Ontology highlight
ABSTRACT:
SUBMITTER: Wyatt AR
PROVIDER: S-EPMC3581772 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
FEBS letters 20130123 5
α(2)-Macroglobulin (α(2)M) is an extracellular chaperone that inhibits amorphous and fibrillar protein aggregation. The reaction of α(2)M with proteases results in an 'activated' conformation, where the proteases become covalently-linked within the interior of a cage-like structure formed by α(2)M. This study investigates, the effect of activation on the ability of α(2)M to inhibit amyloid formation by Aβ(1-42) and I59T human lysozyme and shows that protease-activated α(2)M can act via two disti ...[more]