Heat shock protein 60, via MyD88 innate signaling, protects B cells from apoptosis, spontaneous and induced

J Immunol. 2009 Jul 15;183(2):890-6. doi: 10.4049/jimmunol.0804238. Epub 2009 Jun 26.

Abstract

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-x(L), 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibody Formation
  • Apoptosis Regulatory Proteins / biosynthesis
  • Apoptosis* / drug effects
  • B-Lymphocytes / cytology*
  • B-Lymphocytes / transplantation
  • Caspase Inhibitors
  • Cell Survival
  • Cell Transplantation
  • Chaperonin 60 / physiology*
  • Dexamethasone / pharmacology
  • Immunoglobulin M / immunology
  • Membrane Potential, Mitochondrial
  • Mice
  • Myeloid Differentiation Factor 88 / metabolism*
  • Signal Transduction*
  • Up-Regulation

Substances

  • Apoptosis Regulatory Proteins
  • Caspase Inhibitors
  • Chaperonin 60
  • Immunoglobulin M
  • Myd88 protein, mouse
  • Myeloid Differentiation Factor 88
  • Dexamethasone