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Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms.

Wyatt A.R., Constantinescu P., Ecroyd H., Dobson C.M., Wilson M.R., Kumita J.R., Yerbury J.J.

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 distinct mechanisms: (i) by trapping proteases that remain able to degrade polypeptide chains and (ii) by a chaperone action that prevents misfolded clients from continuing along the amyloid forming pathway.

FEBS Lett. 587:398-403(2013) [PubMed] [Europe PMC]

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