Discovery of the Extracellular Agonist Actions of Molecular Chaperones and Protein-Folding Catalysts

Chapter
Part of the Heat Shock Proteins book series (HESP, volume 6)

Abstract

Surprisingly, the history of the agonist actions of extracellular molecular chaperones can be traced back to the 1970s, with the cytokine macrophage migration inhibitory factor (MIF) and chaperonin (Hsp)10. The next cell stress protein to be identified as a molecular chaperone was the peptidylprolyl isomerase, cyclophilin A, in 1992. It is only later in the 1990s that the major signalling cell stress proteins—chaperonin (Hsp)60 and Hsp70 are found to have agonist activities. There are still ongoing discoveries of stress proteins with agonist actions and the latest such proteins are a new group of molecular chaperones—the extracellular/circulating molecular chaperones which include clusterin and α-acid1-glycoprotein.

Keywords

Molecular chaperones Cytokines Inflammation Hsp10 Hsp27 Hsp60 Hsp70 MiF 

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© Springer Science+Business Media Dordrecht 2012

Authors and Affiliations

  1. 1.Department of Microbial Diseases, UCL-Eastman Dental InstituteUniversity College LondonLondonUK

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