Transmission and Scanning Electron Microscopy of Spongiform Change in Creutzfeldt-Jakob Disease

Chou, S. M.; Payne, W. N.; Gibbs, C. J.; Gajdusek, D. Carleton

doi:10.1093/brain/103.4.885

Cited by 41 publications

(6 citation statements)

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“…The vacuoles observed by light microscopy represent focal swellings of axonal and dendritic neuronal processes associated with the loss of synaptic organelles, and accumulation of abnormal membranes by electron microscopy. [22][23][24] They may be distributed throughout the gray and white matter but are generally most prominent in the gray matter neuropil. They typically range in size from 5 to 25 μm but in advanced cases they may be as large as 100 μm.…”

Section: Pathologic Features Of Prion Diseasesmentioning

confidence: 99%

Prion Diseases

Mastrianni

2015

Rosenberg's Molecular and Genetic Basis of Neurological and Psychiatric Disease

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Section: Pathologic Features Of Prion Diseasesmentioning

confidence: 99%

Prion Diseases

Mastrianni

2015

Rosenberg's Molecular and Genetic Basis of Neurological and Psychiatric Disease

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“…The clinical signs are confined to the central nervous system, and no immune response seems to accompany the progression of the illness [9]. The molecular basis of neurological dysfunction in prion diseases is not known, although there is evidence that spongiform degeneration and death of neurons is related to the accumulation of PrP Sc , which causes alterations in membrane receptors or ion channels functions, among other effects [12,13]. Kristensson et al [14] reported that prion infection of cultured mouse neuroblastoma cells affected intracellular Ca# + regulation, inducing abnormalities in intracellular Ca# + release from internal stores and influx of extracellular Ca# + .…”

Section: Introductionmentioning

confidence: 99%

Activation effects of a prion protein fragment [PrP-(106-126)] on human leucocytes

Diomede

Sozzani

Luini

et al. 1996

Biochemical Journal

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Prion-related encephalopathies are characterized by the intracerebral accumulation of an abnormal isoform of the cellular prion protein (PrPC) named scrapie prion protein (PrPSc). The pathological forms of this protein and its cellular precursor are not only expressed in the brain but also, at lower concentrations, in peripheral tissues. We recently showed that a synthetic peptide corresponding to residues 106-126 [PrP-(106-126)] of the human PrP is toxic to neurons and trophic to astrocytes in vitro. Our experiments were aimed at verifying whether PrP-(106-126) and other peptides corresponding to fragments of the amyloid protein purified from brains of patients with Gerstmann-Sträussler-Scheinker disease-namely PrP-(89-106), PrP-(106-114), PrP-(127-147)-were capable of stimulating circulating leucocytes. Native PrP expression in human lymphocytes, monocytes and neutrophils was first confirmed using PCR amplification of total RNA, after reverse transcription, and immunoblot analysis of cell extracts with anti-PrP antibodies. PrP-(106-126), but not the other peptides, increased membrane microviscosity, intracellular Ca2+ concentration and cell migration in circulating leucocytes, and O2-. production in monocytes and neutrophils. Membrane microviscosity was determined by the fluorescence polarization technique, using diphenylhexatriene as a probe, 300 s after the addition of PrP-(106-126) to the cell suspension in the concentration range 5-50 microM. The increase in intracellular Ca2+ elicited by PrP-(106-126) was dose-dependent in the range 5-500 microM. PrP-(106-126) stimulated O2-. production in monocytes and neutrophils in a dose- (10-300 microM) and time-(5-30 min) dependent manner in the presence of 10 microM dihydrocytochalasin B. Both the increase in Ca2+ concentration and the O2-. production were partially sensitive to pertussis toxin. PrP-(106-126) stimulated leucocyte migration in a dose-dependent (30-300 microM) manner and, at the highest concentration used, this migration was comparable with that elicited by 2.5 nM interleukin 8 or 10 nM fMet-Leu-Phe peptide.

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“…J-C disease is classified as one of subacute spongiform encephalopathies. 4 These represent a group of transmissible encephalopathies caused by unknown agents considered by some observers to represent unconventional viruses. 5,6 They have a long incubation period of many months or years and a characteristic, unremitting always fatal course.…”

Section: Discussionmentioning

confidence: 99%

Jakob-Creutzfeldt Disease Associated with Wernicke Encephalopathy

Gaytan-Garcia

Gilbert

Deck

et al. 1988

Can. j. neurol. sci.

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ABSTRACT:Wernicke disease (WD) is a complication of alcoholism and malnutrition and usually presents acutely and is characterized by disturbances of consciousness, paralysis of the external ocular muscles, and ataxia. The disease results from deficiency of vitamin B 1, or thiamine, an essential coenzyme in intermediate carbohydrate metabolism. On the other hand, Jakob-Creutzfeldt disease (J-C) results from infection with an unconventional agent with a long incubation period and is characterized by a rapidly progressive dementia and histologically by a spongiform encephalopathy associated with neuronal destruction and pronounced astrogliosis. Combination of both diseases has not been reported in the literature previously and their relationship is uncertain. We present 3 cases with this interesting association and consider their relationship.

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Transmission and Scanning Electron Microscopy of Spongiform Change in Creutzfeldt-Jakob Disease

Cited by 41 publications

References 0 publications

Prion Diseases

Prion Diseases

Activation effects of a prion protein fragment [PrP-(106-126)] on human leucocytes

Jakob-Creutzfeldt Disease Associated with Wernicke Encephalopathy

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