Evidence of Rapid Coaggregation of Globular Proteins
during Amyloid Formation
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Abstract
The
question of how an aggregating protein can influence aggregation
of other proteins located in its vicinity is particularly significant
because many proteins coexist in cells. We demonstrate <i>in
vitro</i> coaggregation and cross-seeding of lysozyme, bovine
serum albumin, insulin, and cytochrome <i>c</i> during their
amyloid formation. The coaggregation process seems to be more dependent
on the temperature-induced intermediate species of these proteins
and less dependent on their sequence identities. Because amyloid-linked
inclusions and plaques are recognized as multicomponent entities originating
from aggregation of the associated protein, these findings may add
new insights into the mechanistic understanding of amyloid-related
pathologies