Extracellular chaperones and proteostasis

Amy R. Wyatt, Justin J. Yerbury, Heath Ecroyd, Mark R. Wilson

Research output: Contribution to journalReview articlepeer-review

83 Citations (Scopus)


There exists a family of currently untreatable, serious human diseases that arise from the inappropriate misfolding and aggregation of extracellular proteins. At present our understanding of mechanisms that operate to maintain proteostasis in extracellular body fluids is limited, but it has significantly advanced with the discovery of a small but growing family of constitutively secreted extracellular chaperones. The available evidence strongly suggests that these chaperones act as both sensors and disposal mediators of misfolded proteins in extracellular fluids, thereby normally protecting us from disease pathologies. It is critically important to further increase our understanding of the mechanisms that operate to effect extracellular proteostasis, as this is essential knowledge upon which to base the development of effective therapies for some of the world's most debilitating, costly, and intractable diseases.

Original languageEnglish
Pages (from-to)295-322
Number of pages28
JournalAnnual Review of Biochemistry
Publication statusPublished - 1 Jun 2013


  • Clearance
  • Extracellular chaperones
  • Protein deposition diseases
  • Protein folding
  • Proteostasis


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