In medicine, the term proteopathy (proteo [protein pref.] - patia [disease suff.]) Refers to a class of diseases in which some proteins become structurally abnormal and therefore compromise the cellular action, of the tissues and organs that contain them.
Often, proteins fail to fold back into their normal configuration; in this unfolded state, they can somehow become toxic or can simply lose their function.
The proteopathies (also known as proteinopathies, conformational disorders of proteins or diseases of the protein deployment) also include certain pathologies such as: Alzheimer's disease, Parkinson's disease, prion disease (eg BSE), type diabetes mellitus 2, amyloidosis and many others.
Discovery of Proteopathies
The concept of proteopathy has its origins in the mid-nineteenth century when, in 1854, Rudolf Virchow coined the term "amyloid" for the association of a chemical reaction observed in the "corpora amilacea" to vegetable cellulose. In 1859, Friedreich and Kekulé showed that, rather than cellulose, amyloid is instead made of protein.
Subsequent research has shown that amyloid is made up of many different and combined proteins. Moreover, all amyloids have the same birefringence (optical property) at the cross-polarization of light after the “Rosso Congo” coloration; amyloids also use a fibrillar ultrastructure (if observed with an electronic microscope).
However, some protein lesions (proteopathies) lack birefringence and contain little or no amyloid fibrils; a very indicative example is represented by A-beta protein deposits in the brains of Alzheimer's patients.
Furthermore, it emerged that the small non-fibrillar protein aggregates known as "oligomers" are toxic to the cells of any affected organ. Moreover, the amyloid-genic proteins, if in their fibrillar (normal) form, can be relatively benign.
