In the alternative conformation, PrP-sc, the protein loses its functionality and becomes proteinease resistant. It also gains the ability to somehow catalyse the conversion of normal PrP into PrP-sc. PrP can also aggregate to form plaques and other structures characteristic of spongiform encephalopathies. So much so, that relevant research elsewhere has perhaps been overlooked in the rush to understand the mechanism of the disease. I would like to put forward the hypothesis here that, when looked at as inherited disorders, prion diseases show close similarity to another class of genetic disorders, the lysosomal storage diseases.
Lysosomes are membrane-bound organelles responsible for turnover of cellular components.
This leads to an increase in size and number of the lysosomes, eventually resulting in malfunction of the affected organ or organs. There are currently 36 different types of LSD, some of which exhibit neurological involvement due to the effect of the cellular pathology on the nervous system. The course of each disease is determined by where the substrate accumulates fastest. For example glycogen accumulation is likely to primarily affect muscle tissue. All of the LSDs are serious conditions and most of them are fatal, resulting in death in infancy or early childhood.