Some prion protein mutations create anchorless molecules that cause Gerstmann-Sträussler-Scheinker (GSS) disease. To model GSS, we generated transgenic mice expressing cellular prion protein (PrP(C)) lacking the glycosylphosphatidyl inositol (GPI) anchor, denoted PrP(ΔGPI). Mice overexpressing PrP(ΔGPI) developed a late-onset, spontaneous neurologic dysfunction characterized by widespread amylo...

OBJECTIVE The objective of this investigation was to establish the effectiveness of sustained-release platelet-rich plasma (PRP) on perfusion and neovascularization in diabetic murine hind limb ischemia. METHODS After surgery in streptozotocin-induced diabetic mice, the mice were randomly assigned to the following 4 experimental groups: control (C), 100 μl of the sustained-release form of pla...

BACKGROUND Prion diseases are associated with a conformational switch for PrP from PrP(C) to PrP(Sc). Many genetic mutations are linked with prion diseases, such as mutations T188K/R/A with fCJD. SCOPE OF REVIEW MD simulations for the WT PrP and its mutants were performed to explore the underlying dynamic effects of T188 mutations on human PrP. Although the globular domains are fairly conserv...

Prions are formed of misfolded assemblies (PrP(Sc)) of the variably N-glycosylated cellular prion protein (PrP(C)). In infected species, prions replicate by seeding the conversion and polymerization of host PrP(C). Distinct prion strains can be recognized, exhibiting defined PrP(Sc) biochemical properties such as the glycotype and specific biological traits. While strain information is encoded ...

The cellular prion protein PrP C confers susceptibility to transmissible spongiform encephalopathies, yet its normal function is unknown. Although PrP -deficient mice develop and live normally, expression of amino proximally truncated PrP C ( PrP) or of its structural homolog Doppel (Dpl) causes cerebellar degeneration that is prevented by coexpression of full-length PrP . We now report that mi...

Amyloid fibrils in Gerstmann-Sträussler-Scheinker (GSS) disease are composed of a fragment of the prion protein (PrP), the N and C termini of which correspond to ragged residues 81-90 and 144-153. A synthetic peptide spanning the sequence 82-146 (PrP 82-146) polymerizes into protease-resistant fibrils with the tinctorial properties of amyloid. We investigated the biological activity of PrP 82-1...

OBJECTIVE Dressing is an important activity of daily living, yet many older adults have difficulty due to impairments. The purpose of this study was to explore the use of assistive devices for dressing by older persons with impairments, and to look at differences among frail elders with no dressing difficulty, upper-extremity-only dressing difficulty, lower-extremity-only dressing difficulty, a...

Only a few cell lines have been infected with prions, offering limited genetic diversity and sensitivity to several strains. Here we report that cultured neurospheres expressing cellular prion protein (PrP(C)) can be infected with prions. Neurosphere lines isolated from the brains of mice at embryonic day 13-15 grow as aggregates and contain CNS stem cells. We produced neurosphere cultures from...

Prion diseases are fatal neurodegenerative disorders characterized by the accumulation of prion protein (PrP(C)). To date, there is no effective treatment for the disease. The accumulated PrP, termed PrP(Sc), forms amyloid fibrils and could be infectious. It has been suggested that PrP(Sc) is abnormally folded and resistant to proteolytic degradation, and also inhibits proteasomal functions in ...