results for individual subtests of MoCA-J and MMSE indicated that cognitive function for visuoexecutive, calculation, abstraction, and remote recall significantly correlated with ASCO score. Conclusions: These results suggest that the ASCO phenotypic classification of stroke is useful not only for assessing the etiology of ischemic stroke but also for predicting cognitive decline after ischemic stroke.
    Journal of stroke and cerebrovascular diseases: the official journal of National Stroke Association 08/2014; 23(9). DOI:10.1016/j.jstrokecerebrovasdis.2014.04.009 · 1.99 Impact Factor
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    ABSTRACT: Protein kinase C (PKC) has been implicated in the control of neurotransmitter release. The AS/AGU rat, which has a nonsense mutation in PKCγ, shows symptoms of parkinsonian syndrome, including dopamine release impairments in the striatum. Here, we found that the AS/AGU rat is PKCγ-knock-out (KO) and that PKCγ-KO mice showed parkinsonian syndrome. However, the PKCγ substrates responsible for the regulated exocytosis of dopamine in vivo have not yet been elucidated. To identify the PKCγ substrates involved in dopamine release, we used PKCγ-KO mice and a phosphoproteome analysis. We found 10 candidate phosphoproteins that had decreased phosphorylation levels in the striatum of PKCγ-KO mice. We focused on Pak-interacting exchange factor-β (βPIX), a Cdc42/Rac1 guanine nucleotide exchange factor, and found that PKCγ directly phosphorylates βPIX at Ser583 and indirectly at Ser340 in cells. Furthermore, we found that PKC phosphorylated βPIX in vivo. Classical PKC inhibitors and βPIX knock-down (KD) significantly suppressed Ca(2+)-evoked dopamine release in PC12 cells. Wild-type βPIX, and not the βPIX mutants Ser340 Ala or Ser583 Ala, fully rescued the decreased dopamine release by βPIX KD. Double KD of Cdc42 and Rac1 decreased dopamine release from PC12 cells. These findings indicate that the phosphorylation of βPIX at Ser340 and Ser583 has pivotal roles in Ca(2+)-evoked dopamine release in the striatum. Therefore, we propose that PKCγ positively modulates dopamine release through β2PIX phosphorylation. The PKCγ-βPIX-Cdc42/Rac1 phosphorylation axis may provide a new therapeutic target for the treatment of parkinsonian syndrome.
    The Journal of Neuroscience : The Official Journal of the Society for Neuroscience 07/2014; 34(28):9268-80. DOI:10.1523/JNEUROSCI.4278-13.2014 · 6.75 Impact Factor
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    ABSTRACT: BACKGROUND: -Genetic predisposition to life-threatening cardiac arrhythmias such as in congenital long-QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT) represent treatable causes of sudden cardiac death in young adults and children. Recently, mutations in calmodulin (CALM1, CALM2) have been associated with severe forms of LQTS and CPVT, with life-threatening arrhythmias occurring very early in life. Additional mutation-positive cases are needed to discern genotype-phenotype correlations associated with calmodulin mutations. METHODS AND RESULTS: -We employed conventional and next-generation sequencing approaches including exome analysis in genotype-negative LQTS probands. We identified five novel de novo missense mutations in CALM2 in three subjects with LQTS (p.N98S, p.N98I, p.D134H) and two subjects with clinical features of both LQTS and CPVT (p.D132E, p.Q136P). Age of onset of major symptoms (syncope or cardiac arrest) ranged from 1-9 years. Three of five probands had cardiac arrest and one of these subjects did not survive. Although all probands had LQTS, two subjects also exhibited electrocardiographic features consistent with CPVT. The clinical severity among subjects in this series was generally less than that originally reported for CALM1 and CALM2 associated with recurrent cardiac arrest during infancy. Four of five probands responded to beta-blocker therapy whereas one subject with mutation p.Q136P died suddenly during exertion despite this treatment. Mutations affect conserved residues located within calcium binding loops III (p.N98S, p.N98I) or IV (p.D132E, p.D134H, p.Q136P) and caused reduced calcium binding affinity. CONCLUSIONS: -CALM2M mutations can be associated with LQTS and with overlapping features of LQTS and CPVT.
    Circulation Cardiovascular Genetics 06/2014; 7(4). DOI:10.1161/circgenetics.113.000459 · 6.73 Impact Factor
  • Clinical Neurophysiology 06/2014; 125:S251-S252. DOI:10.1016/S1388-2457(14)50822-X · 2.98 Impact Factor

Publication Stats

7k Citations
1,154.59 Total Impact Points


  • 2009–2015
    • Kobe University
      • Graduate School of Medicine
      Kōbe, Hyōgo, Japan
  • 2012
    • Hertie-Institute for Clinical Brain Research
      Tübingen, Baden-Württemberg, Germany
  • 2010
    • Bangladesh Agricultural University
      • Department of Medicine
      Mymensingh, Bangladesh
    • Tokai University
      • Department of Rehabilitation Medicine
      Hiratuka, Kanagawa, Japan
  • 2006–2010
    • Osaka University
      • • Graduate School of Medicine
      • • Department of Medical Genetics
      • • Division of Clinical Genetics
      Suika, Ōsaka, Japan
  • 2001–2010
    • Osaka City University
      • Department of Orthopaedic Surgery
      Ōsaka, Ōsaka, Japan
  • 2008
    • Showa University
      • Department of Neurology
      Shinagawa, Tōkyō, Japan
  • 2007
    • Kagawa Prefectural Central Hospital
      Takamatu, Kagawa, Japan
    • Osaka Prefecture University
      • Graduate School of Life and Environmental Sciences
      Sakai, Ōsaka, Japan
  • 1995–2007
    • The University of Tokyo
      • • Department of International Health
      • • Center for Human Genome
      Tokyo, Tokyo-to, Japan
  • 2004–2006
    • Fujita Health University
      • Department of Molecular Genetics
      Nagoya, Aichi, Japan
    • Tokyo Metropolitan Institute of Gerontology
      Edo, Tōkyō, Japan
  • 2004–2005
    • Juntendo University
      • Department of Neurology
      Edo, Tōkyō, Japan
  • 1997
    • Tokyo Junshin Women's College
      • Department of Pediatrics
      Edo, Tōkyō, Japan