Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity.

@article{French2008ProteaseAO,
  title={Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity.},
  author={Katie French and Justin J Yerbury and Mark R. Wilson},
  journal={Biochemistry},
  year={2008},
  volume={47 4},
  pages={1176-85}
}
Alpha2-macroglobulin (alpha2M) 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 alpha2M with an exposed binding site for the low-density lipoprotein receptor, facilitating clearance of alpha2M/protease complexes from the body. This report establishes that protease activation also modulates a potent chaperone-like action of alpha2M that has broad specificity for… CONTINUE READING

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