1/18. Variant Gerstmann-Straussler syndrome with the P105L prion gene mutation: an unusual case with nigral degeneration and widespread neurofibrillary tangles.We present here a case of variant Gerstmann-Straussler syndrome (GSS) with a codon 105 mutation of the prion protein gene. A 57-year-old woman developed dementia and gait disturbance dissimilar to the spastic paraparesis that is observed in most cases with codon 105 mutation. The clinical course of the disease in this case was 12 years. The brain weighed 900 g, and the frontal lobe, pallidum and thalamus were markedly atrophic. Severe neuronal loss was observed in the deep layer of the frontal and temporal cortices, and fibrillary gliosis and a marked loss of neurons was observed in the globus pallidus, thalamus and substantia nigra. Many amyloid plaques and some ballooned neurons were present in the frontal, temporal and parietal cortices. However, no spongiform changes were seen. The cerebellum was relatively well preserved. Numerous neurofibrillary tangles (NFTs) were recognized in the cerebral cortices, and scattered NFTs were observed in the basal nucleus of meynert, thalamus, substantia nigra, periaqueductal gray matter, raphe nuclei and locus ceruleus. The case presented here indicates the presence of variations in the pathological findings of cases with codon 105 mutation, and that the formation of cortical and brain stem NFTs might have something to do with the duration of illness and/or the degree of brain tissue destruction that had occurred.- - - - - - - - - - ranking = 1keywords = spongiform, variant (Clic here for more details about this article) |
2/18. A three-sister sibship of gerstmann-straussler-scheinker disease with a CJD phenotype.OBJECTIVE: To describe a rare phenotypic variant of P102L gerstmann-straussler-scheinker disease (GSS). BACKGROUND: Classic GSS is characterized by an early age at onset, prominent cerebellar signs with a slowly evolving dementia, and a neuropathology including multifocal PrP-positive plaques and variable but usually modest spongiform change. methods: Clinical, neuropathologic, immunohistochemical, and molecular genetic analysis of three sisters in a Hungarian family was performed. RESULTS: The clinical course of all three sisters was indistinguishable from sporadic Creutzfeldt-Jakob disease (CJD). Neuropathologic examination revealed spongiform changes, PrP (prion)-positive unicentric "kuru" or multicentric plaques, and abundant beta-A4-positive senile plaques. Molecular genetic analysis of the PRNP gene showed the heterozygous codon P102L mutation of classic GSS, with the methionine encoding allele of a heterozygous codon 129 coupled to the mutant 102 allele. CONCLUSION: The authors report the second recorded example of a sporadic CJD phenotype occurring in association with the P102L GSS genotype, and the first instance in which the phenotype was the rule rather than the exception, or was associated with prominent beta-A4 plaque formation.- - - - - - - - - - ranking = 1.9999170002055keywords = spongiform, variant (Clic here for more details about this article) |
3/18. Report on the first polish case of the Gerstmann-Straussler-Scheinker syndrome.In the course of epidemiological studies on Creutzfeldt-Jakob Disease in poland, the authors found a male patient aged 54 years with dementia rapidly progressing for a year and ataxia of the extremities. EEG tracings were abnormal but without features typical of CJD. About six months after hospitalisation the patient died. Neuropathological examination of his brain demonstrated spongiform lesions of medium intensity present mainly in the cortex of frontal and occipital lobes, with slight proliferation of astroglia. In the cerebellar cortex numerous deposits of PAS-positive substance amorphous or in the shape of kuru plaques were disclosed. A smaller number of these plaques were found in the cortex of occipital and temporal lobes, and in the putamen. All deposits stained strongly with monoclonal 3F4 antibody to human prion protein (PrP). Genetic studies disclosed in the 20th chromosome, in the PrP gene, mutation at codon 102 (P102L). codon 129 was homozygous for methionine (M129M). It was established, moreover, that patient's father had at the same age a similar disease and died after one year and patient's sister died after a six-year-long neurological disease diagnosed as multiple sclerosis. On the basis of clinical, genetic and neuropathological findings the authors diagnosed the Gerstmann-Straussler-Scheinker syndrome, a familial prion disease with autosomal dominant character. This is the first report on this syndrome in poland.- - - - - - - - - - ranking = 0.99991700020549keywords = spongiform (Clic here for more details about this article) |
4/18. A new PRNP mutation (G131V) associated with gerstmann-straussler-scheinker disease.BACKGROUND: gerstmann-straussler-scheinker disease is a rare form of prion disease. OBJECTIVE: To determine the prion mutation in a 51-year-old man without a family history of neurologic disease who died from gerstmann-straussler-scheinker disease. PATIENT AND methods: The patient was a 51-year-old man who died after a 9-year illness characterized by dementia and eventually ataxia. Neuropathologic studies were performed, the results of which revealed abundant prion protein-immunopositive amyloid plaques in the cerebellum without spongiform degeneration. RESULTS: Genetic analysis of the prion protein gene showed a novel mutation at codon 131 that caused a valine-for-glycine substitution (G131V) and homozygosity at codon 129 (129M). Proteinase K-resistant prion protein was detected by Western blot analysis. CONCLUSIONS: This is the first mutation described in the short, antiparallel beta-sheet domain of the prion protein. This report highlights the importance of genetic analysis of patients with atypical dementia even in the absence of a family history.- - - - - - - - - - ranking = 0.99991700020549keywords = spongiform (Clic here for more details about this article) |
5/18. Hyperphosphorylated tau deposition parallels prion protein burden in a case of Gerstmann-Straussler-Scheinker syndrome P102L mutation complicated with dementia.Hyperphosphorylated tau (p-tau) deposition has been documented in a limited population of patients with Gerstmann-Straussler-Scheinker syndrome (GSS) with particular point mutations of the prion protein (PrP) gene. Although its pathogenesis is only poorly understood, p-tau in GSS is known to be identical to that in Alzheimer's disease (AD). We conducted immunohistochemical and quantitative image studies on the brain from a 44-year-old man with a 7-year history of dementia, diagnosed as having GSS with a point mutation of the PrP gene at codon 102 (GSS102), the commonest mutation in GSS. Severe spongiform degeneration and numerous PrP plaques were disclosed in the cerebral cortices and hippocampus, consistent with the diagnosis. However, rarely described in GSS102, prominent p-tau deposits as pretangles, neurofibrillary tangles and degenerating neurites were demonstrated adjacent to or around PrP plaques. beta-amyloid protein (Abeta) plaques were generally sparse and appeared invariably to be of a diffuse type. Double-labeling immunohistochemistry yielded co-localization of p-tau with PrP but not with Abeta. Most PrP plaques did not contain Abeta. These results excluded a diagnosis of concomitant AD. Quantitative analysis on a fractional area density of immunoreactive pixels demonstrated that burdens of PrP and p-tau but not Abeta were significantly correlated. These results suggest that p-tau deposition in this GSS102 is secondarily induced by PrP but not by Abeta (secondary tauopathy). Our study also suggests that p-tau deposition might be a more common phenomenon in long-standing GSS.- - - - - - - - - - ranking = 0.99991700020549keywords = spongiform (Clic here for more details about this article) |
6/18. Neuropathological features of a case with schizophrenia and prion protein gene P102L mutation before onset of gerstmann-straussler-scheinker disease.gerstmann-straussler-scheinker disease (GSS) is a hereditary transmissible spongiform encephalopathy associated with prion protein gene mutation P102L. The age of onset is roughly restricted to around the sixth decade; however, it is unclear whether the disease-specific pathology of GSS is already evident in the pre-clinical stage. We had a chance to examine an autopsy case with PRNP P102L mutation. The patient had died at 50 years of age before the clinical symptoms of GSS had appeared; neither neuronal loss, gliosis nor spongiform change was found anywhere in the brain. immunohistochemistry failed to detect any deposition of prion protein. It is thus considered that amyloid plaque formation in GSS probably develops in a relatively rapid fashion compared with Alzheimer's disease. Although the patient suffered from schizophrenia, no significant pathological changes were detected except for astrocytic inclusion bodies in the cerebral cortex. The nature and significance of the inclusion bodies, which are not observed in patients with GSS, remain unclear.- - - - - - - - - - ranking = 9.4694632062716keywords = spongiform encephalopathy, spongiform, encephalopathy (Clic here for more details about this article) |
7/18. Linkage of the indiana kindred of gerstmann-straussler-scheinker disease to the prion protein gene.The indiana kindred variant of gerstmann-straussler-scheinker disease has amyloid plaques that contain prion protein (PrP), but is atypical because neurofibrillary tangles like those of alzheimer disease are present. To map the position of the disease causing gene, we used three markers for linkage analyses. A missense mutation at codon 198 of the PrP gene (PRNP) is found in all definitely affected individuals and yields a maximum lod score of 6.37 (theta = 0). The disease also is concordant with the two other PRNP-region markers. These results demonstrate tight linkage of the disease-causing gene to PRNP and support the hypothesis that the codon 198 mutation is the cause of IK-GSS. Our studies also suggest that methionine/valine heterozygotes at PRNP codon 129 have a later age of onset of the disease than codon 129 valine/valine homozygotes.- - - - - - - - - - ranking = 8.2999794513739E-5keywords = variant (Clic here for more details about this article) |
8/18. Gerstmann-Straussler syndrome--a variant type: amyloid plaques and Alzheimer's neurofibrillary tangles in cerebral cortex.This report presents a variant of Gerstmann-Straussler syndrome (GSS). A 53-year-old female had developed slowly progressive dementia and atactic gait since the age of 45. No myoclonic jerks and periodic synchronous discharges were observed throughout the illness. The neuropathological study revealed that many amyloid plaques and widespread Alzheimer's neurofibrillary tangles (NFTs) appeared in the cerebral cortex. Characteristically, the plaques reacted with anti-prion protein and none of them reacted with anti-beta protein, and they were made of many components, including amyloid cores, macrophages laden with lipid granules and/or degenerated neurites. neuropil threads were seen mainly in amyloid plaques. Moreover, plaques appeared which were confluent and laminar in arrangement in the fifth and sixth cortical layers and had a close relationship to the neuronal loss. There was no spongiform change in the cerebral cortex or cerebellum. The cerebellum was almost intact except for a few amyloid plaques. Ultrastructurally, some of the plaques simulated kuru plaques and others had many degenerated neurites possessing paired helical filaments and other accumulated organelles. GSS has been proposed to include cases with progressive ataxia, dementia and massive multifocal plaques in the brain with or without cerebral spongiform changes. The case presented here is a very peculiar case of GSS. Recently, similar cases have been reported in some large families, diagnosed as familial Alzheimer's disease. These cases may be a telencephalic form with numerous NFTs of GSS.- - - - - - - - - - ranking = 2.0002489993835keywords = spongiform, variant (Clic here for more details about this article) |
9/18. A prion protein variant in a family with the telencephalic form of Gerstmann-Straussler-Scheinker syndrome.We present a patient with a mutation in the open reading frame of the prion protein gene (PRNP), which results in substitution of valine for alanine at codon 117. The patient is a member of a large American kindred of German descent with the telencephalic form of Gerstmann-Straussler-Scheinker syndrome (GSS). Two other affected members of this kindred carried this mutation, as inferred from haplotypes of their offspring and spouses. The mutation was absent in one member with a protracted neurologic illness that differed from the other affected members' illnesses. The identification of a distinct PRNP mutation in the telencephalic form of GSS supports the hypothesis that allelic forms of PRNP may correspond to distinct clinical disease entities.- - - - - - - - - - ranking = 0.00033199917805496keywords = variant (Clic here for more details about this article) |
10/18. Report on the first Chinese family with gerstmann-straussler-scheinker disease manifesting the codon 102 mutation in the prion protein gene.The authors found a female patient aged 33-years with dementia and cerebellar ataxia rapidly progressing for a year. EEG tracings were abnormal but without features of typical CJD. The patient died 13 months after the onset of illness. biopsy of her cerebral cortex showed moderate spongiform changes, neuronal loss and gliosis. Numerous deposits of eosinophilic substance amorphous or in the shape of kuru plaques were disclosed in the cerebral cortex. All deposits stained strongly with monoclonal 3F4 antibody to human prion protein. Genetic studies disclosed the Pro to Leu point mutation at codon 102 with a 102 Leu-129 Met in the PrP gene. codon 129 was heterozygous for Met/Val, and codon 219 was homozygous for Glu/Glu. It was established; moreover, that the patient's grandfather had a similar disease and died at age 48 and the patient's brother died after a 10-year long neurological disease diagnosed as hereditary cerebellar ataxia. On the basis of clinical, neuropathological and genetic findings, the authors diagnosed the gerstmann-straussler-scheinker disease, a familial prion disease with an autosomal dominant character. This is the first report on this disease in china.- - - - - - - - - - ranking = 0.99991700020549keywords = spongiform (Clic here for more details about this article) |
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