Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.

ABSTRACT:

Background

Proteolytic processing of the prion protein (PrPC) by endogenous proteases generates bioactive membrane-bound and soluble fragments which may help to explain the pleiotropic roles of this protein in the nervous system and in brain diseases. Shedding of almost full-length PrPC into the extracellular space by the metalloprotease ADAM10 is of peculiar relevance since soluble PrP stimulates axonal outgrowth and is protective in neurodegenerative conditions such as Alzheimer’s and prion disease. However, molecular determinates and mechanisms regulating the shedding of PrP are entirely unknown.

Methods

We produced an antibody recognizing the neo-epitope of shed PrP generated by ADAM10 in biological samples and used i

SUBMITTER: Linsenmeier L 

PROVIDER: S-EPMC5889536 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature