2002
DOI: 10.1212/wnl.58.1.120
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TorsinA immunoreactivity in brains of patients with DYT1 and non- DYT1 dystonia

Abstract: A mutation of the DYT1 gene, which codes for torsinA, has been identified as the cause of one form of autosomal dominantly inherited dystonia. TorsinA immunohistochemistry was used to examine a case of DYT1, and several cases of non-DYT1, dystonia. No evidence was found for alterations of immunoreactivity at the light microscopic level, specifically neither cytoplasmic aggregations nor colocalization of torsinA immunoreactivity with a marker for endoplasmic reticulum. These findings contrast with results of re… Show more

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Cited by 74 publications
(68 citation statements)
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“…In addition, recent evidence indicates that a significant pool of torsinA exhibits a topology in which the AAA ϩ domain faces the cytoplasm (20). In support of this topology, torsinA is found in the cytoplasm, neuronal processes, and synaptic terminals (2,3,15,(23)(24)(25)(26) and has been shown to bind cytosolic proteins snapin (27) and kinesin light chain 1 (20). TorsinA has been proposed to play a role in several cellular processes, including dopaminergic neurotransmission (28 -31), NE organization and dynamics (17,22,32), and protein trafficking (27,33).…”
mentioning
confidence: 86%
See 1 more Smart Citation
“…In addition, recent evidence indicates that a significant pool of torsinA exhibits a topology in which the AAA ϩ domain faces the cytoplasm (20). In support of this topology, torsinA is found in the cytoplasm, neuronal processes, and synaptic terminals (2,3,15,(23)(24)(25)(26) and has been shown to bind cytosolic proteins snapin (27) and kinesin light chain 1 (20). TorsinA has been proposed to play a role in several cellular processes, including dopaminergic neurotransmission (28 -31), NE organization and dynamics (17,22,32), and protein trafficking (27,33).…”
mentioning
confidence: 86%
“…This autosomal dominant disease has childhood onset and its dystonic symptoms are thought to result from neuronal dysfunction rather than neurodegeneration (2,3). Most DYT1 cases are caused by deletion of a single glutamate residue at positions 302 or 303 (torsinA ⌬E) of the 332-amino acid protein torsinA (4).…”
mentioning
confidence: 99%
“…The question of whether inclusion body pathology is specific to the transgenic mouse models, or whether it is also part of human DYT1 disease remains somewhat controversial. Most histopathological studies of brains from patients with DYT1 failed to find evidence of protein accumulation or inclusion bodies (Walker et al, 2002;Rostasy et al, 2003), but a recent study of postmortem material from DYT1 patients has reported that perinuclear inclusion bodies are present in neurons in various brain stem areas (McNaught et al, 2004).…”
Section: Animal Models For Dyt1 Dystoniamentioning
confidence: 99%
“…Postmortem analysis of DYT1 brain has not identified specific neuropathological findings or changes in TA expression or subcellular distribution (Augood et al, 2002;Walker et al, 2002;Rostasy et al, 2003). Studies in cell-based models of DYT1, however, have revealed aberrant localization of mutant TA (TAmut).…”
Section: Introductionmentioning
confidence: 99%