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Books > Science & Mathematics > Biology, life sciences > Biochemistry > Proteins
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Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases (Hardcover, 2012 ed.)
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Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases (Hardcover, 2012 ed.)
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Amyloid-forming proteins are implicated in over 30 human diseases.
The proteins involved in each disease have unrelated sequences and
dissimilar native structures, but they all undergo conformational
alterations to form fibrillar polymers. The fibrillar assemblies
accumulate progressively into disease-specific lesions in vivo.
Substantial evidence suggests these lesions are the end state of
aberrant protein folding whereas the actual disease-causing
culprits likely are soluble, non-fibrillar assemblies preceding the
aggregates. The non-fibrillar protein assemblies range from small,
low-order oligomers to spherical, annular, and protofibrillar
species. Oligomeric species are believed to mediate various
pathogenic mechanisms that lead to cellular dysfunction,
cytotoxicity, and cell loss, eventuating in disease-specific
degeneration and systemic morbidity. The particular pathologies
thus are determined by the afflicted cell types, organs, systems,
and the proteins involved. Evidence suggests that the oligomeric
species may share structural features and possibly common
mechanisms of action. In many cases, the structure function
interrelationships amongst the various protein assemblies described
in vitro are still elusive. Deciphering these intricate structure
function correlations will help understanding a complex array of
pathogenic mechanisms, some of which may be common across different
diseases albeit affecting different cell types and systems."
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