Introduction

Prion diseases, or transmissible spongiform encephalopathies (TSE), are caused by an innate protein that has been folded incorrectly. It is beleived that exposure to the abnormally folded protein (PrPsc) can cause the normal proteins (PrPc) present to take on the conformation of the rouge protein, which cannot be degraded by proteinases. There are both infectious and genetic causes of the various spongiform encephalopathies in humans, while the animal kingdom has TSE diseases affecting sheep, cows, elk, deer, and mink. Diseases such as Creutzfeldt-Jakob disease (CJD) and Fatal familial insomnia (FFI) have been found to be genetic, while new variant CJD and the now extinct Kuru are both linked to consumption of the abnormal protein. This "chain reaction" causes accumulation of plaques in the brain, termed spongy changes, to encroach on the normal tissues and dementia ensues. Normally, once symptoms such as abnormal gait, altered cognition, and speech problems begin, the life-expectancy of the patient is only three to six months. One of the mysteries of the disease is how the aberrant protein crosses the blood brain barrier (BBB) and begins to alter the normal proteins, though studies have shown the immune system plays a critical role in chaperoning the PrPsc proteins into the brain from the blood.

Laboratories Investigating Prion Diseases & the Role of the Blood Brain Barrier

• The Institute for Neurpathology at the University of Zurich
  
• Dr. Ma's Laboratory in the Department of Molecular and Cellular Biochemistry at Ohio State University