Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins.

The 37 kDa/67 kDa laminin receptor LRP/LR acts as a receptor for both PrPc and PrPSc at the cell surface. Here, we further analyzed the subcellular localization of fluorescent labeled prion protein (PrP) and laminin receptor (LRP/LR) molecules. We show that EGFP-PrP is localized at the cell surface and in a perinuclear compartment, respectively.

Therapeutic approaches for prion disorders.

Prion diseases are lethal for both humans and animals, and affected individuals die after several months following a rapid disease progression. Although researchers have attempted for decades to develop effective therapeutics for the therapy of human prion disorders, until now no efficient drug has been available on the market for transmissible spongiform encephalopathy (TSE) treatment or cure. Approximately 200 patients worldwide have died or suffer from variant Creutzfeldt-Jakob disease (CJD).

Therapeutic approaches targeting the prion receptor LRP/LR.

Transmissible spongiform encephalopathies known as prion diseases are a group of fatal neurodegenerative disorders that affect both humans and animals. The generally accepted principle of the disease is that the conversion of the cellular prion protein (PrP(c)) into the disease associated isoform PrP(Sc) leads to spongiform degeneration of the brain and amyloid plaque formation. Until now no therapy leading to potential alleviation or even cure of the disease exists.