Introduction
Abnormally-folded proteins occur in several diseases that affect humans and animals, known as prion diseases. Prion diseases include
sporadic and variant Creutzfeldt-Jakob disease (CJD), Kuru, bovine spongiform encephalopathy (BSE, or mad cow disease), scrapie, and
chronic wasting disease (CWD). Known prion diseases result in
progressive neurodegenerative disease, leading to early death. Alzheimer’s disease (AD),
Parkinson’s disease (PD), and Amyotrophic lateral sclerosis (ALS) are
also considered by many as under the umbrella of prion disease, because
of the observed parallels between members of the entire group (1).
Accordingly, an understanding of traditional transmissible spongiform
encephalopathies (TSE) is likely to contribute significantly to an
improved understanding of the more frequently seen Alzheimer's disease, Parkinson's disease,
and Amyotrophic lateral sclerosis (ALS), which in total affect millions of individuals worldwide. Similarly, an
improvement in the understanding of the pathogenesis of AD, PD, or ALS
may provide significant insight into the entire group of prion diseases.
Unfortunately the mechanism of protein misfolding in both human and
animal diseases has remained poorly understood, and there has been
little progress to date in improving outcomes (1).
The protein-only hypothesis has provided for many valuable steps in
understanding, although there remains a further need for a more complete
model of the mechanism of protein misfolding. Novel theories, such as
that described herein, may provide alternative and adjunctive
explanations that can improve our understanding of all prion diseases.
The mineral-lipid hypothesis has been described in a previous manuscript and represents a novel theory to explain the formation and propagation
of prions (1). The aim of this shorter manuscript is to expand this hypothesis to consider whether it may represent a special case, or
particular example of, a more encompassing “Lipid-Carrier
Initiator” prion theory, which is described herein.