Endoproteolysis is a normal post-translational process in the eukaryotic
cell that plays a role in protein evolution allowing protein catabolism and the
generation of amino acids. Endoproteolytic cleavage regulates many crucial cellular
processes including the activity of many proteins, their protein-protein interactions
and the amplification of cell signals. Not surprisingly, disruption or alternation of
endoproteolytic cleavage may be the root cause of many human diseases such as
Alzheimer’s disease, Huntington’s disease and prion diseases. Most
neurodegenerative diseases (ND) are caused by the build-up of misfolded proteins
and the promotion of aggregation events. A common event that occurs in these ND
is the alteration of endoproteolytic cleavage due to genetic mutations of the
associated-proteases or target substrate. Endoproteolytic cleavage resulting in protein truncation has
significant effects on the structure and function of a protein representing a common feature of ND. In
this review, we will discuss the endoproteolytic cleavage events that lead to ND, namely Alzheimer’s
disease, Huntington’s disease and prion diseases.
Keywords: Alzheimer’s disease, endoproteolytic cleavage, huntington’s disease, prion disease.
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