Giampaolo Merlini, Vittorio Bellotti, Alessia Andreola, Giovanni Palladini, Laura Obici, Simona Casarini, Vittorio Perfetti
Protein Aggregation
Protein aggregation occurs in vivo as a result of improper
folding or misfolding. Diverse diseases arise
from protein misfolding and are now grouped under the
term “protein conformational diseases”, including
most of the neurodegenerative disorders such as
Alzheimer's disease, Parkinson's disease, the prion encephalopathies
and Huntington's disease, as well as
cystic fibrosis, sickle cell anemia and other less common
conditions. The hallmark event in these diseases is
a change in the secondary and/or tertiary structure of a
normal, functional protein, leading to the formation of
protein aggregates with various supramolecular organizations.
In most cases the aggregates are organized in
structurally well-defined fibrils forming amyloid deposits.
The crucial feature of the amyloidogenic proteins
is their structural instability induced either by
mutations, post-translational modifications, or local
conditions, such as pH, temperature, and co-solutes.
The conformational change may promote the disease
either by gain of a toxic activity or by the lack of biological
function of the natively folded protein. As different
molecular mechanisms are involved in the formation of
the various forms of protein aggregates, the laboratory
diagnostic approach remains frequently elusive.
Clinical Chemical Laboratory Medicine, Walter de Gruyter
Print ISSN: 1434-6621
Volume: 39, 11/2001
Pages: 1065 - 1075
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