Amplified Molecular Binding of Prion Protein Homologues in Self-Progressive Injury of Neuronal Membranes and Trafficking Systems
Prion particles might be viewed as essential sources of cyclical coupling and uncoupling of depolarization and repolarization of the neuronal plasmalemma. In terms of different parametric functions, the cellular PrPc, both as a source and also a mediated means of induced replication of the Prion particle PrPsc, would be considered in terms of agent amplification as induced by the bovine host. One might view bovine spongiform disease as a source of variant Creutzfeldt-Jakob disease in the human that would involve such amplified uncoupling of membrane-based phenomena of ion-determined polarization events. It would, in addition, appear that a spongiform change of neurons that progresses in conjunction with neuropil alterations and as a primarily self-amplified system of spreading progression in the brain would necessarily constitute a reactive series of cell injury. It is indeed in terms of a neuronal reactivity linked, for example, to mitochondrial overactivity and also to perhaps nucleotide inserts within neurons that one might consider species specificity of prion particle transmission a host-based series of events giving rise to and constituting also a final expression of disease process events.It might be realistic to consider interspecies transmissibility, and once this occurs, a fundamental pathway of evolutionary adaptability that arises and progresses simply in terms of progressively amplified reactivity.Reactivity to neuronal injury would appear an integral system of self-progression based on a primary and also a series of secondary changes that evolve in terms of a PrPc particle that itself promotes self-conversion to PrPsc. Indeed, conformational changes to PrPsc might be defined as a system disorder of neuronal reactivity that self-progresses as amplified progressiveness of the neuronal injury.