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Published online June 26, 2009
The Journal of Immunology, 2009, 183, 890 -896
Copyright © 2009 by The American Association of Immunologists, Inc.
doi:10.4049/jimmunol.0804238
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Heat Shock Protein 60, via MyD88 Innate Signaling, Protects B Cells from Apoptosis, Spontaneous and Induced1

Michal Cohen-Sfady, Meirav Pevsner-Fischer, Raanan Margalit and Irun R. Cohen2

Department of Immunology, The Weizmann Institute of Science, Rehovot, Israel

We recently reported that heat shock protein 60 (HSP60) via TLR4 signaling activates B cells and induces them to proliferate and secrete IL-10. We now report that HSP60 inhibits mouse B cell apoptosis, spontaneous or induced by dexamethasone or anti-IgM activation. Unlike HSP60 enhancement of B cell proliferation and IL-10 secretion, TLR4 signaling was not required for the inhibition of apoptosis by HSP60; nevertheless, MyD88 was essential. Inhibition of apoptosis by HSP60 was associated with up-regulation of the antiapoptotic molecules Bcl-2, Bcl-xL, and survivin, maintenance of the mitochondrial transmembrane potential, and inhibition of caspase-3 activation. Moreover, B cells incubated with HSP60 manifested prolonged survival following transfer into recipient mice. These results extend the varied role of HSP60 in the innate regulation of the adaptive immune response.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 This work was supported by the European Union and by the Center for the Study of Emerging Diseases.

2 Address correspondence and reprint requests to Dr. Irun R. Cohen, Department of Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel. E-mail address: irun.cohen{at}weizmann.ac.il

3 Abbreviations used in this paper: HSP60, heat shock protein 60; DEX, dexamethasone; {Delta}{Psi}m, mitochondrial transmembrane potential.






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