gerstmann-straussler-scheinker disease/protease

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Molecular analysis of the protease-resistant prion protein in scrapie and bovine spongiform encephalopathy transmitted to ovine transgenic and wild-type mice.

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The existence of different strains of infectious agents involved in scrapie, a transmissible spongiform encephalopathy (TSE) of sheep and goats, remains poorly explained. These strains can, however, be differentiated by characteristics of the disease in mice and also by the molecular features of the

In situ formation of protease-resistant prion protein in transmissible spongiform encephalopathy-infected brain slices.

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The transmissible spongiform encephalopathies (TSEs) comprise a group of fatal neurodegenerative diseases that are characterized by the conversion of the normal host cellular prion protein (PrPC), to the abnormal protease-resistant prion protein isoform (PrP-res). It has been proposed, though not

Relationship of protease-resistant protein, scrapie-associated fibrils and tubulofilamentous particles to the agent of spongiform encephalopathies.

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Tubulofilamentous particles and scrapie-associated fibrils (SAF) are ultrastructural markers, while protease-resistant protein (PrP) is a molecular biological marker for all spongiform encephalopathies. Review of all published work has suggested that PrP molecules aggregate to form a

Protease-resistant PrP deposition in brain and non-central nervous system tissues of a murine model of bovine spongiform encephalopathy.

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Infectivity within the central nervous system has been demonstrated by the transmission of bovine spongiform encephalopathy (BSE) from affected cattle to inbred laboratory mice. Sedimentable, protease-resistant PrP (PrPSc) has also been extracted from BSE-affected cattle brain. Both infectivity and

Regression of HIV encephalopathy and basal ganglia signal intensity abnormality at MR imaging in patients with AIDS after the initiation of protease inhibitor therapy.

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OBJECTIVE To determine whether protease inhibitors cause regression of periventricular white matter signal intensity abnormalities in patients with human immunodeficiency virus (HIV) encephalopathy and whether the changes on magnetic resonance (MR) images correlate with cognitive

Molecular typing of protease-resistant prion protein in transmissible spongiform encephalopathies of small ruminants, France, 2002-2009.

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The agent that causes bovine spongiform encephalopathy (BSE) may be infecting small ruminants, which could have serious implications for human health. To distinguish BSE from scrapie and to examine the molecular characteristics of the protease-resistant prion protein (PrP(res)), we used a

Stability properties of PrP(Sc) from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay.

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BACKGROUND Transmissible Spongiform Encephalopathies (TSEs), including scrapie in sheep, chronic wasting disease (CWD) in cervids, transmissible mink encephalopathy (TME), and bovine spongiform encephalopathy (BSE), are fatal diseases of the nervous system associated with accumulation of misfolded

Spongiform encephalopathy in siblings with no evidence of protease-resistant prion protein or a mutation in the prion protein gene.

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We discuss relevant aspects in two siblings with a neurodegenerative process of unclear aetiology who developed progressive dementia with global aphasia and hyperoral behaviour at the ages of 39 and 46 years and who died 6 and 5 years after disease onset. The cases were reported to the National

Phenotypic similarity of transmissible mink encephalopathy in cattle and L-type bovine spongiform encephalopathy in a mouse model.

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Transmissible mink encepholapathy (TME) is a foodborne transmissible spongiform encephalopathy (TSE) of ranch-raised mink; infection with a ruminant TSE has been proposed as the cause, but the precise origin of TME is unknown. To compare the phenotypes of each TSE, bovine-passaged TME isolate and 3

Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy.

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The development of transmissible spongiform encephalopathies in experimental models depends on two major factors: the intracerebral accumulation of an abnormal, protease-resistant isoform of PrP (PrPres), which is a host protein mainly expressed in neurons; and the existence of different strains of

N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro.

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Transmissible spongiform encephalopathy diseases are characterized by conversion of the normal protease-sensitive host prion protein, PrP-sen, to an abnormal protease-resistant form, PrP-res. In the current study, deletions were introduced into the flexible tail of PrP-sen (23) to determine if this

USP8 ameliorates cognitive and motor impairments via microglial inhibition in a mouse model of sepsis-associated encephalopathy.

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Sepsis-associated encephalopathy (SAE) is a common and serious complication of sepsis, which is thought to be caused by neuroinflammation. In our previous study, ubiquitin-specific protease 8 (USP8), was reported to regulate inflammation in vitro. In the current study, we investigated whether

A prion disease--possible Gerstmann-Straussler-Scheinker disease: a case report.

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A 50-year-old patient with a 6-month history of progressive cognitive and motor disability is presented. There were no myoclonic jerks on examination and no periodic sharp waves by electroencephalography. Imaging showed high signal on T2-weighted scans in the basal ganglia and posterior limbs of the

[182 offspring of cows with bovine spongiform encephalopathy (BSE) in Switzerland. 2. Epidemiology and pathological findings].

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In order to detect lesions of a spongiform encephalopathy and/or accumulation of the protease resistant prion protein (PrPres), 182 offspring of cows affected with BSE were examined neuropathological and immunohistochemically. Neither spongiform encephalopathy nor PrPres accumulation were found. In

A critical review of the nature of the spongiform encephalopathy agent: protein theory versus virus theory.

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All spongiform encephalopathies (SEs) result in brain disorders brought about by a slow virus. Since the origin of bovine SE (BSE), the infectious nature of the disease has been firmly established. Tubulofilamentous particles/scrapie termed nemavirus (NVP) and scrapie-associated fibrils (SAF) are

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