Ultrastructure of Brain and Nerve Biopsy Tissue in Wilson Disease

Anzil, A. P.; Herrlinger, H.; Blinzinger, K.; Heldrich, Albrecht

doi:10.1001/archneur.1974.00490380042004

Cited by 34 publications

(7 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In some cases these changes were more evident in the cortex (86). Mottling of basal lamina in cortical capillaries has also been observed with electronic microscopy (87). Some authors have clearly admitted the presence of circulatory disturbances (73, 79, 85, 88).…”

Section: Discussionmentioning

confidence: 95%

Comparison of MRI, EEG, EPs and ECD-SPECT in Wilson's disease

Tamburini

Piga³

et al. 2001

Acta Neurologica Scandinavica

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 95%

Comparison of MRI, EEG, EPs and ECD-SPECT in Wilson's disease

Tamburini

Piga³

et al. 2001

Acta Neurologica Scandinavica

View full text Add to dashboard Cite

show abstract

“…Das and Ray 2006), in accordance with the parkinsonian symptoms. Brain damage in WD is accom-panied by gliosis (Anzil et al 1974;McGeer et al 1987;Thomas et al 1995).…”

mentioning

confidence: 99%

Neuroinflammatory and behavioural changes in the Atp7B mutant mouse model of Wilson’s disease

Terwel

Löschmann

Schmidt

et al. 2011

Journal of Neurochemistry

View full text Add to dashboard Cite

Wilson's disease (WD) is caused by mutations in the copper transporting ATPase 7B (Atp7b). Patients present with liver pathology or behavioural disturbances. Studies on rodent models for WD so far mainly focussed on liver, not brain. The effect of knockout of atp7b on sensori-motor and cognitive behaviour, as well as neuronal number, inflammatory markers, copper and synaptic proteins in brain were studied in so-called toxic milk mice. Copper accumulated in striatum and hippocampus of toxic milk mice, but not in cerebral cortex. Inflammatory markers were increased in striatum and corpus callosum, but not in cerebral cortex and hippocampus, whereas neuronal numbers were unchanged. Toxic milk mice were mildly impaired in the rotarod and cylinder test and unable to acquire spatial memory in the Morris water maze. Despite the latter observation only synaptophysin of a number of synaptic proteins, was altered in the hippocampus of toxic milk mice. In addition to disturbances in neuronal signalling by increased brain copper, inflammation and inflammatory signalling from the periphery to the brain might add to the behavioural disturbances in the toxic milk mice. These mice can be used to evaluate therapeutic strategies to alleviate behavioural disturbances and cerebral pathology observed in WD.

show abstract

“…During the past three decades, Hirano bodies have been reported to be associated with a broad array of conditions, including Alzheimer's disease (21,44,45,60), Parkinson's disease (25), Pick's disease (61), amyotrophic lateral sclerosis (25), ataxic Creutzfeldt-Jakob disease (3), kuru (9), scrapie (10), leukoencephalopathy (23), chronic alcoholism (32), diabetes (64), cancer (12,20), muscle degeneration (11), and neuronal degeneration associated with abnormal copper homeostasis (1,46,53,71). Hirano bodies are paracrystalline cytoplasmic inclusions that contain actin filaments and actinassociated proteins (19,22,39).…”

mentioning

confidence: 99%

Formation of Hirano Bodies Induced by Expression of an Actin Cross-Linking Protein with a Gain-of-Function Mutation

et al. 2003

View full text Add to dashboard Cite

Hirano bodies are paracrystalline actin filament-containing structures reported to be associated with a variety of neurodegenerative diseases. However, the biological function of Hirano bodies remains poorly understood, since nearly all prior studies of these structures were done with postmortem samples of tissue. In the present study, we generated a full-length form of a Dictyostelium 34-kDa actin cross-linking protein with point mutations in the first putative EF hand, termed 34-kDa ⌬EF1. The 34-kDa ⌬EF1 protein binds calcium normally but has activated actin binding that is unregulated by calcium. The expression of the 34-kDa ⌬EF1 protein in Dictyostelium induces the formation of Hirano bodies, as assessed by both fluorescence microscopy and transmission electron microscopy. Dictyostelium cells bearing Hirano bodies grow normally, indicating that Hirano bodies are not associated with cell death and are not deleterious to cell growth. Moreover, the expression of the 34-kDa ⌬EF1 protein rescues the phenotypes of cells lacking the 34-kDa protein and cells lacking both the 34-kDa protein and ␣-actinin. Finally, the expression of the 34-kDa ⌬EF1 protein also initiates the formation of Hirano bodies in cultured mouse fibroblasts. These results show that the failure to regulate the activity and/or affinity of an actin cross-linking protein can provide a signal for the formation of Hirano bodies. More generally, the formation of Hirano bodies is a cellular response to or a consequence of aberrant function of the actin cytoskeleton.

show abstract

Ultrastructure of Brain and Nerve Biopsy Tissue in Wilson Disease

Cited by 34 publications

References 8 publications

Comparison of MRI, EEG, EPs and ECD-SPECT in Wilson's disease

Comparison of MRI, EEG, EPs and ECD-SPECT in Wilson's disease

Neuroinflammatory and behavioural changes in the Atp7B mutant mouse model of Wilson’s disease

Formation of Hirano Bodies Induced by Expression of an Actin Cross-Linking Protein with a Gain-of-Function Mutation

Contact Info

Product

Resources

About