When looking at the damaged nerve cells of an Alzheimer’s patient under a microscope, one observes clumps of proteins that seem out of place.  Researchers have discovered these protein masses behave much like prions – malformed proteins normally found in healthy neurons.  These contorted proteins in turn cause like proteins to misfold and bind to one another, resulting in a chain reaction or cascade that destroys entire regions of the brain.  Prions are most commonly associated with the contagious neurodegenerative mad cow disease, however all evidence suggests Alzheimer’s and Parkinson’s lack the infectious agent of classic prion diseases.  Regardless, these recent findings provide scientists with a “signpost” for neurodegenerative diseases that may point toward eventual treatment options for the millions of patients suffering around the world.

 While research into human neurodegenerative diseases show that they are not contagious, they spread via a similar process, known as pathogenic protein seeding.  This process involves the release and uptake of proteinaceuous seeds among neurons that contribute to the proliferation of the disease from one area of the brain to another.  The clumping of proteins is also understood to involve two major microscopic abnormalities in the brain, senile plaques and neurofibrillary tangles.  In these processes proteins aggregations are able to disable and damage normal cells in a variety of ways, ranging from the release of harmful toxins, to blocking normal proteins from finding the sites where they function properly.  Prion-like seeded protein accumulation may help to explain the origins of some of humanity’s most feared and merciless illnesses and may provide a signature that future treatment options can utilize.