Biology:Extracellular chaperone
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
- ↑ Braun, Janice E. A. (February 2023). "Extracellular chaperone networks and the export of J-domain proteins". The Journal of Biological Chemistry 299 (2). doi:10.1016/j.jbc.2022.102840. ISSN 1083-351X. PMID 36581212.
- ↑ 2.0 2.1 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. 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" (in en). Protein Science 30 (11): 2272–2286. doi:10.1002/pro.4189. ISSN 1469-896X. PMID 34553437.
- ↑ West, Jennifer; Satapathy, Sandeep; Whiten, Daniel R.; Kelly, Megan; Geraghty, Nicholas J.; Proctor, Emma-Jayne; Sormanni, Pietro; Vendruscolo, Michele et al. (2021-12-10). "Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation". Science Advances 7 (50). doi:10.1126/sciadv.abf7606. PMID 34890220.
- ↑ "How 'extracellular chaperones' help remove abnormal proteins" (in en). https://phys.org/news/2023-05-extracellular-chaperones-abnormal-proteins.html.
 |  |
