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Protease Activation Of A2-Macroglobulin Modulates A Chaperone-Like Action With Broad Specificity, Katie French, Justin Yerbury, Mark Wilson

Mark R Wilson

α2-Macroglobulin (α2M) is a major human blood glycoprotein best known for its ability to inhibit a broad spectrum of proteases by a unique trapping method. This action induces an “activated” conformation of α2M with an exposed binding site for the low density lipoprotein receptor, facilitating clearance of α2M-protease complexes from the body. This report establishes that protease activation also modulates a potent chaperone-like action of α2M which has broad specificity for proteins partly unfolded as a result of heat or oxidative stress. Protease-mediated activation of α2M abolishes its chaperone-like activity. However, native α2M is able to form soluble complexes with …