Extracellular chaperone (ECs) are a type of chaperone protein that resides outside of cells in extracellular space such as blood plasma. They are secreted out of cells. Their function is to protect and assist in protein folding for a diverse array of proteins in this space. Their role is vital as proteins in extracellular space can easily aggregate and unfold.[1] Examples of extracellular chaperones include J-___domain proteins, Clusterins (CLU), Haptoglobin (HP), α2-macroglobulin (a2m) and many others.[2][3]
They can interact with invading pathogens and the immune system response including the complementary pathway.[2] Some extracellular chaperones such as neuroserpin and transthyretin also inhibit amyloid formation which causes many neurodegenerative diseases such as Alzheimers or Parkinson’s disease.[4] Because of their role in the cleanup of misfolded and aggregated proteins and their interactions with the immune system, they are valuable in medical research. They can be used to potentially treat neurodegenerative diseases.[5]
References
edit- ^ Braun, Janice E. A. (February 2023). "Extracellular chaperone networks and the export of J-___domain proteins". The Journal of Biological Chemistry. 299 (2) 102840. doi:10.1016/j.jbc.2022.102840. ISSN 1083-351X. PMC 9867986. PMID 36581212.
- ^ a b Geraghty, Nicholas J.; Satapathy, Sandeep; Wilson, Mark R. (2022-12-02). "The Emerging Roles of Extracellular Chaperones in Complement Regulation". Cells. 11 (23): 3907. doi:10.3390/cells11233907. ISSN 2073-4409. PMC 9738919. PMID 36497163.
- ^ Geraghty, Nicholas J.; Satapathy, Sandeep; Kelly, Megan; Cheng, Flora; Lee, Albert; Wilson, Mark R. (2021). "Expanding the family of extracellular chaperones: Identification of human plasma proteins with chaperone activity". Protein Science. 30 (11): 2272–2286. doi:10.1002/pro.4189. ISSN 1469-896X. PMC 8521303. PMID 34553437.
- ^ West, Jennifer; Satapathy, Sandeep; Whiten, Daniel R.; Kelly, Megan; Geraghty, Nicholas J.; Proctor, Emma-Jayne; Sormanni, Pietro; Vendruscolo, Michele; Buxbaum, Joel N.; Ranson, Marie; Wilson, Mark R. (2021-12-10). "Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation". Science Advances. 7 (50): eabf7606. doi:10.1126/sciadv.abf7606. PMC 8664251. PMID 34890220.
{{cite journal}}: CS1 maint: article number as page number (link) - ^ "How 'extracellular chaperones' help remove abnormal proteins". phys.org. Retrieved 2025-08-06.
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