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Comment
. 2013 Aug;123(8):3206-8.
doi: 10.1172/jci70799.

The future of molecular chaperones and beyond

Rona G Giffard  1 , Alberto J L Macario, Everly Conway de Macario
Affiliations
Comment

The future of molecular chaperones and beyond

Rona G Giffard et al. J Clin Invest. 2013 Aug.

Abstract

Protection of hair cells by HSP70 released by supporting cells is reported by May et al. in this issue of the JCI. Their findings suggest a new way to reduce ototoxicity from therapeutic medications and raise larger questions about the role and integration of heat shock proteins in non–cell-autonomous responses to stress. Increasing evidence suggests an important role for extracellular heat shock proteins in both the nervous system and the immune system. The work also suggests that defective chaperones could cause ear disease and supports the potential use of chaperone therapeutics.

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Comment on

  • Inner ear supporting cells protect hair cells by secreting HSP70.
    May LA, Kramarenko II, Brandon CS, Voelkel-Johnson C, Roy S, Truong K, Francis SP, Monzack EL, Lee FS, Cunningham LL. May LA, et al. J Clin Invest. 2013 Aug;123(8):3577-87. doi: 10.1172/JCI68480. Epub 2013 Jul 25. J Clin Invest. 2013. PMID: 23863716 Free PMC article.

References

    1. Georgopoulos C, Welch WJ. Role of the major heat shock proteins as molecular chaperones. Ann Rev Cell Biol. 1993;9:601–634. doi: 10.1146/annurev.cb.09.110193.003125. - DOI - PubMed
    1. Lindquist S, Craig EA. The heat-shock proteins. Annu Rev Genet. 1988;22:631–677. doi: 10.1146/annurev.ge.22.120188.003215. - DOI - PubMed
    1. Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci. 2005;62(6):670–684. doi: 10.1007/s00018-004-4464-6. - DOI - PMC - PubMed
    1. Young JC, Agashe VR, Siegers K, Hartl FU. Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol. 2004;5(10):781–791. doi: 10.1038/nrm1492. - DOI - PubMed
    1. Fleshner M, Johnson JD. Endogenous extra-cellular heat shock protein 72: releasing signal(s) and function. Int J Hypertherm. 2005;21(5):457–471. doi: 10.1080/02656730500088211. - DOI - PubMed

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