A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease? [In Process Citation]

Koide, Reiji; Kobayashi, S.; Shimohata, Takayoshi; Ikeuchi, Takeshi; Maruyama, Mieko; Saito, Masaaki; Yamada, Mitsunori; Takahashi, Hitoshi; Tsuji, Shoji

doi:10.1093/hmg/8.11.2047

Cited by 374 publications

(253 citation statements)

References 27 publications

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“…Routine molecular diagnostic for FRDA, SCA1, 2, 3, 6, 7, 10, and 12 loci revealed heterozygosity for two normal-sized alleles. For SCA17, PCR was performed using primers described by Koide et al 8 Products were separated and visualized on 6% denaturing polyacrylamide gels and silver staining.…”

Section: Clinical Data Of the Patientmentioning

confidence: 99%

“…Among patients with various forms of neurological diseases, one individual showed a de novo expansion of the repeat in the TBP gene because of a partial duplication 8 resulting in an expanded polyglutamine domain with 63 amino-acid residues. Clinically, this patient presented with ataxia, short stature, atypical absences, pyramidal signs, and mental deterioration.…”

Section: Introductionmentioning

confidence: 99%

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SCA17 caused by homozygous repeat expansion in TBP due to partial isodisomy 6

Zühlke

Spranger

et al. 2003

Eur J Hum Genet

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An expanded polyglutamine domain in the TATA-binding protein (TBP) has been described in patients with spinocerebellar ataxia type 17 (SCA17) characterized by cerebellar ataxia associated with dementia. TBP is a general transcription initiation factor that regulates the expression of most eukaryotic genes transcribed by RNA polymerase II. SCA17, as an autosomal dominantly inherited progressive neurodegenerative disorder, is caused by heterozygous expansion of a CAG repeat coding for glutamine. Alleles with 27 to a maximum of 44 glutamine residues were found as the normal range, whereas expansions above 45 repeat units were considered pathological. Here, we present a patient with a very severe phenotype with a late onset but rapidly progressing ataxia associated with dementia and homozygous 47 glutamine residues caused by an apparent partial isodisomy 6. This extraordinary case has important implications for the insights of TBP and SCA17. The expanded polyglutamine domain in both TBP copies is not correlated with embryonic death indicating that the normal function of the protein is not disrupted by this kind of mutation but may account for the dementia seen in this patient.

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Section: Clinical Data Of the Patientmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

SCA17 caused by homozygous repeat expansion in TBP due to partial isodisomy 6

Zühlke

Spranger

et al. 2003

Eur J Hum Genet

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“…To date, 9 polyQ diseases have been identified: spinal-bulbar muscular atrophy (SBMA) [1], Huntington disease (HD) [2], spinocerebellar ataxia (SCA) type 1 (SCA1) [3], SCA type 3 (SCA3) [4], dentatorubral-pallidoluysian atrophy (DRPLA) [5], SCA type 2 (SCA2) [6], SCA type 7 (SCA7) [7], SCA type 6 (SCA6) [8], and SCA type 17 (SCA17) [9]. All of these diseases share autosomal dominant inheritance, with the exception of SBMA, which shows Xlinked inheritance.…”

Section: Introductionmentioning

confidence: 99%

The Role for Alterations in Neuronal Activity in the Pathogenesis of Polyglutamine Repeat Disorders

Chopra

Shakkottai

2014

Neurotherapeutics

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Polyglutamine diseases are a class of neurodegenerative diseases that share an expansion of a glutamineencoding CAG tract in the respective disease genes as a central hallmark. In all of these diseases there is progressive degeneration in a select subset of neurons, and the mechanisms behind this degeneration remain unclear. Emerging evidence from animal models of disease has identified abnormalities in synaptic signaling and intrinsic excitability in affected neurons, which coincide with the onset of symptoms and precede apparent neuropathology. The appearance of these early changes suggests that altered neuronal activity might be an important component of network dysfunction and that these alterations in network physiology could contribute to symptoms of disease. Here we review abnormalities in neuronal function that have been identified in both animal models and patients, and highlight ways in which these changes in neuronal activity may contribute to disease symptoms. We then review the literature supporting an emerging role for abnormalities in neuronal activity as a driver of neurodegeneration. Finally, we identify common themes that emerge from studies of neuronal dysfunction in polyglutamine disease.

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“…This is the case for some forms of autosomal dominant cerebellar ataxia, specifically spinocerebellar ataxia type 17 (SCA17) (Koide et al 1999;Nakamura et al 2001), and dentatorubropallidoluysian atrophy (DRPLA) (Koide et al 1994), which may show clinical features similar to those of HD, namely dementia, chorea, Parkinsonism and dystonia. SCA17 is caused by an expansion of a CAA/ CAG repeat segment on the TATA-binding protein gene (TBP), and DRPLA is also caused by an expansion of a (CAG) n in the gene encoding athrophin-1 (ATN1).…”

Section: Introductionmentioning

confidence: 99%

Exclusion of mutations in the PRNP, JPH3, TBP, ATN1, CREBBP, POU3F2 and FTL genes as a cause of disease in Portuguese patients with a Huntington-like phenotype

et al. 2006

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Huntington disease (HD) is an autosomal dominant neurodegenerative disorder characterised by chorea, cognitive impairment, dementia and personality changes, caused by the expansion of a CAG repeat in the HD gene. Often, patients with a similar clinical presentation do not carry expansions of the CAG repeat in this gene [Huntington disease-like (HDL) patients]. We report the genetic analysis of 107 Portuguese patients with an HDL phenotype. The HDL genes PRNP and JPH3, encoding the prion protein and junctophilin-3, respectively, were screened for repeat expansions in these patients. Given the partial clinical overlap of SCA17, DRPLA and neuroferritinopathy with HD, their causative genes (TBP, ATN1, and FTL, respectively) were also analysed. Finally, repeat expansions in two candidate genes, CREBBP and POU3F2, which encode the nuclear transcriptional coactivator CREB-binding protein and the CNS-specific transcription factor NOct-3, respectively, were also studied. Expansions of the repetitive tracts of the PRNP, JPH3, TBP, ATN1, CREBBP and POU3F2 genes were excluded in all patients, as were sequence alterations in the FTL gene. Since none of the genes already included in the differential diagnosis of HD was responsible for the disease in our sample, the genetic heterogeneity of the HDL phenotype is still open for investigation.

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A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease? [In Process Citation]

Cited by 374 publications

References 27 publications

SCA17 caused by homozygous repeat expansion in TBP due to partial isodisomy 6

SCA17 caused by homozygous repeat expansion in TBP due to partial isodisomy 6

The Role for Alterations in Neuronal Activity in the Pathogenesis of Polyglutamine Repeat Disorders

Exclusion of mutations in the PRNP, JPH3, TBP, ATN1, CREBBP, POU3F2 and FTL genes as a cause of disease in Portuguese patients with a Huntington-like phenotype

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